ID 100K_RAT STANDARD; PRT; 889 AA. AC Q62671; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 100 kDa protein (EC 6.3.2.-). OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Testis; RX MEDLINE=92253337; PubMed=1533713; RA Mueller D., Rehbein M., Baumeister H., Richter D.; RT "Molecular characterization of a novel rat protein structurally RT related to poly(A) binding proteins and the 70K protein of the U1 RT small nuclear ribonucleoprotein particle (snRNP)."; RL Nucleic Acids Res. 20:1471-1475(1992). RN [2] RP ERRATUM. RA Mueller D., Rehbein M., Baumeister H., Richter D.; RL Nucleic Acids Res. 20:2624-2624(1992). CC -!- FUNCTION: E3 UBIQUITIN-PROTEIN LIGASE WHICH ACCEPTS UBIQUITIN FROM CC AN E2 UBIQUITIN-CONJUGATING ENZYME IN THE FORM OF A THIOESTER AND CC THEN DIRECTLY TRANSFERS THE UBIQUITIN TO TARGETED SUBSTRATES (BY CC SIMILARITY). THIS PROTEIN MAY BE INVOLVED IN MATURATION AND/OR CC POST-TRANSCRIPTIONAL REGULATION OF MRNA. CC -!- TISSUE SPECIFICITY: HIGHEST LEVELS FOUND IN TESTIS. ALSO PRESENT CC IN LIVER, KIDNEY, LUNG AND BRAIN. CC -!- DEVELOPMENTAL STAGE: IN EARLY POST-NATAL LIFE, EXPRESSION IN CC THE TESTIS INCREASES TO REACH A MAXIMUM AROUND DAY 28. CC -!- MISCELLANEOUS: A CYSTEINE RESIDUE IS REQUIRED FOR CC UBIQUITIN-THIOLESTER FORMATION. CC -!- SIMILARITY: A CENTRAL REGION (AA 485-514) IS SIMILAR TO THE CC C-TERMINAL DOMAINS OF MAMMALIAN AND YEAST POLY (A) RNA BINDING CC PROTEINS (PABP). CC -!- SIMILARITY: CONTAINS MIXED-CHARGE DOMAINS SIMILAR TO RNA-BINDING CC PROTEINS. CC -!- SIMILARITY: CONTAINS 1 HECT-TYPE E3 UBIQUITIN-PROTEIN LIGASE CC DOMAIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64411; CAA45756.1; -. DR InterPro; IPR000569; HECT. DR InterPro; IPR002004; PABP. DR Pfam; PF00632; HECT; 1. DR Pfam; PF00658; PABP; 1. DR SMART; SM00119; HECTc; 1. DR SMART; SM00517; PolyA; 1. DR PROSITE; PS50237; HECT; 1. KW Ubiquitin conjugation; Ligase. FT DOMAIN 77 88 ASP/GLU-RICH (ACIDIC). FT DOMAIN 127 150 PRO-RICH. FT DOMAIN 420 439 ARG/GLU-RICH (MIXED CHARGE). FT DOMAIN 448 457 ARG/ASP-RICH (MIXED CHARGE). FT DOMAIN 485 514 PABP-LIKE. FT DOMAIN 579 590 ASP/GLU-RICH (ACIDIC). FT DOMAIN 786 889 HECT. FT DOMAIN 827 847 PRO-RICH. FT BINDING 858 858 UBIQUITIN (BY SIMILARITY). SQ SEQUENCE 889 AA; 100368 MW; ABD7E3CD53961B78 CRC64; MMSARGDFLN YALSLMRSHN DEHSDVLPVL DVCSLKHVAY VFQALIYWIK AMNQQTTLDT PQLERKRTRE LLELGIDNED SEHENDDDTS QSATLNDKDD ESLPAETGQN HPFFRRSDSM TFLGCIPPNP FEVPLAEAIP LADQPHLLQP NARKEDLFGR PSQGLYSSSA GSGKCLVEVT MDRNCLEVLP TKMSYAANLK NVMNMQNRQK KAGEDQSMLA EEADSSKPGP SAHDVAAQLK SSLLAEIGLT ESEGPPLTSF RPQCSFMGMV ISHDMLLGRW RLSLELFGRV FMEDVGAEPG SILTELGGFE VKESKFRREM EKLRNQQSRD LSLEVDRDRD LLIQQTMRQL NNHFGRRCAT TPMAVHRVKV TFKDEPGEGS GVARSFYTAI AQAFLSNEKL PNLDCIQNAN KGTHTSLMQR LRNRGERDRE REREREMRRS SGLRAGSRRD RDRDFRRQLS IDTRPFRPAS EGNPSDDPDP LPAHRQALGE RLYPRVQAMQ PAFASKITGM LLELSPAQLL LLLASEDSLR ARVEEAMELI VAHGRENGAD SILDLGLLDS SEKVQENRKR HGSSRSVVDM DLDDTDDGDD NAPLFYQPGK RGFYTPRPGK NTEARLNCFR NIGRILGLCL LQNELCPITL NRHVIKVLLG RKVNWHDFAF FDPVMYESLR QLILASQSSD ADAVFSAMDL AFAVDLCKEE GGGQVELIPN GVNIPVTPQN VYEYVRKYAE HRMLVVAEQP LHAMRKGLLD VLPKNSLEDL TAEDFRLLVN GCGEVNVQML ISFTSFNDES GENAEKLLQF KRWFWSIVER MSMTERQDLV YFWTSSPSLP ASEEGFQPMP SITIRPPDDQ HLPTANTCIS RLYVPLYSSK QILKQKLLLA IKTKNFGFV // ID 104K_THEPA STANDARD; PRT; 924 AA. AC P15711; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-AUG-1992 (Rel. 23, Last annotation update) DE 104 kDa microneme-rhoptry antigen. OS Theileria parva. OC Eukaryota; Alveolata; Apicomplexa; Piroplasmida; Theileriidae; OC Theileria. OX NCBI_TaxID=5875; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MUGUGA; RX MEDLINE=90158697; PubMed=1689460; RA Iams K.P., Young J.R., Nene V., Desai J., Webster P., RA Ole-Moiyoi O.K., Musoke A.J.; RT "Characterisation of the gene encoding a 104-kilodalton microneme- RT rhoptry protein of Theileria parva."; RL Mol. Biochem. Parasitol. 39:47-60(1990). CC -!- SUBCELLULAR LOCATION: IN MICRONEME/RHOPTRY COMPLEXES. CC -!- DEVELOPMENTAL STAGE: SPOROZOITE ANTIGEN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M29954; AAA18217.1; -. DR PIR; A44945; A44945. KW Antigen; Sporozoite; Repeat. FT DOMAIN 1 19 HYDROPHOBIC. FT DOMAIN 905 924 HYDROPHOBIC. SQ SEQUENCE 924 AA; 103625 MW; 289B4B554A61870E CRC64; MKFLILLFNI LCLFPVLAAD NHGVGPQGAS GVDPITFDIN SNQTGPAFLT AVEMAGVKYL QVQHGSNVNI HRLVEGNVVI WENASTPLYT GAIVTNNDGP YMAYVEVLGD PNLQFFIKSG DAWVTLSEHE YLAKLQEIRQ AVHIESVFSL NMAFQLENNK YEVETHAKNG ANMVTFIPRN GHICKMVYHK NVRIYKATGN DTVTSVVGFF RGLRLLLINV FSIDDNGMMS NRYFQHVDDK YVPISQKNYE TGIVKLKDYK HAYHPVDLDI KDIDYTMFHL ADATYHEPCF KIIPNTGFCI TKLFDGDQVL YESFNPLIHC INEVHIYDRN NGSIICLHLN YSPPSYKAYL VLKDTGWEAT THPLLEEKIE ELQDQRACEL DVNFISDKDL YVAALTNADL NYTMVTPRPH RDVIRVSDGS EVLWYYEGLD NFLVCAWIYV SDGVASLVHL RIKDRIPANN DIYVLKGDLY WTRITKIQFT QEIKRLVKKS KKKLAPITEE DSDKHDEPPE GPGASGLPPK APGDKEGSEG HKGPSKGSDS SKEGKKPGSG KKPGPAREHK PSKIPTLSKK PSGPKDPKHP RDPKEPRKSK SPRTASPTRR PSPKLPQLSK LPKSTSPRSP PPPTRPSSPE RPEGTKIIKT SKPPSPKPPF DPSFKEKFYD DYSKAASRSK ETKTTVVLDE SFESILKETL PETPGTPFTT PRPVPPKRPR TPESPFEPPK DPDSPSTSPS EFFTPPESKR TRFHETPADT PLPDVTAELF KEPDVTAETK SPDEAMKRPR SPSEYEDTSP GDYPSLPMKR HRLERLRLTT TEMETDPGRM AKDASGKPVK LKRSKSFDDL TTVELAPEPK ASRIVVDDEG TEADDEETHP PEERQKTEVR RRRPPKKPSK SPRPSKPKKP KKPDSAYIPS ILAILVVSLI VGIL // ID 108_LYCES STANDARD; PRT; 102 AA. AC Q43495; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Protein 108 precursor. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. VF36; TISSUE=Anther; RX MEDLINE=94143497; PubMed=8310077; RA Chen R., Smith A.G.; RT "Nucleotide sequence of a stamen- and tapetum-specific gene from RT Lycopersicon esculentum."; RL Plant Physiol. 101:1413-1413(1993). CC -!- TISSUE SPECIFICITY: STAMEN- AND TAPETUM-SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE A9 / FIL1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z14088; CAA78466.1; -. DR Mendel; 8853; LYCes;1133;1. DR InterPro; IPR003612; AAI. DR InterPro; IPR001768; Cereal_tryp_amyl_inh. DR Pfam; PF00234; tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. KW Signal. FT SIGNAL 1 30 POTENTIAL. FT CHAIN 31 102 PROTEIN 108. FT DISULFID 41 77 BY SIMILARITY. FT DISULFID 51 66 BY SIMILARITY. FT DISULFID 67 92 BY SIMILARITY. FT DISULFID 79 99 BY SIMILARITY. SQ SEQUENCE 102 AA; 10576 MW; CFBAA1231C3A5E92 CRC64; MASVKSSSSS SSSSFISLLL LILLVIVLQS QVIECQPQQS CTASLTGLNV CAPFLVPGSP TASTECCNAV QSINHDCMCN TMRIAAQIPA QCNLPPLSCS AN // ID 10KD_VIGUN STANDARD; PRT; 75 AA. AC P18646; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 10 kDa protein precursor (Clone PSAS10). OS Vigna unguiculata (Cowpea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Vigna. OX NCBI_TaxID=3917; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Cotyledon; RX MEDLINE=91355865; PubMed=2103443; RA Ishibashi N., Yamauchi D., Miniamikawa T.; RT "Stored mRNA in cotyledons of Vigna unguiculata seeds: nucleotide RT sequence of cloned cDNA for a stored mRNA and induction of its RT synthesis by precocious germination."; RL Plant Mol. Biol. 15:59-64(1990). CC -!- FUNCTION: THIS PROTEIN IS REQUIRED FOR GERMINATION. CC -!- SIMILARITY: BELONGS TO THE GAMMA-PUROTHIONIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16877; CAA34760.1; -. DR PIR; S11156; S11156. DR HSSP; P45639; 1CHL. DR InterPro; IPR002118; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR ProDom; PD002594; Gamma-thionin; 1. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00940; GAMMA_THIONIN; 1. KW Germination; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 75 10 KDA PROTEIN. FT DISULFID 31 75 BY SIMILARITY. FT DISULFID 42 63 BY SIMILARITY. FT DISULFID 48 69 BY SIMILARITY. FT DISULFID 52 71 BY SIMILARITY. SQ SEQUENCE 75 AA; 8523 MW; 6D72D9D238CF7650 CRC64; MEKKSIAGLC FLFLVLFVAQ EVVVQSEAKT CENLVDTYRG PCFTTGSCDD HCKNKEHLLS GRCRDDVRCW CTRNC // ID 110K_PLAKN STANDARD; PRT; 296 AA. AC P13813; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE 110 kDa antigen (PK110) (Fragment). OS Plasmodium knowlesi. OC Eukaryota; Alveolata; Apicomplexa; Haemosporida; Plasmodium. OX NCBI_TaxID=5850; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88039002; PubMed=2444886; RA Perler F.B., Moon A.M., Qiang B.Q., Meda M., Dalton M., Card C., RA Schmidt-Ullrich R., Wallach D., Lynch J., Donelson J.E.; RT "Cloning and characterization of an abundant Plasmodium knowlesi RT antigen which cross reacts with Gambian sera."; RL Mol. Biochem. Parasitol. 25:185-193(1987). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19152; AAA29471.1; -. DR PIR; A54527; A54527. KW Malaria; Antigen; Repeat. FT NON_TER 1 1 FT DOMAIN 131 296 13.5 X 12 AA TANDEM REPEATS OF E-E-T-Q-K- FT T-V-E-P-E-Q-T. SQ SEQUENCE 296 AA; 34077 MW; B0D7CD175C7A3625 CRC64; FNSNMLRGSV CEEDVSLMTS IDNMIEEIDF YEKEIYKGSH SGGVIKGMDY DLEDDENDED EMTEQMVEEV ADHITQDMID EVAHHVLDNI THDMAHMEEI VHGLSGDVTQ IKEIVQKVNV AVEKVKHIVE TEETQKTVEP EQIEETQNTV EPEQTEETQK TVEPEQTEET QNTVEPEQIE ETQKTVEPEQ TEEAQKTVEP EQTEETQKTV EPEQTEETQK TVEPEQTEET QKTVEPEQTE ETQKTVEPEQ TEETQKTVEP EQTEETQKTV EPEQTEETQN TVEPEPTQET QNTVEP // ID 11S3_HELAN STANDARD; PRT; 493 AA. AC P19084; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 11S globulin seed storage protein G3 precursor (Helianthinin G3). GN HAG3. OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids II; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89232734; PubMed=2469623; RA Vonder Haar R.A., Allen R.D., Cohen E.A., Nessler C.L., Thomas T.L.; RT "Organization of the sunflower 11S storage protein gene family."; RL Gene 74:433-443(1988). CC -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN. CC -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A CC BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A CC DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEIN (GLOBULINS) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28832; AAA33374.1; -. DR PIR; JA0089; JA0089. DR InterPro; IPR000459; Seedstore_11s. DR Pfam; PF00190; Seedstore_11s; 1. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Multigene family; Signal. FT SIGNAL 1 20 FT CHAIN 21 305 ACIDIC CHAIN. FT CHAIN 306 493 BASIC CHAIN. FT DISULFID 103 312 INTERCHAIN (ACIDIC-BASIC) (POTENTIAL). FT DOMAIN 23 35 GLN-RICH. FT DOMAIN 111 127 GLN/GLY-RICH. FT DOMAIN 191 297 GLN-RICH. SQ SEQUENCE 493 AA; 55687 MW; A007B6F99D189AB5 CRC64; MASKATLLLA FTLLFATCIA RHQQRQQQQN QCQLQNIEAL EPIEVIQAEA GVTEIWDAYD QQFQCAWSIL FDTGFNLVAF SCLPTSTPLF WPSSREGVIL PGCRRTYEYS QEQQFSGEGG RRGGGEGTFR TVIRKLENLK EGDVVAIPTG TAHWLHNDGN TELVVVFLDT QNHENQLDEN QRRFFLAGNP QAQAQSQQQQ QRQPRQQSPQ RQRQRQRQGQ GQNAGNIFNG FTPELIAQSF NVDQETAQKL QGQNDQRGHI VNVGQDLQIV RPPQDRRSPR QQQEQATSPR QQQEQQQGRR GGWSNGVEET ICSMKFKVNI DNPSQADFVN PQAGSIANLN SFKFPILEHL RLSVERGELR PNAIQSPHWT INAHNLLYVT EGALRVQIVD NQGNSVFDNE LREGQVVVIP QNFAVIKRAN EQGSRWVSFK TNDNAMIANL AGRVSASAAS PLTLWANRYQ LSREEAQQLK FSQRETVLFA PSFSRGQGIR ASR // ID 11SB_CUCMA STANDARD; PRT; 480 AA. AC P13744; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-NOV-1990 (Rel. 16, Last annotation update) DE 11S globulin beta subunit precursor. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. KUROKAWA AMAKURI NANKIN; RX MEDLINE=88166744; PubMed=2450746; RA Hayashi M., Mori H., Nishimura M., Akazawa T., Hara-Nishimura I.; RT "Nucleotide sequence of cloned cDNA coding for pumpkin 11-S globulin RT beta subunit."; RL Eur. J. Biochem. 172:627-632(1988). RN [2] RP SEQUENCE OF 22-30 AND 297-302. RA Ohmiya M., Hara I., Mastubara H.; RT "Pumpkin (Cucurbita sp.) seed globulin IV. Terminal sequences of the RT acidic and basic peptide chains and identification of a pyroglutamyl RT peptide chain."; RL Plant Cell Physiol. 21:157-167(1980). CC -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN. CC -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A CC BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A CC DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEIN (GLOBULINS) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M36407; AAA33110.1; -. DR PIR; S00366; FWPU1B. DR InterPro; IPR000459; Seedstore_11s. DR Pfam; PF00190; Seedstore_11s; 1. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Signal. FT SIGNAL 1 21 FT CHAIN 22 480 11S GLOBULIN BETA SUBUNIT. FT CHAIN 22 296 GAMMA CHAIN (ACIDIC). FT CHAIN 297 480 DELTA CHAIN (BASIC). FT MOD_RES 22 22 PYRROLIDONE CARBOXYLIC ACID. FT DISULFID 124 303 INTERCHAIN (GAMMA-DELTA) (POTENTIAL). FT CONFLICT 27 27 S -> E (IN REF. 2). FT CONFLICT 30 30 E -> S (IN REF. 2). SQ SEQUENCE 480 AA; 54625 MW; BCD8A83DD1AED93C CRC64; MARSSLFTFL CLAVFINGCL SQIEQQSPWE FQGSEVWQQH RYQSPRACRL ENLRAQDPVR RAEAEAIFTE VWDQDNDEFQ CAGVNMIRHT IRPKGLLLPG FSNAPKLIFV AQGFGIRGIA IPGCAETYQT DLRRSQSAGS AFKDQHQKIR PFREGDLLVV PAGVSHWMYN RGQSDLVLIV FADTRNVANQ IDPYLRKFYL AGRPEQVERG VEEWERSSRK GSSGEKSGNI FSGFADEFLE EAFQIDGGLV RKLKGEDDER DRIVQVDEDF EVLLPEKDEE ERSRGRYIES ESESENGLEE TICTLRLKQN IGRSVRADVF NPRGGRISTA NYHTLPILRQ VRLSAERGVL YSNAMVAPHY TVNSHSVMYA TRGNARVQVV DNFGQSVFDG EVREGQVLMI PQNFVVIKRA SDRGFEWIAF KTNDNAITNL LAGRVSQMRM LPLGVLSNMY RISREEAQRL KYGQQEMRVL SPGRSQGRRE // ID 120K_RICRI STANDARD; PRT; 1300 AA. AC P14914; DT 01-APR-1990 (Rel. 14, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 120 kDa surface-exposed protein. GN P120. OS Rickettsia rickettsii. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=783; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=R; RX MEDLINE=90136087; PubMed=2515418; RA Gilmore R.D. Jr., Joste N., McDonald G.A.; RT "Cloning, expression and sequence analysis of the gene encoding the RT 120 kD surface-exposed protein of Rickettsia rickettsii."; RL Mol. Microbiol. 3:1579-1586(1989). CC -!- FUNCTION: MAJOR STRUCTURAL PROTEIN WHICH MAY PLAY A ROLE AS CC RICKETTSIAL VIRULENCE FACTOR AND/OR IMMUNOGEN DURING INFECTION. CC -!- SUBCELLULAR LOCATION: CELL WALL. THIS BACTERIUM IS COVERED BY A CC S-LAYER WITH HEXAGONAL SYMMETRY. CC -!- MISCELLANEOUS: ITS C-TERMINUS POTENTIALLY MAY BEAR THE EPITOPES CC CONFERRING ANTIGENICITY TO THE PROTEIN. CC -!- SIMILARITY: BELONGS TO THE RICKETTSIAE OMPA/OMPB FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16353; CAA34402.1; -. DR PIR; S07575; S07575. DR InterPro; IPR003858; rOmpA_rOmpB. DR Pfam; PF02708; rOmpA_rOmpB; 1. KW Antigen; Glycoprotein; S-layer. FT CARBOHYD 7 7 N-LINKED (POTENTIAL). FT CARBOHYD 66 66 N-LINKED (POTENTIAL). FT CARBOHYD 86 86 N-LINKED (POTENTIAL). FT CARBOHYD 103 103 N-LINKED (POTENTIAL). FT CARBOHYD 147 147 N-LINKED (POTENTIAL). FT CARBOHYD 268 268 N-LINKED (POTENTIAL). FT CARBOHYD 330 330 N-LINKED (POTENTIAL). FT CARBOHYD 375 375 N-LINKED (POTENTIAL). FT CARBOHYD 415 415 N-LINKED (POTENTIAL). FT CARBOHYD 424 424 N-LINKED (POTENTIAL). FT CARBOHYD 430 430 N-LINKED (POTENTIAL). FT CARBOHYD 436 436 N-LINKED (POTENTIAL). FT CARBOHYD 444 444 N-LINKED (POTENTIAL). FT CARBOHYD 515 515 N-LINKED (POTENTIAL). FT CARBOHYD 547 547 N-LINKED (POTENTIAL). FT CARBOHYD 593 593 N-LINKED (POTENTIAL). FT CARBOHYD 655 655 N-LINKED (POTENTIAL). FT CARBOHYD 698 698 N-LINKED (POTENTIAL). FT CARBOHYD 710 710 N-LINKED (POTENTIAL). FT CARBOHYD 799 799 N-LINKED (POTENTIAL). FT CARBOHYD 800 800 N-LINKED (POTENTIAL). FT CARBOHYD 826 826 N-LINKED (POTENTIAL). FT CARBOHYD 844 844 N-LINKED (POTENTIAL). FT CARBOHYD 861 861 N-LINKED (POTENTIAL). FT CARBOHYD 879 879 N-LINKED (POTENTIAL). FT CARBOHYD 920 920 N-LINKED (POTENTIAL). FT CARBOHYD 926 926 N-LINKED (POTENTIAL). FT CARBOHYD 1116 1116 N-LINKED (POTENTIAL). FT CARBOHYD 1128 1128 N-LINKED (POTENTIAL). FT CARBOHYD 1140 1140 N-LINKED (POTENTIAL). FT CARBOHYD 1146 1146 N-LINKED (POTENTIAL). FT CARBOHYD 1211 1211 N-LINKED (POTENTIAL). SQ SEQUENCE 1300 AA; 132801 MW; E09E52C3F647243D CRC64; MVIQSANATG QVNFRHIVDV GADGTTAFKT AASKVTITQD SNFGNTDFGN LAAQIKVPNA ITLTGNFTGD ASNPGNTAGV ITFDANGTLE SASADANVAV TNNITAIEAS GAGVVQLSGT HAAELRLGNA GSIFKLADGT VINGKVNQTA LVGGALAAGT ITLDGSATIT GDIGNAGGAA ALQRITLAND AKKTLTLGGA NIIGAGGGTI DLQANGGTIK LTSTQNNIVV DFDLAIATDQ TGVVDASSLT NAQTLTINGK IGTIGANNKT LGQFNIGSSK TVLSNGNVAI NELVIGNDGA VQFAHDTYLI TRTTNAAGQG KIIFNPVVNN GTTLAAGTNL GSATNPLAEI NFGSKGVNVD TVLNVGEGVN LYATNITTTD ANVGSFVFNA GGTNIVSGTV GGQQGNKFNT VALENGTTVK FLGNATFNGN TTIAANSTLQ IGGNYTADCV ASADGTGIVE FVNTGPITVT LNKQAAPVNA LKQITVSGPG NVVINEIGNA GNHHGAVTDT IAFENSSLGA VVFLPRGIPF NDAGNTMPLT IKSTVGNKTA KGFDVPSVVV LGVDSVIADG QVIGDQNNIV GLGLGSDNGI IVNATTLYAG ISTLNNNQGT VTLSGGVPNT PGTVYGLGTG IGASKFKQVT FTTDYNNLGN IIATNATIND GVTVTTGGIA GIGFDGKITL GSVNGNGNVR FADGILSNST SMIGTTKANN GTVTYLGNAF VGNIGDSDTP VASVRFTGSD SGAGLQGNIY SQVIDFGTYN LGIVNSNIIL GGGTTAINGK IDLVTNTLTF ASGTSTWGNN TSIETTLTLA NGNIGHIVIL EGAQVNTTTT GTTTIKVQDN ANANFSGTQT YTLIQGGARF NGTLGSPNFA VTGSNRFVNY SLIRAANQDY VITRTNNAEN VVTNDIANSP FGGAPGVDQN VTTFVNATNT AAYNNLLLAK NSANSANFVG AIVTDTSAAI TNVQLDLAKD IQAQLGNRLG ALRYLGTPET AEMAGPEAGA ISAAVAAGDE AIDNVAYGIW AKPFYTDAHQ SKKGGLAGYK AKTTGVVIGL DTLANDNLMI GAAIGITKTD IKHQDYKKGD KTDVNGFSFS LYGAQQLVKN FFAQGSAIFS LNQVKNKSQR YFFDANGNMS KQIAAGHYDN MTFGGNLTVG YDYNAMQGVL VTPMAGLSYL KSSDENYKET GTTVANKQVN SKFSDRTDLI VGAKVAGSTM NRTDLAVYPE VHAFVVHKVT GRLSKTQSVL DGQVTPCINQ PDRTTKTSYN LGLSASIRSD AKMEYGIGYD AQISSKYTAH QGTLKVRVNF // ID 128U_DROME STANDARD; PRT; 368 AA. AC P32234; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE GTP-binding protein 128UP. GN 128UP OR GTP-BP. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OREGON-R; RX MEDLINE=94166747; PubMed=8121394; RA Sommer K.A., Petersen G., Bautz E.K.F.; RT "The gene upstream of DmRP128 codes for a novel GTP-binding protein RT of Drosophila melanogaster."; RL Mol. Gen. Genet. 242:391-398(1994). CC -!- SIMILARITY: BELONGS TO THE GTP1 / OBG FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X71866; CAA50701.1; -. DR PIR; S33467; S33467. DR PIR; S42582; S42582. DR FlyBase; FBgn0010339; 128up. DR InterPro; IPR000765; GTP1_OBG. DR InterPro; IPR004095; TGS. DR Pfam; PF01018; GTP1_OBG; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR PROSITE; PS00905; GTP1_OBG; 1. KW GTP-binding. FT NP_BIND 71 78 GTP (BY SIMILARITY). FT NP_BIND 117 121 GTP (BY SIMILARITY). FT NP_BIND 248 251 GTP (BY SIMILARITY). SQ SEQUENCE 368 AA; 41129 MW; 07C592292BA12A6E CRC64; MITILEKISA IESEMARTQK NKATSAHLGL LKANVAKLRR ELISPKGGGG GTGEAGFEVA KTGDARVGFV GFPSVGKSTL LSNLAGVYSE VAAYEFTTLT TVPGCIKYKG AKIQLLDLPG IIEGAKDGKG RGRQVIAVAR TCNLIFMVLD CLKPLGHKKL LEHELEGFGI RLNKKPPNIY YKRKDKGGIN LNSMVPQSEL DTDLVKTILS EYKIHNADIT LRYDATSDDL IDVIEGNRIY IPCIYLLNKI DQISIEELDV IYKIPHCVPI SAHHHWNFDD LLELMWEYLR LQRIYTKPKG QLPDYNSPVV LHNERTSIED FCNKLHRSIA KEFKYALVWG SSVKHQPQKV GIEHVLNDED VVQIVKKV // ID 12AH_CLOS4 STANDARD; PRT; 29 AA. AC P21215; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-AUG-1991 (Rel. 19, Last annotation update) DE 12-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) (Fragment). OS Clostridium sp. (strain C 48-50). OC Bacteria; Firmicutes; Bacillus/Clostridium group; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=1507; RN [1] RP SEQUENCE. RX MEDLINE=91177018; PubMed=2007406; RA Braun M., Luensdorf H., Bueckmann A.F.; RT "12 alpha-hydroxysteroid dehydrogenase from Clostridium group P, RT strain C 48-50. Production, purification and characterization."; RL Eur. J. Biochem. 196:439-450(1991). CC -!- FUNCTION: CATALYSES THE OXIDATION OF THE 12-ALPHA-HYDROXYL GROUP CC OF BILE ACIDS, BOTH IN THEIR FREE AND CONJUGATED FORM. ALSO ACTS CC ON BILE ALCOHOLS. CC -!- CATALYTIC ACTIVITY: 3-ALPHA,7-ALPHA,12-ALPHA-TRIHYDROXY-5-BETA- CC CHOLANATE + NADP(+) = 3-ALPHA,7-ALPHA-DIHYDROXY-12-OXO-5-BETA- CC CHOLANATE + NADPH. CC -!- SUBUNIT: HOMOTETRAMER. CC -!- MISCELLANEOUS: THE THERMOSTABILITY OF THE ENZYME IS GREATLY CC INCREASED DUE TO NADP BINDING. DR PIR; S14099; S14099. KW Oxidoreductase; NADP. FT NON_TER 29 29 SQ SEQUENCE 29 AA; 2900 MW; A827DB34DB6C8812 CRC64; MIFDGKVAII TGGGKAKSIG YGIAVAYAK // ID 12KD_FRAAN STANDARD; PRT; 111 AA. AC Q05349; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Auxin-repressed 12.5 kDa protein. OS Fragaria ananassa (Strawberry). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Rosales; Rosaceae; Rosoideae; Fragaria. OX NCBI_TaxID=3747; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. OZARK BEAUTY; TISSUE=Flower; RX MEDLINE=91329668; PubMed=2101687; RA Reddy A.S.N., Poovaiah B.W.; RT "Molecular cloning and sequencing of a cDNA for an auxin-repressed RT mRNA: correlation between fruit growth and repression of the RT auxin-regulated gene."; RL Plant Mol. Biol. 14:127-136(1990). CC -!- INDUCTION: REPRESSED BY EXOGENOUS AUXIN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52429; CAA36676.1; -. DR EMBL; L44142; AAA73872.1; -. FT DOMAIN 43 57 PRO/THR-RICH. SQ SEQUENCE 111 AA; 12416 MW; E44CACBADE6F3C51 CRC64; MVLLDKLWDD IVAGPQPERG LGMLRKVPQP LNLKDEGESS KITMPTTPTT PVTPTTPISA RKDNVWRSVF HPGSNLSSKT MGNQVFDSPQ PNSPTVYDWM YSGETRSKHH R // ID 12KD_MYCSM STANDARD; PRT; 24 AA. AC P80438; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE 12 kDa protein (Fragment). OS Mycobacterium smegmatis. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1772; RN [1] RP SEQUENCE. RA Pahl A., Keller U.; RL Submitted (MAR-1995) to the SWISS-PROT data bank. FT NON_TER 24 24 SQ SEQUENCE 24 AA; 2764 MW; 0D19F1F488DB3201 CRC64; MFHVLTLTYL CPLDVVXQTR PAHV // ID 12S1_ARATH STANDARD; PRT; 472 AA. AC P15455; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 12S seed storage protein precursor. GN CRA1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. LANDSBERG ERECTA; RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; RT "Molecular cloning, genome organization, expression and evolution of RT 12S seed storage protein genes of Arabidopsis thaliana."; RL Plant Mol. Biol. 11:805-820(1988). RN [2] RP SEQUENCE OF 420-472 FROM N.A. RC STRAIN=CV. COLUMBIA; RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN. CC -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A CC BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A CC DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEIN (GLOBULINS) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37247; AAA32777.1; -. DR EMBL; X14312; CAA32493.1; -. DR EMBL; Z17590; CAA79005.1; -. DR PIR; S08509; S08509. DR InterPro; IPR000459; Seedstore_11s. DR Pfam; PF00190; Seedstore_11s; 1. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Multigene family; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 282 ACIDIC CHAIN (BY SIMILARITY). FT CHAIN 283 472 BASIC CHAIN (BY SIMILARITY). FT DISULFID 112 289 INTERCHAIN (ALPHA-BETA) (POTENTIAL). SQ SEQUENCE 472 AA; 52624 MW; 89C43E952B0F46F9 CRC64; MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQQPLV IVSVFDLASH QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYETDGE AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA // ID 12S2_ARATH STANDARD; PRT; 455 AA. AC P15456; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 12S seed storage protein precursor. GN CRB. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. LANDSBERG ERECTA; RA Pang P.P., Pruitt R.E., Meyerowitz E.M.; RT "Molecular cloning, genome organization, expression and evolution of RT 12S seed storage protein genes of Arabidopsis thaliana."; RL Plant Mol. Biol. 11:805-820(1988). RN [2] RP SEQUENCE OF 240-360 FROM N.A. RC STRAIN=CV. COLUMBIA; RA Raynal M., Grellet F., Laudie M., Meyer Y., Cooke R., Delseny M.; RL Submitted (OCT-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIS IS A SEED STORAGE PROTEIN. CC -!- SUBUNIT: HEXAMER; EACH SUBUNIT IS COMPOSED OF AN ACIDIC AND A CC BASIC CHAIN DERIVED FROM A SINGLE PRECURSOR AND LINKED BY A CC DISULFIDE BOND. CC -!- SIMILARITY: BELONGS TO THE 11S SEED STORAGE PROTEIN (GLOBULINS) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M37248; AAA32778.1; -. DR EMBL; X14313; CAA32494.1; -. DR EMBL; Z17654; CAA79024.1; -. DR PIR; S08510; S08510. DR InterPro; IPR000459; Seedstore_11s. DR Pfam; PF00190; Seedstore_11s; 1. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. KW Seed storage protein; Multigene family; Signal. FT SIGNAL 1 24 POTENTIAL. FT CHAIN 25 269 ACIDIC CHAIN (BY SIMILARITY). FT CHAIN 270 455 BASIC CHAIN (BY SIMILARITY). FT DISULFID 106 276 INTERCHAIN (ALPHA-BETA) (POTENTIAL). SQ SEQUENCE 455 AA; 50643 MW; A9AC23AAA7F6B538 CRC64; MGRVSSIISF SLTLLILFNG YTAQQWPNEC QLDQLNALEP SQIIKSEGGR IEVWDHHAPQ LRCSGFAFER FVIEPQGLFL PTFLNAGKLT FVVHGRGLMG RVIPGCAETF MESPVFGEGQ GQGQSQGFRD MHQKVEHLRC GDTIATPSGV AQWFYNNGNE PLILVAAADL ASNQNQLDRN LRPFLIAGNN PQGQEWLQGR KQQKQNNIFN GFAPEILAQA FKINVETAQQ LQNQQDNRGN IVKVNGPFGV IRPPLRRGEG GQQPHEIANG LEETLCTMRC TENLDDPSDA DVYKPSLGYI STLNSYNLPI LRLLRLSALR GSIRKNAMVL PQWNVNANAA LYVTNGKAHI QMVNDNGERV FDQEISSGQL LVVPQGFSVM KHRIGEQFEW IEFKTNENAQ VNTLAGRTSV MRGLPLEVIT NGYQISPEEA KRVKFSTIET TLTHSSPMSY GRPRA // ID 1431_ENTHI STANDARD; PRT; 239 AA. AC P42648; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3 protein 1 (14-3-3-1). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13418; AAA80185.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 239 AA; 27338 MW; 6BDE1496C8428FFC CRC64; MASREDCVYT AKLAEQSERY DEMVQCMKQV AEMEAELSIE ERNLLSVAYK NVIGAKRASW RIISSLEQKE QAKGNDKHVE IIKGYRAKIE KELSTCCDDV LKVIQENLLP KASTSESKVF FKKMEGDYYR YFAEFTVDEK RKEVADKSLA AYTEATEISN AELAPTHPIR LGLALNFSVF YFEIMNDADK ACQLAKQAFD DAIAKLDEVP ENMYKDSTLI MQLLRDNLTL WTSDACDEE // ID 1431_LYCES STANDARD; PRT; 249 AA. AC P93206; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 1. GN TFT1. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95900; CAA65145.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 249 AA; 28163 MW; 42701A500DD2DEC3 CRC64; MALPENLTRE QCLYLANVAE QAERYEEMVK FMDKLVIGSG SSELTVEERN LLSVAYKNVI GSLRAAWRIV SSIEQKEEGR KNDEHVVLVK DYRSKVESEL SDVCAGILKI LDQYLIPSAS AGESKVFYLK MKGDYYRYLA EFKVGNERKE AAEDTMLAYK AAQDIAVADV APTHPIRLGL ALNFSVFYYE ILNASEKACS MAKQAFEEAI AELDTMGEES YKDSTLIMQL LRDNLTLWTS DMQEQMDEA // ID 1431_MAIZE STANDARD; PRT; 261 AA. AC P49106; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 14-3-3-like protein GF14-6. GN GRF1. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95148741; PubMed=7846163; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX TO BIND TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S77133; AAB33304.1; -. DR HSSP; P29312; 1A38. DR MaizeDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29662 MW; 25EC70725A5F6801 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ETHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL RDNLTLWTSD ISEDPAEEIR EAPKRDSSEG Q // ID 1431_SCHMA STANDARD; PRT; 252 AA. AC Q26540; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein homolog 1. OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Turbellarian Platyhelminths; OC Rhabditophora; Eulecithophora; Revertospermata; Mediofusata; OC Neodermata; Trematoda; Digenea; Strigeidida; Schistosomatoidea; OC Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=PUERTO RICAN; RX MEDLINE=96123403; PubMed=8577340; RA Schechtman D., Ram D., Tarrab-Hazdai R., Arnon R., Schechter I.; RT "Stage-specific expression of the mRNA encoding a 14-3-3 protein RT during the life cycle of Schistosoma mansoni."; RL Mol. Biochem. Parasitol. 73:275-278(1995). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U24281; AAC46983.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT SIMILAR 133 149 TO THE C-TERMINUS OF ANNEXINS. SQ SEQUENCE 252 AA; 28371 MW; 39103EB5B71A2C08 CRC64; MTTSWVLQSK DLSNTDLVHI AKLAEQAERY DDMAAAMKRY TEASGNLGNE ERNLLSVAYK NVVGARRSAW RVIHGSEMKA VNDRTKKQIA EEYRIKMEKE LNTICNQVLA LLEDYLLPNA SPDDSKVFFL KMQGDYYRYL AEVATDDART EVVQKSLDAY TKATTAAENL PTTHPIRLGL ALNFSVFFYE IQNDAAKACE LAKSAFDSAI AELDQLQDDS YKDSTLIMQL LRDNLTLWAS DQTAEGDVEN DS // ID 1432_ENTHI STANDARD; PRT; 238 AA. AC P42649; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3 protein 2 (14-3-3-2). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13419; AAA80186.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 238 AA; 27579 MW; 5F2F8EA3C3BE4976 CRC64; MTSREDLVYL SKLAEQSERY EEMVQYMKQV AEMGTELSVE ERNLISVAYK NVVGSRRASW RIISSLEQKE QAKGNTQRVE LIKTYRAKIE QELSQKCDDV LKIITEFLLK NSTSIESKVF FKKMEGDYYR YYAEFTVDEK RKEVADKSLA AYQEATDTAA SLVPTHPIRL GLALNFSVFY YQIMNDADKA CQLAKEAFDE AIQKLDEVPE ESYKESTLIM QLLRDNLTLW TSDMGDDE // ID 1432_LYCES STANDARD; PRT; 254 AA. AC P93208; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 2. GN TFT2. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95901; CAA65146.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 254 AA; 28822 MW; 702D7E9A19A6EA23 CRC64; MAREENVYMA NVAEQAERYE EMVQFMEKVS TSLGSEELTV EERNLLSVAY KNVIGARTLA WRIISSIEQK EESRGNEEHV KCIKEYRSKI ESELSDICDG ILKLLDSNLI PSASNGDSKV FYLKMKGDYH RYLAEFKTGA ERKEAAESTL SAYKAAQDIA NTELAPTHPI RLGLALNFSV FYYEILNSPD RACNLAKQAF DEAIAELDTL GEESYKDSTL IMQLLRDNLT LWTSDMQDDG ADEIKETKND NEQQ // ID 1432_MAIZE STANDARD; PRT; 261 AA. AC Q01526; DT 01-JUL-1993 (Rel. 26, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 14-3-3-like protein GF14-12. GN GRF2. OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95148741; PubMed=7846163; RA de Vetten N.C., Ferl R.J.; RT "Two genes encoding GF14 (14-3-3) proteins in Zea mays. Structure, RT expression, and potential regulation by the G-box binding complex."; RL Plant Physiol. 106:1593-1604(1994). RN [2] RP SEQUENCE OF 14-261 FROM N.A. RX MEDLINE=93076113; PubMed=1446170; RA de Vetten N.C., Lu G., Ferl R.J.; RT "A maize protein associated with the G-box binding complex has RT homology to brain regulatory proteins."; RL Plant Cell 4:1295-1307(1992). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX TO BIND TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S77135; -; NOT_ANNOTATED_CDS. DR EMBL; M96856; AAA33505.1; -. DR PIR; JQ1680; JQ1680. DR HSSP; P29312; 1A4O. DR MaizeDB; 65832; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29636 MW; DE7B707538BA1662 CRC64; MASAELSREE NVYMAKLAEQ AERYEEMVEF MEKVAKTVDS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEEGRG NEDRVTLIKD YRGKIETELT KICDGILKLL ESHLVPSSTA PESKVFYLKM KGDYYRYLAE FKTGAERKDA AENTMVAYKA AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACSL AKQAFDEAIS ELDTLSEESY KDSTLIMQLL HDNLTLWTSD ISEDPAEEIR EAPKHDLSEG Q // ID 1432_SCHMA STANDARD; PRT; 214 AA. AC Q26537; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein homolog 2 (14-3-3-2) (Fragment). OS Schistosoma mansoni (Blood fluke). OC Eukaryota; Metazoa; Platyhelminthes; Turbellarian Platyhelminths; OC Rhabditophora; Eulecithophora; Revertospermata; Mediofusata; OC Neodermata; Trematoda; Digenea; Strigeidida; Schistosomatoidea; OC Schistosomatidae; Schistosoma. OX NCBI_TaxID=6183; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NMRI; RA Lee K.W., Thakur A., Karim A.M., Loverde P.T.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L78441; AAB02100.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 214 AA; 24607 MW; 0B98AEF8CBCC7AD3 CRC64; SNNELTNEER NLLSVAYKNV VGARRSSWRV ISSIEQKTEG SERKQQMAKD YREKIEKELK DICHEVLTLL DKFLIPKATT AESKVFYLKM KGDYYRYLAE VATGDERQKV IEESQRAYND AFDIAKNQMQ PTHPIRLGLA LNFSVFYYEI LNAPDRACHL AKQAFDDAIA ELDTLNEDSY KDSTLIMQLL RDNLTLWTSD TGGDDDANAP DEHQ // ID 1433_CAEEL STANDARD; PRT; 248 AA. AC P41932; Q21537; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein 1. GN FTT-1 OR M117.2. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RX MEDLINE=95011616; PubMed=7926802; RA Wang W., Shakes D.C.; RT "Isolation and sequence analysis of a Caenorhabditis elegans cDNA RT which encodes a 14-3-3 homologue."; RL Gene 147:215-218(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Kershaw J.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U05038; AAA61872.1; -. DR EMBL; Z73910; CAA98138.1; -. DR HSSP; P29312; 1A38. DR WormPep; M117.2; CE06200. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 118 118 A -> V (IN REF. 2). SQ SEQUENCE 248 AA; 28162 MW; B9350039628341AF CRC64; MSDTVEELVQ RAKLAEQAER YDDMAAAMKK VTEQGQELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TEGSEKKQQL AKEYRVKVEQ ELNDICQDVL KLLDEFLIVK AGAAESKAFY LKMKGDYYRY LAEVASEDRA AVVEKSQKAY QEALDIAKDK MQPTHPIRLG LALNFSVFYY EILNTPEHAC QLAKQAFDDA IAELDTLNED SYKDSTLIMQ LLRDNLTLWT SDVGAEDQEQ EGNQEAGN // ID 1433_CANAL STANDARD; PRT; 264 AA. AC O42766; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14-3-3 protein homolog. GN BMH1 OR BMH. OS Candida albicans (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5476; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SC5314; RA Cognetti D., Sturtevant J.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF038154; AAB96910.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 264 AA; 29469 MW; 19242B28150838B6 CRC64; MPASREDSVY LAKLAEQAER YEEMVENMKA VASSGQELSV EERNLLSVAY KNVIGARRAS WRIVSSIEQK EEAKGNESQV ALIRDYRAKI EAELSKICED ILSVLSDHLI TSAQTGESKV FYYKMKGDYH RYLAEFAIAV FRKEAADLSL EAYKAASDVA VTELPPTHPI RLGLALNFSV FYYEILNSPD RACHLAKQAF DDAVADLETL SEDSYKDSTL IMQLLRDNLT LWTDLSEAPA ATEEQQQSSQ APAAQPTEGK ADQE // ID 1433_CHLRE STANDARD; PRT; 259 AA. AC P52908; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein. OS Chlamydomonas reinhardtii. OC Eukaryota; Viridiplantae; Chlorophyta; Chlorophyceae; Volvocales; OC Chlamydomonadaceae; Chlamydomonas. OX NCBI_TaxID=3055; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CW15; RX MEDLINE=95359208; PubMed=7632738; RA Lieblich I., Voigt J.; RT "A Chlamydomonas homologue to the 14-3-3 proteins: cDNA and deduced RT amino acid sequence."; RL Biochim. Biophys. Acta 1263:79-85(1995). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20461845; PubMed=11004511; RA Voigt J., Liebich I., Woestemeyer J., Adam K.H., Marquardt O.; RT "Nucleotide sequence, genomic organization and cell-cycle-dependent RT expression of a Chlamydomonas 14-3-3 gene."; RL Biochim. Biophys. Acta 1492:395-405(2000). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X79445; CAA55964.1; -. DR EMBL; Y19105; CAC03467.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 259 AA; 29514 MW; 2FE3D203FC8B27A1 CRC64; MAVDREECVY MAKLAEQAER YDEMVEEMKK VAKLVHDQEL SVEERNLLSV AYKNVIGARR ASWRIISSIE QKEEAKGNEE HVQRIRKYRT VVEEELSKIC ASILQLLDDH LIPTASTGES KVFYLKMKGD YHRYLAEFKT GADRKEAAEH TLLAYKAAQD IALVDLPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAIAELD SLGEESYKDS TLIMQLLRDN LTLWTSDMQD PAAGDDREGA DMKVEDAEP // ID 1433_DICDI STANDARD; PRT; 252 AA. AC P54632; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein. GN FTTB. OS Dictyostelium discoideum (Slime mold). OC Eukaryota; Mycetozoa; Dictyosteliida; Dictyostelium. OX NCBI_TaxID=44689; RN [1] RP SEQUENCE FROM N.A. RA Knetsch M.L.W., Ennis H.L., van Heusden P., Snaar-Jagalska B.E.; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95568; CAA64814.1; -. DR HSSP; P29312; 1A38. DR DictyDb; DD01070; fttB. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 252 AA; 28734 MW; 8A5A966E363E3A9A CRC64; MTREENVYMA KLAEQAERYE EMVETMKKVA ELDVELTVEE RNLLSVAYKN VIGARRASWR IISSIEQKEE SKGNENHVKK IKEYKCKVEK ELTDICNDIL EVLESHLIVS SASGESKVFY YKMKGDYFRY LAEFATGNPR KTSAESSLIA YKAASDIAVT ELPPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKTAFDD AIAELDTLSE DSYKDSTLIM QLLRDNLTLW TSDVHNMEKN QDGDDDQNEP GM // ID 1433_ENTHI STANDARD; PRT; 236 AA. AC P42650; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3 protein 3 (14-3-3-3) (Fragment). OS Entamoeba histolytica. OC Eukaryota; Entamoebidae; Entamoeba. OX NCBI_TaxID=5759; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=HM-1:IMSS; RA Samuelson J., Shen P., Meckler G., Descoteaux S., Fu H., Lohia A.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U13420; AAA80187.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 236 AA; 27055 MW; CC7D9958AD1BB46D CRC64; SEDCVFLSKL AEQSERYDEM VQYMKQVAAL NTELSVEERN LLSVAYKNVI GSRRASWRII TSLEQKEQAK GNDKHVEIIK GYRAKIEDEL AKYCDDVLKV IKENLLPNAS TSESKVFYKK MEGDYYRYYA EFTVDEKRQE VADKSLAAYT EATEISNADL APTHPIRLGL ALNFSVFYYE IMNDADKACQ LAKQAFDDSI AKLDEVPESS YKDSTLIMQL LRDNLTLWTS DTADEE // ID 1433_FUCVE STANDARD; PRT; 251 AA. AC Q39757; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein. OS Fucus vesiculosus. OC Eukaryota; stramenopiles; Phaeophyceae; Fucales; Fucaceae; Fucus. OX NCBI_TaxID=49266; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Frond tips; RA Nicolaus B.H.H.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98886; CAA67389.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; FALSE_NEG. SQ SEQUENCE 251 AA; 28169 MW; 749042151B2684B8 CRC64; MASRDDLVYM AKLAEQAERF DEMVDHMKAV AQQPKELSVE ERNLLSVAYK NVIGSRRASW RVISSIEGKD TVSDQLPLIR DYKSKIETEL TDICADILKI IEAELIPNST SEEGKVFYYK MKGDYHRYLA EFQSADERKT SASDALDAYQ LASDHANQDL PPTHPIRLGL ALNFSVFYYE ILNSPDRACG LAKAAFDDAI AELDTLSEES YKDSTLIIMQ LLRDNLTLWT SDQGEAEEAP GNADGTVVED L // ID 1433_HELAN STANDARD; PRT; 259 AA. AC O65352; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14-3-3-like protein. OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids II; Asterales; Asteraceae; Asteroideae; OC Heliantheae; Helianthus. OX NCBI_TaxID=4232; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. HA300; TISSUE=Pollen; RA Eliasson A., Hammann P., Steinmetz A.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF066076; AAC17447.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 259 AA; 28947 MW; B027B91EE9BE3313 CRC64; MAAASSPREE NVYLAKLAEQ AERYEEMVEF MEKVVAAADG GEELTIEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEGHVSTIR DYRSKIESEL SSICDGILKV LDSKLIGSAS GGDSKVFYLK MKGDYYRYLA EFKTGDERKL AAENTLSAYK AAQDIANAEL APTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI AELDTLGEDS YKDSTLIMQL LRDNLTLWTS DMQDDTAEEV KEAPKPDDQ // ID 1433_LILLO STANDARD; PRT; 259 AA. AC Q9SP07; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein. OS Lilium longiflorum (Trumpet lily). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Liliales; Liliaceae; OC Lilium. OX NCBI_TaxID=4690; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Pollen; RA Pertl H., Himly M., Gehwolf R., Kriechbaumer R., Strasser D., RA Michalke W., Richter K., Ferreira F., Obermeyer G.; RT "A 14-3-3 protein may be involved in regulation of the plasma membrane RT H+ ATPase during pollen grain germination and tube growth of lily RT pollen."; RL Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF191746; AAF05737.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 259 AA; 29253 MW; 392E38B1430B446B CRC64; MSPAEPSREE NVYMAKLAEQ AERYEEMVEF MEKVARTVDT EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEDHVALIKD YRGKIEAELS KICDGILKLL DSHLVPSSTA PESKVFYLKM KGDYHRYLAE FKSGAERKEA AESTLLAYKS AQDIALAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIS ELDTLGEESY KDSTLIMQLL RDNLTLWTSD INEEAGDEIK EASKAVEGQ // ID 1433_LYCES STANDARD; PRT; 260 AA. AC P93209; P42651; DT 01-NOV-1995 (Rel. 32, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 3 (PBLT3). GN TFT3. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 30-260 FROM N.A. RC STRAIN=CV. AILSA CRAIG; TISSUE=Fruit; RX MEDLINE=95359205; PubMed=7632735; RA Laughner B., Lawrence S.D., Ferl R.J.; RT "Two cDNA clones encoding 14-3-3 homologs from tomato fruit."; RL Biochim. Biophys. Acta 1263:67-70(1995). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95902; CAA65147.1; -. DR EMBL; L29151; AAA99430.1; ALT_INIT. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 73 73 I -> V (IN REF. 2). FT CONFLICT 158 158 A -> G (IN REF. 2). SQ SEQUENCE 260 AA; 29304 MW; 2AE0C3E877BBD081 CRC64; MAVVAPTARE ENVYMAKLAD RAESDEEMVE FMEKVSNSLG SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEEHVNSIR EYRSKIENEL SKICDGILKL LDSKLIPSAT SGDSKVFYLK MKGDYHRYLA EFKTGAERKE AAESTLTAYK AAQDIASAEL APTHPIRLGL ALNFSVFYYE ILNSPDRACN LAKQAFDEAI AELDTLGEES YKDSTLIMQL LRDNLTLWTS DMQDDGADEI KEDPKPEEKN // ID 1433_MESCR STANDARD; PRT; 264 AA. AC P93259; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein (G-box binding factor). GN GBF. OS Mesembryanthemum crystallinum (Common ice plant). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllidae; Caryophyllales; Aizoaceae; Mesembryanthemum. OX NCBI_TaxID=3544; RN [1] RP SEQUENCE FROM N.A. RA Michalowski C.B., Quigley-Landreau F., Bohnert H.J.; RL Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U80070; AAB40395.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 264 AA; 29912 MW; E8F2EE8D617435D6 CRC64; MSSESSREEN VYMAKLAEQA ERYEEMVEFM EKVAKMTDTE ELSVEERNLL SVAYKNVIGA RRASWRIISS IEQKEESRGN EDHVSTIKEY RGKIETELSK ICDGILNLLE SHLIPSASTA ESKVFYLKMK GDYHRYLAEF KTGAERKEAA ENTLLAYKSA QDIALAELAP THPIRLGLAL NFSVFYYEIL NSPDRACNLA KQAFDEAISE LDTLGEESYK DSTLIMQLLR DNLTLWTSDN AEEGGDEIKE AAAKRESGEE KPQQ // ID 1433_NEOCA STANDARD; PRT; 266 AA. AC Q25538; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein homolog. OS Neospora caninum. OC Eukaryota; Alveolata; Apicomplexa; Coccidia; Eimeriida; Sarcocystidae; OC Neospora. OX NCBI_TaxID=29176; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NC-1; RX MEDLINE=96258557; PubMed=8992315; RA Lally N.C., Jenkins M.C., Dubey J.P.; RT "Development of a polymerase chain reaction assay for the diagnosis RT of neosporosis using the Neospora caninum 14-3-3 gene."; RL Mol. Biochem. Parasitol. 75:169-178(1996). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U31542; AAC47012.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT DOMAIN 251 254 POLY-GLN. SQ SEQUENCE 266 AA; 30650 MW; 6DA471FE7ECC7C04 CRC64; MAEEIKNLRD EYVYKAKLAE QAERYDEMAE AMKNLVENCL DEQQPKDELS VEERNLLSVA YKNAVGARRA SWRIISSVEQ KELSKQHMQN KALAAEYRQK VEEELNKICH DILQLLTDKL IPKTSDSESK VFYYKMKGDY YRYISEFSGE EGKKQAADQA QESYQKATET AEGHSPATHP IRLGLALNYS VFFYEILNLP QQACEMAKRA FDDAITEFDN VSEDSYKDST LIMQLLRDNL TLWTSDLQAD QQQQEGGEKP AEQADQ // ID 1433_OENHO STANDARD; PRT; 260 AA. AC P29307; DT 01-DEC-1992 (Rel. 24, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1995 (Rel. 32, Last annotation update) DE 14-3-3-like protein. OS Oenothera hookeri (Hooker's evening primrose). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Myrtales; Onagraceae; Oenothera. OX NCBI_TaxID=85636; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92128551; PubMed=1733782; RA Hirsch S., Aitken A., Bertsch U., Soll J.; RT "A plant homologue to mammalian brain 14-3-3 protein and protein RT kinase C inhibitor."; RL FEBS Lett. 296:222-224(1992). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62838; CAA44642.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 260 AA; 29255 MW; A333C405F8416291 CRC64; MATAPSPREE NVYLAKLAEQ AERYEEMVEF MEKVCAAADS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NDDHVSTIRD YRSKIETELS NICGGILKLL DSRLIPSAAS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLSAYKA AQDIANAELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL ANEAFDEAIA ELDTLEEESY KDSTLIMQLL RDNLTLWTSD MQDDGGDEIK EAAPKPDEQY // ID 1433_ORYSA STANDARD; PRT; 260 AA. AC Q06967; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 01-JUN-1994 (Rel. 29, Last annotation update) DE 14-3-3-like protein S94. OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94009718; PubMed=8405471; RA Uchimiya H., Kidou S., Anai T., Umeda M., Aotsuka S., Tsuge T., RA Kato A.; RT "Molecular structure of ras-related small GTP-binding protein genes RT of rice plants and GTPase activities of gene products in Escherichia RT coli."; RL FEBS Lett. 332:282-286(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93144687; PubMed=7678761; RA Kidou S., Umeda M., Kato A., Uchimiya H.; RT "Isolation and characterization of a rice cDNA similar to the bovine RT brain-specific 14-3-3 protein gene."; RL Plant Mol. Biol. 21:191-194(1993). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D16140; BAA03711.1; -. DR PIR; S30927; S30927. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 260 AA; 29129 MW; 47B2BE8006697166 CRC64; MSPAEASREE NVYMAKLAEQ AERYEEMVEF MEKVAKTTDV GELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEAYVASIKE YRSRIETELS KICDGILKLL DSHLVPSATA AESNVFYLKM KGDYHRYLAE FKSGAERKEA AENTLVAYKS AQDIALADLP TTHPIRLGLA LNLSVFYYEI LNSPDRACNL AKQAFDDAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD NAEDGGDEIK EAAKPEGEGH // ID 1433_PEA STANDARD; PRT; 260 AA. AC P46266; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 14-3-3-like protein. OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Pisum. OX NCBI_TaxID=3888; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. ALASKA; RX MEDLINE=95288384; PubMed=7770545; RA Stankovic B., Garic-Stankovic A., Smith C.M., Davies E.; RT "Isolation, sequencing, and analysis of a 14-3-3 brain protein RT homolog from pea (Pisum sativum L.)."; RL Plant Physiol. 107:1481-1482(1995). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U15036; AAA85817.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 260 AA; 29330 MW; 9A5D103E0F87C13A CRC64; MAAAHTPREE NVYMAKLAEQ AERYEEMVEF MEKVSANADS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEDHVAVIRD YRSKIESELS NICDGILKLL DTRLIPSASS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLTGYKS AQDIANAELP PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EAAPKADEQQ // ID 1433_SOLTU STANDARD; PRT; 259 AA. AC Q41418; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. DESIREE; RA Wilczynski G., Szopa J.; RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases. CC -!- TISSUE SPECIFICITY: LEAF-SPECIFIC. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X97724; CAA66309.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 259 AA; 29395 MW; 808C13F2E69498E5 CRC64; MADSREENVY MAKLAEQAER YEEMVEFMEK VAKVDVEELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VSSIKEYRVK IEAELSKICD GILSLLESHL VPSASTAESK VFYLKMKGDY HRYLAEFKTG ARERKEAAEN TLLAYKSAQD IALAELTPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDDAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDTTD DAEDEIREGS KQESGDGQQ // ID 1433_SPIOL STANDARD; PRT; 220 AA. AC P29308; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-DEC-1992 (Rel. 24, Last annotation update) DE 14-3-3-like protein (Fragment). OS Spinacia oleracea (Spinach). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllidae; Caryophyllales; Chenopodiaceae; Spinacia. OX NCBI_TaxID=3562; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92128551; PubMed=1733782; RA Hirsch S., Aitken A., Bertsch U., Soll J.; RT "A plant homologue to mammalian brain 14-3-3 protein and protein RT kinase C inhibitor."; RL FEBS Lett. 296:222-224(1992). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62837; CAA44641.1; -. DR PIR; S20581; S20581. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT NON_TER 1 1 SQ SEQUENCE 220 AA; 24731 MW; E6D91ABC807944DA CRC64; RNLLSVAYKN VVGARRASWR IISSIEQKEE SRGNEDHVSV IRDYRSRIEK ELSDNCDGIL KLLDTKLVPA ASSGDSKVFY LKMKGDYHRY LAEFKTGAQR KEAAESTLTA YKAAQDIANA ELAPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKQAFVE AIAELDTLGE DSYKDSTLIM QLLRDNLTLW TSDMQDEAAD EITEEAAKQQ KAVNNNKIAY // ID 1433_TOBAC STANDARD; PRT; 251 AA. AC Q41246; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. WISCONSIN 38; RX MEDLINE=95093475; PubMed=8000427; RA Chen Z., Fu H., Liu D., Chang P.F., Narasimhan M., Ferl R., RA Hasegawa P.M., Bressan R.A.; RT "A NaCl-regulated plant gene encoding a brain protein homology that RT activates ADP ribosyltransferase and inhibits protein kinase C."; RL Plant J. 6:729-740(1994). CC -!- TISSUE SPECIFICITY: MOST ABUNDANT IN ROOTS AND FLOWERS. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S76737; AAB32832.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 251 AA; 28667 MW; FC010F3FF8674740 CRC64; MDKEREKQVY LARLAEQAER YDEMVEAMKT VAKMDVELTV EERNLVSVGY KNVIGARRAS WRILSSIEQK EESKGHDQNV KRIKTYQQRV EDELTKYALT LSVIDEHVVP SSTSGESTVF YYKMKGDYYR YLAEFKSGDD RKEAADQSLK AYEAATATAS ADLAPTHPIR LGLALNFSVF YYEILNSPER ACHLAKQAFD EAIAELDSLS EESYKDSTLI MQLLRDNFTL WTSDLEEGGE HSKGDERQGE N // ID 1433_TRIHA STANDARD; PRT; 262 AA. AC Q99002; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein homolog (TH1433). OS Trichoderma harzianum. OC Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreales; mitosporic Hypocreales; Trichoderma. OX NCBI_TaxID=5544; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=P1; RX MEDLINE=96257206; PubMed=8675020; RA Klemsdal S.S., Hayes C.K., Hjeljord L., Lorito M., Harman G.E., RA Tronsmo A.; RT "Isolation and characterization of a cDNA from Trichoderma harzianum RT P1 encoding a 14-3-3 protein homolog."; RL Gene 171:123-127(1996). CC -!- DEVELOPMENTAL STAGE: HIGHEST EXPRESSION DURING THE ACTIVE GROWTH CC PERIOD 10-12 HOURS AFTER GERMINATION. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U24158; AAB17101.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. SQ SEQUENCE 262 AA; 29998 MW; 377D1B15E06A2103 CRC64; MGHEDAVYLA KLAEQAERYE EMVENMKIVA SEDRDLTVEE RNLLSVAYKN VIGARRASWR IVTSIEQKEE SKGNSSQVTL IKEYRQKIEN ELAKICDDIL EVLDQHLIPS AKSGESKVFY HKIKGDYHRY LAEFAIGDRR KDSADKSLEA YKAATEVAQT ELPPTHPIRL GLALNFSVFY YEILNAPDQA CHLAKQAFDD AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSSEAETPAR LMPLLRRRPL LRLPSRRRRA QG // ID 1433_XENLA STANDARD; PRT; 235 AA. AC P29309; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-DEC-1992 (Rel. 24, Last annotation update) DE 14-3-3-like protein (Fragment). OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92272745; PubMed=1375463; RA Martens G.J., Piosik P.A., Danrn E.H.J.; RT "Evolutionary conservation of the 14-3-3 protein."; RL Biochem. Biophys. Res. Commun. 184:1456-1469(1992). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86928; AAA49698.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. FT NON_TER 1 1 SQ SEQUENCE 235 AA; 26785 MW; 09928B15D86A3E7A CRC64; AKLSEQAERY DDMAASMKAV TELGAELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT EGNDKRQQMA REYREKVETE LQDICKDVLD LLDRFLVPNA TPPESKVFYL KMKGDYYRYL SEVASGDSKQ ETVASSQQAY QEAFEISKSE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKSAFDEA IRELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGEEADN VEGDN // ID 1434_CAEEL STANDARD; PRT; 248 AA. AC Q20655; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein 2. GN FTT-2 OR F52D10.3. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Kershaw J.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z66564; CAA91474.1; -. DR HSSP; P29312; 1A38. DR WormPep; F52D10.3; CE03389. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 248 AA; 28067 MW; 566D9CF5DB7A4B96 CRC64; MSDGKEELVN RAKLAEQAER YDDMAASMKK VTELGAELSN EERNLLSVAY KNVVGARRSS WRVISSIEQK TEGSEKKQQM AKEYREKVEK ELRDICQDVL NLLDKFLIPK AGAAESKVFY LKMKGDYYRY LAEVASGDDR NSVVEKSQQS YQEAFDIAKD KMQPTHPIRL GLALNFSVFF YEILNAPDKA CQLAKQAFDD AIAELDTLNE DSYKDSTLIM QLLRDNLTLW TSDAATDDTD ANETEGGN // ID 1434_LYCES STANDARD; PRT; 260 AA. AC P42652; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 4 (PBLT4). OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. AILSA CRAIG; TISSUE=Fruit; RX MEDLINE=95359205; PubMed=7632735; RA Laughner B., Lawrence S.D., Ferl R.J.; RT "Two cDNA clones encoding 14-3-3 homologs from tomato fruit."; RL Biochim. Biophys. Acta 1263:67-70(1995). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L29150; AAA99431.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 260 AA; 29298 MW; 955E5BE81765CBB9 CRC64; MADSSREENV YLAKLAEQAE RYEEMIEFME KVAKTADVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVNTIKEYR SKIEADLSKI CDGILSLLES NLIPSASTAE SKVFHLKMKG DYHRYLAEFK TGTERKEAAE NTLLAYKSAQ DIALAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAISEL DTLGEESYKD STLIMQLLRD NLTLWTSDNA DDVGDDIKEA SKPESGEGQQ // ID 1434_SOLTU STANDARD; PRT; 254 AA. AC Q43643; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein RA215. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. DESIREE; TISSUE=Root; RA Wilczynski G., Szopa J.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X87370; CAA60800.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 254 AA; 28595 MW; 5C52EC19BE1D742E CRC64; MASPREENVY MANVAARAER YEEMVEFMEK VVAALDTELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VASIKKYRSQ IENELTSICN GILKLLDSKL IGSAATGDSK VFYLKMKGDY YRYLAEFKTG TERKEAAENT LSAYKSAQDI ANGELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIADVDT LGEESYKDST LIMQLLRDNL TLWTSDMQDD GADEIKEPSK ADNE // ID 1435_LYCES STANDARD; PRT; 255 AA. AC P93210; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 5. GN TFT5. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95903; CAA65148.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 255 AA; 28754 MW; 5E6AA7BEF0B9FE93 CRC64; MASPREENVY MANVADEAER YEEMVEFMEK VVAALNGEEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNED HVASIKKYRS QIENELTSIC NGILKLLDSK LIGSAATGDS KVFYLKMKGD YYRYLAEFKT GTERKEAAEN TLSAYKSAQD IANGELAPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDEAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDMQD DGTDEIKEPS KADNE // ID 1435_SOLTU STANDARD; PRT; 258 AA. AC P93784; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 16R. OS Solanum tuberosum (Potato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4113; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. DESIREE; TISSUE=Root; RA Wilczynski G., Szopa J.; RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11685; CAA72381.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 258 AA; 28936 MW; 1F3B3FD3F3F109D0 CRC64; MASPREENVY MAKLAEQAER YEEMVEFMEK VVAAADGAEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVASIKEYR SKIESELTSI CNGILKLLDS KLIGSAATGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSAYKAAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDMQ DDGTDEIKEA APKPDNNE // ID 1436_LYCES STANDARD; PRT; 258 AA. AC P93211; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 6. GN TFT6. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95904; CAA65149.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; FALSE_NEG. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 258 AA; 29007 MW; 15AE104114EBFA78 CRC64; MAFAREENVY MANVAEQRRS YEEMVEFMEK VVAAADGAEE LTVEERILLS VAYKNVMGAR RASWRIISSI EQKEESRGNE DHVASIKEYR SKIESELTSI CNGILKLLDS KLIGSAATGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSAYKAAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTSWTSDMQ DDGTDEIKEA TPKPDDNE // ID 1437_LYCES STANDARD; PRT; 129 AA. AC P93212; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 7 (Fragment). GN TFT7. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95905; -; NOT_ANNOTATED_CDS. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; PARTIAL. KW Multigene family. FT NON_TER 129 129 SQ SEQUENCE 129 AA; 14975 MW; C9D6BCDED90DEA7E CRC64; MEKEREKQVY LARLAEQAHT YDEMVEAMKA IAKMDVELTV EERNLVSVGY NNVIGATRAS WRILSSIEQK EESKGHEQNV KRIKTYRQRV EDELTKYAAY ILSVIDELLV PSSTTGESIV FYYKMKGDY // ID 1438_LYCES STANDARD; PRT; 131 AA. AC P93213; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 8 (Fragment). GN TFT8. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98864; CAA67372.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; PARTIAL. KW Multigene family. FT NON_TER 131 131 SQ SEQUENCE 131 AA; 15048 MW; DD3E8E086334913A CRC64; MASSKERESL VYIARLAEQR ERYDEMVDAM KNVANLDVEL TVEERNLLSV GYKNVVGSRR ASWRILSSIE QKEDASGNEQ NVKRIQGYRQ KVESELTDIC NNIMTVIDEH LIPSCTAGES TVFYYKMKGD Y // ID 1439_LYCES STANDARD; PRT; 131 AA. AC P93214; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 9 (Fragment). GN TFT9. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98865; CAA67373.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; PARTIAL. KW Multigene family. FT NON_TER 131 131 SQ SEQUENCE 131 AA; 15099 MW; 1ABF23DC97DAE2D9 CRC64; MASSKERENF VYVAKLAEQA ERYDEMVEAM KNVANMDVEL TVEERNLLSV GYKNVVGSRR ASWRILSSIE QKEESRGNEQ NVKRIKEYLQ KVESELTNIC NDIMVVIDQH LIPSCSAGES TVFYHKMKGD Y // ID 143A_HORVU STANDARD; PRT; 262 AA. AC P29305; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein A (14-3-3A). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. PALLAS; TISSUE=Leaf; RX MEDLINE=93258422; PubMed=1302634; RA Brandt J.M., Thordal-Christensen H., Vad K., Gregersen P.L., RA Collinge D.B.; RT "A pathogen-induced gene of barley encodes a protein showing high RT similarity to a protein kinase regulator."; RL Plant J. 2:815-820(1992). CC -!- INDUCTION: IN RESPONSE TO PENETRATION ATTEMPTS OF POWDERY MILDEW CC FUNGI. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X62388; CAA44259.1; -. DR PIR; S18911; S18911. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 262 AA; 29352 MW; DAE722EA5D416DAA CRC64; MSTAEATREE NVYMAKLAEQ AERYEEMVEF MEKVAKTADV GELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEAYVASIKE YRTRIETELS KICDGILKLL DSHLVPSATA AESKVFYLKM KGDYHRYLAE FKAGAERKEA AENTLVAYKS AQDIALADLP TTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDSLGEESY KDSTLIMQLL RDNLTLWTSD NAEEGGDEIK EAASKPEGEG HS // ID 143A_LYCES STANDARD; PRT; 138 AA. AC P93207; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein 10 (Fragment). GN TFT10. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. MONEYMAKER; TISSUE=Leaf; RA Roberts M.R., Bowles D.J.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X98866; CAA67374.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; PARTIAL. KW Multigene family. FT NON_TER 138 138 SQ SEQUENCE 138 AA; 15727 MW; 11380CB8379F6D54 CRC64; MAALIPENLS REQCLYLAKL AEQAERYEEM VQFMDKLVLN STPADDLTVE ERNLLSVAYK NVIGSLRAAW RIVSSIEQKE ESRKNEEHVH LVKEYRGKVE NELSQVCAGI LKLLESNLVP SATTSESKVF HLKMKGDY // ID 143A_SOYBN STANDARD; PRT; 257 AA. AC Q96450; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein A (SGF14A). GN GF14A. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. WILLIAMS; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70533; AAB09580.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 257 AA; 29048 MW; 76DB93EC9828F430 CRC64; MSDSSREENV YMAKLADEAE RYEEMVEFME KVAKTVEVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVAIIKEYR GKIEAELSKI CDGILNLLES NLIPSAASPE SKVFYLKMKG DYHRYLAEFK TGAERKEAAE STLLAYKSAQ DIALADLAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAISEL DTLGEESYKD STLIMQLLRD NLTLWTSDIT DIAGDEIKET SKQQPGE // ID 143A_TOBAC STANDARD; PRT; 255 AA. AC P93342; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein A. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. BRIGHT YELLOW 2; RA Shen W.H., Gigot C.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11212; CAA72095.1; -. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 255 AA; 28660 MW; 29F95F841B418C72 CRC64; MASPREENVY LAKLAEQAER YEEMVEFMEK VVGAGDDELT IEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VASIKTYRSK IESELTSICN GILKLLDSKL IGTAATGDSK VFYLKMKGDY YRYLAEFKTG AERKEAAENT LSAYKSAQDI ANGELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIAELGT LGEESYKDST LIMQLFCDNL TLWTSDMQDD GTDEIKEPSK AEEQQ // ID 143A_VICFA STANDARD; PRT; 261 AA. AC P42653; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein A (VFA-1433A). OS Vicia faba (Broad bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Vicia. OX NCBI_TaxID=3906; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Cotyledon; RA Saalbach G., Christov V., Schwerdel M.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z48504; CAA88415.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29420 MW; EE41151B7679570F CRC64; MATAPTPREE FVYMAKLAEQ AERYEEMVEF MEKVTAAVES EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NDEHVSVIRD YRSKIETELS NICNGILKLL DSRLIPSAAL GDSKVFYLKM KGDYHRYLAE FKSGAERKDA AESTLTAYKS AQDIANTELP PTHPIRLGLA LNFSVFYYEI LNSPDRACGL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EAAPKGNDEP Q // ID 143B_BOVIN STANDARD; PRT; 245 AA. AC P29358; DT 01-DEC-1992 (Rel. 24, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1) DE (KCIP-1). GN YWHAB. OS Bos taurus (Bovine), and OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913, 9940; RN [1] RP SEQUENCE. RC SPECIES=Bovine; RX MEDLINE=91108808; PubMed=1671102; RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., RA Takahashi Y.; RT "Distinct forms of the protein kinase-dependent activator of tyrosine RT and tryptophan hydroxylases."; RL J. Mol. Biol. 217:125-132(1991). RN [2] RP SEQUENCE OF 2-145 FROM N.A. RC SPECIES=Bovine; TISSUE=Retina; RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 2-83; 121-186 AND 199-241. RC SPECIES=Sheep; TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). RN [4] RP SEQUENCE OF 2-23. RC SPECIES=Sheep; TISSUE=Brain; RX MEDLINE=90345949; PubMed=2143472; RA Toker A., Ellis C.A., Sellers L.A., Aitken A.; RT "Protein kinase C inhibitor proteins. Purification from sheep brain RT and sequence similarity to lipocortins and 14-3-3 protein."; RL Eur. J. Biochem. 191:421-429(1990). RN [5] RP PHOSPHORYLATION. RC SPECIES=Sheep; RX MEDLINE=95197587; PubMed=7890696; RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.; RT "14-3-3 alpha and delta are the phosphorylated forms of RT raf-activating 14-3-3 beta and zeta. In vivo stoichiometric RT phosphorylation in brain at a Ser-Pro-Glu-Lys motif."; RL J. Biol. Chem. 270:5706-5709(1995). RN [6] RP POST-TRANSLATIONAL MODIFICATIONS. RC SPECIES=Sheep; RA Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J., RA Howell S.; RT "Electrospray mass spectroscopy analysis with online trapping of RT posttranslationally modified mammalian and avian brain 14-3-3 RT isoforms."; RL J. Protein Chem. 13:463-465(1994). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE CC INITIATION. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING CC PHOSPHORYLATED. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF043736; AAC02090.1; -. DR PIR; S13467; S13467. DR PIR; S10804; S10804. DR PIR; S23179; S23179. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family; KW Alternative initiation. FT INIT_MET 0 0 FT CHAIN 1 245 14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM. FT CHAIN 2 245 14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM. FT INIT_MET 2 2 FOR SHORT ISOFORM. FT MOD_RES 1 1 ACETYLATION. FT MOD_RES 2 2 ACETYLATION (IN SHORT ISOFORM). FT MOD_RES 185 185 PHOSPHORYLATION. SQ SEQUENCE 245 AA; 27950 MW; AA91C2314D99549F CRC64; TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICNDVLQ LLDKYLIPNA TQPESKVFYL KMKGDYFRYL SEVASGDNKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA GEGEN // ID 143B_HORVU STANDARD; PRT; 262 AA. AC Q43470; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein B (14-3-3B). OS Hordeum vulgare (Barley). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; Pooideae; OC Triticeae; Hordeum. OX NCBI_TaxID=4513; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. PALLAS; TISSUE=Leaf; RA Thordal-Christensen H., Brandt J.M., Collinge D.B.; RL Submitted (NOV-1995) to the EMBL/GenBank/DDBJ databases. CC -!- INDUCTION: IN RESPONSE TO PENETRATION ATTEMPTS OF POWDERY MILDEW CC FUNGI. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X93170; CAA63658.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 262 AA; 29691 MW; 00D4A898110EA35F CRC64; MAQPAELSRE ENVYMAKLAE QAERYEEMVE FMEKVAKTVD SEELTVEERN LLSVAYKNVI GARRASWRII SSIEQKEESR GNEDRVTLIK DYRGKIEVEL TKICDGILKL LDSHLVPSST APESKVFYLK MKGDYYRYLA EFKSGTERKD AAENTMVAYK AAQEIALAEL PPTHPIRLGL ALNFSVFYYE ILNSPDRACD LAKQAFDEAI SELDSLSEES YKDSTLIMQL LRDNLTLWTS DISEDAAEEM KDAPKGESGD GQ // ID 143B_HUMAN STANDARD; PRT; 245 AA. AC P31946; DT 01-JUL-1993 (Rel. 26, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1) DE (KCIP-1) (Protein 1054). GN YWHAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Keratinocytes; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP SEQUENCE FROM N.A. RA Clark G.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Skin; RA Strausberg R.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE CC INITIATION (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING CC PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57346; CAA40621.1; -. DR EMBL; AL008725; CAA15497.1; -. DR EMBL; BC001359; AAH01359.1; -. DR HSSP; P29312; 1A38. DR MIM; 601289; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family; KW Alternative initiation. FT INIT_MET 0 0 BY SIMILARITY. FT CHAIN 1 245 14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM. FT CHAIN 2 245 14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM. FT INIT_MET 2 2 FOR SHORT ISOFORM (BY SIMILARITY). FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 2 2 ACETYLATION (IN SHORT ISOFORM) FT (BY SIMILARITY). FT MOD_RES 185 185 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 245 AA; 27951 MW; 0BCA59BF97595485 CRC64; TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICNDVLE LLDKYLIPNA TQPESKVFYL KMKGDYFRYL SEVASGDNKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA GEGEN // ID 143B_MOUSE STANDARD; PRT; 245 AA. AC Q9CQV8; O70455; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1) DE (KCIP-1). GN YWHAB. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=C57BL/6J; TISSUE=Embryo, Kidney, and Liver; RX MEDLINE=21085660; PubMed=11217851; RA Kawai J., Shinagawa A., Shibata K., Yoshino M., Itoh M., Ishii Y., RA Arakawa T., Hara A., Fukunishi Y., Konno H., Adachi J., Fukuda S., RA Aizawa K., Izawa M., Nishi K., Kiyosawa H., Kondo S., Yamanaka I., RA Saito T., Okazaki Y., Gojobori T., Bono H., Kasukawa T., Saito R., RA Kadota K., Matsuda H.A., Ashburner M., Batalov S., Casavant T., RA Fleischmann W., Gaasterland T., Gissi C., King B., Kochiwa H., RA Kuehl P., Lewis S., Matsuo Y., Nikaido I., Pesole G., Quackenbush J., RA Schriml L.M., Staubli F., Suzuki R., Tomita M., Wagner L., Washio T., RA Sakai K., Okido T., Furuno M., Aono H., Baldarelli R., Barsh G., RA Blake J., Boffelli D., Bojunga N., Carninci P., de Bonaldo M.F., RA Brownstein M.J., Bult C., Fletcher C., Fujita M., Gariboldi M., RA Gustincich S., Hill D., Hofmann M., Hume D.A., Kamiya M., Lee N.H., RA Lyons P., Marchionni L., Mashima J., Mazzarelli J., Mombaerts P., RA Nordone P., Ring B., Ringwald M., Rodriguez I., Sakamoto N., RA Sasaki H., Sato K., Schoenbach C., Seya T., Shibata Y., Storch K.-F., RA Suzuki H., Toyo-oka K., Wang K.H., Weitz C., Whittaker C., Wilming L., RA Wynshaw-Boris A., Yoshida K., Hasegawa Y., Kawaji H., Kohtsuki S., RA Hayashizaki Y.; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES (BY SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE CC INITIATION (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING CC PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF058797; AAC14343.1; -. DR EMBL; AK011389; BAB27587.1; -. DR EMBL; AK002632; BAB22246.1; -. DR EMBL; AK004872; BAB23631.1; -. DR HSSP; P29312; 1A38. DR MGD; MGI:1891917; Ywhab. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family; KW Alternative initiation. FT INIT_MET 0 0 BY SIMILARITY. FT CHAIN 1 245 14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM. FT CHAIN 2 245 14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM. FT INIT_MET 2 2 FOR SHORT ISOFORM (BY SIMILARITY). FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 2 2 ACETYLATION (IN SHORT ISOFORM) FT (BY SIMILARITY). FT MOD_RES 185 185 PHOSPHORYLATION (BY SIMILARITY). FT CONFLICT 9 9 Q -> H (IN REF. 1). FT CONFLICT 73 73 N -> D (IN REF. 1). SQ SEQUENCE 245 AA; 27955 MW; 31E896ED85AC5A7F CRC64; TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICNDVLE LLDKYLILNA TQAESKVFYL KMKGDYFRYL SEVASGENKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA GEGEN // ID 143B_RAT STANDARD; PRT; 245 AA. AC P35213; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 14-3-3 protein beta/alpha (Protein kinase C inhibitor protein-1) DE (KCIP-1) (Prepronerve growth factor RNH-1). GN YWHAB. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Brain; RX MEDLINE=93164855; PubMed=8381897; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H.; RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 RT protein and developmental changes in expression of their mRNAs in the RT nervous system."; RL Brain Res. Mol. Brain Res. 17:135-146(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=96318520; PubMed=8749325; RA Takai R., Tanaka E., Miyazaki T., Suda M., Tashiro F.; RT "Function of RNH-1/14-3-3 beta gene in cellular differentiation and RT proliferation."; RL J. Biochem. 118:1045-1053(1995). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: TWO FORMS ARE PRODUCED BY ALTERNATIVE CC INITIATION (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM ALPHA DIFFERS FROM ISOFORM BETA IN BEING CC PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D17446; BAA04260.1; -. DR EMBL; S55223; AAA13843.1; -. DR EMBL; S83440; AAB50874.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT INIT_MET 0 0 BY SIMILARITY. FT CHAIN 1 245 14-3-3 PROTEIN BETA/ALPHA, LONG ISOFORM. FT CHAIN 2 245 14-3-3 PROTEIN BETA/ALPHA, SHORT ISOFORM. FT INIT_MET 2 2 FOR SHORT ISOFORM (BY SIMILARITY). FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 2 2 ACETYLATION (IN SHORT ISOFORM) FT (BY SIMILARITY). FT MOD_RES 185 185 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 245 AA; 27923 MW; D64821F2183048D1 CRC64; TMDKSELVQK AKLAEQAERY DDMAAAMKAV TEQGHELSNE ERNLLSVAYK NVVGARRSSW RVISSIEQKT ERNEKKQQMG KEYREKIEAE LQDICSDVLE LLDKYLILNA THAESKVFYL KMKGDYFRYL SEVASGDNKQ TTVSNSQQAY QEAFEISKKE MQPTHPIRLG LALNFSVFYY EILNSPEKAC SLAKTAFDEA IAELDTLNEE SYKDSTLIMQ LLRDNLTLWT SENQGDEGDA GEGEN // ID 143B_SOYBN STANDARD; PRT; 247 AA. AC Q96451; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein B (SGF14B) (Fragment). GN GF14B. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. WILLIAMS; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70534; AAB09581.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 247 AA; 27921 MW; 9EDFBB4B4F61C468 CRC64; AEGLNREQYV YLANVSEQAE RYEEMVEFMQ KVVVGSTPAS ELTVEERNLL SVAYKNVIGS LRAAWRIVSS IEQKEEGRKN DDHVSLVKHY RSKVENELTQ VCATILSLLD SNLVPSASAS ESKVFYLKMK GDYHRYLAEF KVGDERKTAT EDTMLSYKAA QDIASADLPP THPIRLGLAL NFSVFYYEIL NQSDKACAMA KQAFEEAIAE LDTLGEESYK DSTLIMQLLR DNLTLWTSDV QDQLDEP // ID 143B_TOBAC STANDARD; PRT; 255 AA. AC O49995; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein B. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98105599; PubMed=9443388; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U91723; AAC49891.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 255 AA; 28827 MW; 65CE3CD2FD83DF1E CRC64; MAREENVYMA KLAEQAERYE EMVSFMEKVS TSLGTSEELT VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESRGNEDH VKCIQEYRSK IESELSNICD GILKLLDSCL IPSASAGDSK VFYLKMKGDY HRYLAEFKTG AERKEAAEST LSAYKAAQDI ANAELAPTHP IRLGLALNFS VFYYEILNSP DRACNLAKQA FDEAIAELDT LGEESYKDST LIMQLLRDNL TLWTSDMQDD GADEIKETKT DNEQQ // ID 143B_VICFA STANDARD; PRT; 261 AA. AC P42654; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3-like protein B (VFA-1433B). OS Vicia faba (Broad bean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Vicia. OX NCBI_TaxID=3906; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Cotyledon; RA Saalbach G., Christov V., Schwerdel M.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z48505; CAA88416.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29524 MW; 2981BA7AE4C7E314 CRC64; MASTKDRENF VYIAKLAEQA ERYEEMVDSM KNVANLDVEL TIEERNLLSV GYKNVIGARR ASWRILSSIE QKEESKGNDV NAKRIKEYRH KVETELSNIC IDVMRVIDEH LIPSAAAGES TVFYYKMKGD YYRYLAEFKT GNEKKEAGDQ SMKAYESATT AAEAELPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDIPE DGEDSQKANG TAKFGGGDDA E // ID 143C_ARATH STANDARD; PRT; 267 AA. AC P42643; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 chi (General regulatory factor 1). GN GRF1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95062733; PubMed=7972511; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP REVISIONS TO N-TERMINUS. RC STRAIN=CV. COLUMBIA; RA Ferl R.J., Lu G.; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95175611; PubMed=7870824; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09112; AAA96323.1; -. DR EMBL; U09377; AAA96254.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 267 AA; 29901 MW; 328FA53189EB0290 CRC64; MATPGASSAR DEFVYMAKLA EQAERYEEMV EFMEKVAKAV DKDELTVEER NLLSVAYKNV IGARRASWRI ISSIEQKEES RGNDDHVSLI RDYRSKIETE LSDICDGILK LLDTILVPAA ASGDSKVFYL KMKGDYHRYL AEFKSGQERK DAAEHTLTAY KAAQDIANSE LAPTHPIRLG LALNFSVFYY EILNSPDRAC NLAKQAFDEA IAELDTLGEE SYKDSTLIMQ LLRDNLTLWA SDMQDDVADD IKEAAPAAAK PADEQQS // ID 143C_SOYBN STANDARD; PRT; 258 AA. AC Q96452; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein C (SGF14C). GN GF14C. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. WILLIAMS; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70535; AAB09582.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 258 AA; 29208 MW; 6663BFC6E6992E5F CRC64; MASTKERENF VYVAKLAEQA ERYEEMVEAM KNVANLNVEL TVEERNLLSV GYKNVVGARR ASWRILSSIE QKEEAKGNDV SVKRIKEYRL KVESELSNIC SDIMTVIDEY LIPSSSSGEP SVFFYKMKGD YYRYLAEFKS GDERKEAADH SMKAYQLAST TAEAELASTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLSEESYKDS TLIMQLLRDN LTLWTSDIPE DGEEQKVDSA RADGGDDA // ID 143C_TOBAC STANDARD; PRT; 260 AA. AC P93343; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein C (14-3-3-like protein B). OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. BRIGHT YELLOW 2; RA Shen W.H., Gigot C.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=98105599; PubMed=9443388; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Y11211; CAA72094.1; -. DR EMBL; U91724; AAC49892.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 260 AA; 29364 MW; BDCA77561ED45758 CRC64; MAVAPTAREE NVYMAKLAEQ AERYEEMVEF MEKVSNSLGS EELTVEERNL LSVAYKNVIG ARRASWRIIS SIEQKEESRG NEEHVNSIRE YRSKIENELS KICDGILKLL DAKLIPSAAS GDSKVFYLKM KGDYHRYLAE FKTGAERKEA AESTLTAYKA AQDIATTELA PTHPIRLGLA LNFSVFYYEI LNSPDRACNL AKQAFDEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQDDGADEIK EDPKPDEAKN // ID 143D_SOYBN STANDARD; PRT; 261 AA. AC Q96453; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3-like protein D (SGF14D). GN GF14D. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. WILLIAMS; RA Ryu G.R., Yoo C.M., Jeong H.J., Hong J.C.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U70536; AAB09583.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 261 AA; 29518 MW; F54DF5F5F0E0659B CRC64; MTASKDRENF VYIAKLAEQA ERYEEMVESM KNVANLDVEL TVEERNLLSV GYKNVIGARR ASWRILSSIE QKEETKGNEL NAKRIKEYRQ KVELELSNIC NDVMRVIDEH LIPSAAAGES TVFYYKMKGD YYRYLAEFKS GNEKKEAADQ SMKAYESATA AAEADLPPTH PIRLGLALNF SVFYYEILNS PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDIPE DGEDAQKVNG TAKLGGGEDA E // ID 143D_TOBAC STANDARD; PRT; 249 AA. AC O49996; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein D. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98105599; PubMed=9443388; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U91725; AAC49893.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 249 AA; 28257 MW; 383ECB97BBF1BBF2 CRC64; MAVPENLTRE QCLYLAKLAE QAERYEEMVK FMDRLVAVSA SSELTVEERN LLSVAYKNVI GSLRAAWRIV SSIEQKEEGR KNEEHVVLVK DYRSKVESEL SDVCAGILKI LDQYLIPSAA AGESKVFYLK MKGDYYRYLA EFKVGNERKE AAEDTMLAYK AAQDIALAEL APTHPIRLGL ALNYSVFYYE ILNASEKACS MAKQAFEEAI AELDTLGEES YKDSTLIMQL LRDNLTLWTS DMQEQMDEA // ID 143E_ARATH STANDARD; PRT; 254 AA. AC P48347; DT 01-FEB-1996 (Rel. 33, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 epsilon (General regulatory factor 10). GN GRF10. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (In) Plant Gene Register PGR99-114. CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36446; AAA79699.1; -. DR EMBL; AF145302; AAD51785.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 254 AA; 28915 MW; 037405C341845C25 CRC64; MENEREKQVY LAKLSEQTER YDEMVEAMKK VAQLDVELTV EERNLVSVGY KNVIGARRAS WRILSSIEQK EESKGNDENV KRLKNYRKRV EDELAKVCND ILSVIDKHLI PSSNAVESTV FFYKMKGDYY RYLAEFSSGA ERKEAADQSL EAYKAAVAAA ENGLAPTHPV RLGLALNFSV FYYEILNSPE SACQLAKQAF DDAIAELDSL NEESYKDSTL IMQLLRDNLT LWTSDLNEEG DERTKGADEP QDEN // ID 143E_DROME STANDARD; PRT; 260 AA. AC P92177; Q9VEA8; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein epsilon (Suppressor of RAS1 3-9). GN 14-3-3-EPSILON OR 14-3-3E OR SR3-9 OR CG8045. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND MUTAGENESIS OF GLU-183; PHE-199 AND TYR-214. RX MEDLINE=97302963; PubMed=9159394; RA Chang H.C., Rubin G.M.; RT "14-3-3 epsilon positively regulates Ras-mediated signaling in RT Drosophila."; RL Genes Dev. 11:1132-1139(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: POSITIVELY REGULATES RAS-MEDIATED PATHWAYS. ACTS CC DOWNSTREAM OR PARALLEL TO RAF, BUT UPSTREAM OF NUCLEAR FACTORS IN CC RAS SIGNALING. THREE MUTANTS HAVE BEEN ISOLATED, THAT SUPPRESS THE CC ROUGH EYE PHENOTYPE CAUSED BY MUTATED RAS1 (SEV-RAS1 V12). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U84898; AAC47520.1; -. DR EMBL; U84897; AAC47519.1; -. DR EMBL; AE003721; AAF55519.1; -. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0020238; 14-3-3-epsilon. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT MUTAGEN 183 183 E->K: SUPPRESSOR OF SEV-RAS1 V12; FT SUBVIABLE. FT MUTAGEN 199 199 F->Y: SUPPRESSOR OF SEV-RAS1 V12. FT MUTAGEN 214 214 Y->F: SUPPRESSOR OF SEV-RAS1 V12. SQ SEQUENCE 260 AA; 29570 MW; 1282192917E3A7A4 CRC64; MTERENNVYK AKLAEQAERY DEMVEAMKKV ASMDVELTVE ERNLLSVAYK NVIGARRASW RIITSIEQKE ENKGAEEKLE MIKTYRGQVE KELRDICSDI LNVLEKHLIP CATSGESKVF YYKMKGDYHR YLAEFATGSD RKDAAENSLI AYKAASDIAM NDLPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQAEDP NAGDGEPKEQ IQDVEDQDVS // ID 143E_HUMAN STANDARD; PRT; 255 AA. AC P42655; P29360; Q63631; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14-3-3 protein epsilon (Mitochondrial import stimulation factor L DE subunit) (Protein kinase C inhibitor protein-1) (KCIP-1) (14-3-3E). GN YWHAE. OS Homo sapiens (Human), OS Mus musculus (Mouse), OS Rattus norvegicus (Rat), OS Bos taurus (Bovine), and OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090, 10116, 9913, 9940; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=95372385; PubMed=7644510; RA Conklin D.S., Galaktionov K., Beach D.; RT "14-3-3 proteins associate with cdc25 phosphatases."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7892-7896(1995). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Heart; RA Luk S.C.W., Lee C.Y., Waye M.M.Y.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Human; RX MEDLINE=96300316; PubMed=8684458; RA Jin D.-Y., Lyu M.S., Kozak C.A., Jeang K.-T.; RT "Function of 14-3-3 proteins."; RL Nature 382:308-308(1996). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Liver; RX MEDLINE=97011338; PubMed=8858348; RA Chong S.S., Tanigami A., Roschke A.V., Ledbetter D.H.; RT "14-3-3 epsilon has no homology to LIS1 and lies telomeric to it on RT chromosome 17p13.3 outside the Miller-Dieker syndrome chromosome RT region."; RL Genome Res. 6:735-741(1996). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Human; RA Tanigami A., Chong S.S., Ledbetter D.H.; RT "14-3-3 epsilon genomic sequence."; RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Placenta; RA Strausberg R.; RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RC SPECIES=Rat, and Sheep; TISSUE=Pineal gland; RX MEDLINE=94296566; PubMed=8024705; RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., RA Moffet J.R., Namboodiri M.A., Klein D.C.; RT "Cloning and characterization of the epsilon and zeta isoforms of the RT 14-3-3 proteins."; RL DNA Cell Biol. 13:629-640(1994). RN [8] RP SEQUENCE FROM N.A. RC SPECIES=Rat; TISSUE=Liver; RX MEDLINE=95122474; PubMed=7822263; RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., RA Kitajima M., Mihara K., Omura T.; RT "cDNA cloning and characterization of mitochondrial import RT stimulation factor (MSF) purified from rat liver cytosol."; RL J. Biochem. 116:416-425(1994). RN [9] RP SEQUENCE FROM N.A. RC SPECIES=Rat; TISSUE=Brain; RX MEDLINE=96280718; PubMed=8694795; RA Gao L., Gu X.B., Yu D.S., Yu R.K., Zeng G.; RT "Association of a 14-3-3 protein with CMP-NeuAc:GM1 alpha 2,3- RT sialyltransferase."; RL Biochem. Biophys. Res. Commun. 224:103-107(1996). RN [10] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=SWISS; TISSUE=Kidney; RX MEDLINE=95269876; PubMed=7750640; RA McConnell J.E., Armstrong J.F., Bard J.B.; RT "The mouse 14-3-3 epsilon isoform, a kinase regulator whose RT expression pattern is modulated in mesenchyme and neuronal RT differentiation."; RL Dev. Biol. 169:218-228(1995). RN [11] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=129/SV; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., RA Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [12] RP SEQUENCE FROM N.A. RC SPECIES=Bovine; RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [13] RP SEQUENCE OF 1-152; 165-184 AND 216-255. RC SPECIES=Sheep; TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). RN [14] RP SEQUENCE OF 1-23 AND 125-140. RC SPECIES=Sheep; TISSUE=Brain; RX MEDLINE=90345949; PubMed=2143472; RA Toker A., Ellis C.A., Sellers L.A., Aitken A.; RT "Protein kinase C inhibitor proteins. Purification from sheep brain RT and sequence similarity to lipocortins and 14-3-3 protein."; RL Eur. J. Biochem. 191:421-429(1990). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U28936; AAA75301.1; -. DR EMBL; U20972; AAC50175.1; -. DR EMBL; U43399; AAC50625.1; -. DR EMBL; U43430; AAD00026.1; -. DR EMBL; U54778; AAC50710.1; -. DR EMBL; AB017103; BAA32538.1; -. DR EMBL; AB017098; BAA32538.1; JOINED. DR EMBL; AB017099; BAA32538.1; JOINED. DR EMBL; AB017100; BAA32538.1; JOINED. DR EMBL; AB017101; BAA32538.1; JOINED. DR EMBL; AB017102; BAA32538.1; JOINED. DR EMBL; BC000179; AAH00179.1; -. DR EMBL; BC001440; AAH01440.1; -. DR EMBL; M84416; AAC37659.1; -. DR EMBL; D30739; BAA06401.1; -. DR EMBL; Z19599; CAA79659.1; -. DR EMBL; U53882; AAC52676.1; -. DR EMBL; L07914; AAC37321.1; -. DR EMBL; D87663; BAA13424.1; -. DR EMBL; AF043735; AAC61927.1; -. DR PIR; S10806; S10806. DR PIR; S10807; S10807. DR HSSP; P29312; 1A38. DR MIM; 605066; -. DR MGD; MGI:894689; Ywhae. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Acetylation; Multigene family. FT MOD_RES 1 1 ACETYLATION. FT CONFLICT 73 73 K -> T (IN REF. 9). FT CONFLICT 120 120 F -> S (IN REF. 9). FT CONFLICT 123 123 K -> Y (IN REF. 9). FT CONFLICT 129 129 H -> Y (IN REF. 14). SQ SEQUENCE 255 AA; 29174 MW; 07817CCBD1F75B26 CRC64; MDDREDLVYQ AKLAEQAERY DEMVESMKKV AGMDVELTVE ERNLLSVAYK NVIGARRASW RIISSIEQKE ENKGGEDKLK MIREYRQMVE TELKLICCDI LDVLDKHLIP AANTGESKVF YYKMKGDYHR YLAEFATGND RKEAAENSLV AYKAASDIAM TELPPTHPIR LGLALNFSVF YYEILNSPDR ACRLAKAAFD DAIAELDTLS EESYKDSTLI MQLLRDNLTL WTSDMQGDGE EQNKEALQDV EDENQ // ID 143E_TOBAC STANDARD; PRT; 272 AA. AC O49997; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein E. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98105599; PubMed=9443388; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U91726; AAC49894.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 272 AA; 30570 MW; 6083BA2F40612AD6 CRC64; MAESTREENV YMAKLAEQAE RYEEMVEFME KVAKTVDVEE LTVEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVSSIKEYR GKIEAELSKI CDGILNLLES HLIPVASTAE SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLLAYKSAQ DIALAELAPT HPIRLGLALN FSVFYYEILN SSDRACNLAK QAFDDAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDTT VSLSLSQKYT PTNADAPTNN TVHTSKSFLG SA // ID 143F_HUMAN STANDARD; PRT; 245 AA. AC Q04917; DT 01-OCT-1993 (Rel. 27, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein eta (Protein AS1). GN YWHAH OR YWHA1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=94032477; PubMed=8218406; RA Swanson K.D., Dhar M.S., Joshi J.G.; RT "The human and bovine 14-3-3 eta protein mRNAs are highly conserved RT in both their translated and untranslated regions."; RL Biochim. Biophys. Acta 1216:145-148(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=92251832; PubMed=1578511; RA Ichimura-Ohshima Y., Morii K., Ichimura T., Araki K., RA Takahashi Y., Isobe T., Minoshima S., Fukuyama R., Shimizu N., RA Kuwano R.; RT "cDNA cloning and chromosome assignment of the gene for human brain RT 14-3-3 protein eta chain."; RL J. Neurosci. Res. 31:600-605(1992). RN [3] RP SEQUENCE FROM N.A. RA Leffers H., Tommerup N., Celis J.E.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=96123461; PubMed=8561965; RA Muratake T., Hayashi S., Ichimura Y., Morii K., Kuwano R., RA Ichikawa T., Kumanishi T., Isobe T., Watanabe M., Kondo H.; RT "The effect on methamphetamine on the mRNA level for 14.3.3 eta chain RT in the human cultured cells."; RL Mol. Neurobiol. 11:223-230(1995). RN [5] RP SEQUENCE FROM N.A. RX MEDLINE=96411648; PubMed=8812417; RA Muratake T., Hayashi S., Ichikawa T., Kumanishi T., Ichimura Y., RA Kuwano R., Isobe T., Wang Y., Minoshima S., Shimizu N., RA Takahashi Y.; RT "Structural organization and chromosomal assignment of the human RT 14-3-3 eta chain gene (YWHAH)."; RL Genomics 36:63-69(1996). RN [6] RP SEQUENCE FROM N.A. RX MEDLINE=20057165; PubMed=10591208; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A., RA Bagguley C., Bailey J., Barlow K., Bates K.N., Beasley O., Bird C.P., RA Blakey S., Bridgeman A.M., Buck D., Burgess J., Burrill W.D., RA Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., RA Cobley V., Cole C.G., Collier R.E., Connor R.E., Conroy D., Corby N., RA Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., RA Dodsworth S.J., Durbin R.M., Ellington A., Evans K.L., Fey J.M., RA Fleming K French L., Garner A.A., Gilbert J.G.R., Goward M.E., RA Grafham D., Griffiths M.N., Hall C., Hall R., Hall-Tamlyn G., RA Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., RA Kimberley A., King A., Laird G.K., Langford C.F., Leversha M.A., RA Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., RA Matthews L., Mccann O.T., Mcclay J., Mclaren S., Mcmurray A.A., RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., RA Pearson D., Phillimore B.J., Phillips S.H., Plumb R.W., Ramsay H., RA Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., RA Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., RA Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., RA Whiteley M.N., Willey D., Williams L., Williams S., Williamson H., RA Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., RA Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., RA Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., RA Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., RA Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., RA Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., RA Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., RA Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., RA Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., RA Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., RA Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., RA Nelson J., Korf I., Bedell J.A., Hillier L., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [7] RP SEQUENCE FROM N.A. RC TISSUE=Lymph; RA Strausberg R.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 26-224 FROM N.A. RC TISSUE=Keratinocytes; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: EXPRESSED MAINLY IN THE BRAIN AND PRESENT IN CC OTHER TISSUES ALBEIT AT LOWER LEVELS. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L20422; AAA35483.1; -. DR EMBL; X80536; CAA56676.1; -. DR EMBL; X78138; CAA55017.1; -. DR EMBL; X57345; CAA40620.1; -. DR EMBL; D78577; BAA11418.1; -. DR EMBL; D78576; BAA11418.1; JOINED. DR EMBL; S80794; AAB36036.1; -. DR EMBL; Z82248; CAB05112.1; -. DR EMBL; BC003047; AAH03047.1; -. DR PIR; S29339; S29339. DR PIR; S34756; S34756. DR HSSP; P29312; 1A38. DR MIM; 113508; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT CONFLICT 143 143 N -> T (IN REF. 8). FT CONFLICT 156 156 A -> G (IN REF. 1). FT CONFLICT 236 236 Q -> L (IN REF. 1). SQ SEQUENCE 245 AA; 28087 MW; B7244C100C5A0277 CRC64; GDREQLLQRA RLAEQAERYD DMASAMKAVT ELNEPLSNED RNLLSVAYKN VVGARRSSWR VISSIEQKTM ADGNEKKLEK VKAYREKIEK ELETVCNDVL SLLDKFLIKN CNDFQYESKV FYLKMKGDYY RYLAEVASGE KKNSVVEASE AAYKEAFEIS KEQMQPTHPI RLGLALNFSV FYYEIQNAPE QACLLAKQAF DDAIAELDTL NEDSYKDSTL IMQLLRDNLT LWTSDQQDEE AGEGN // ID 143F_MOUSE STANDARD; PRT; 245 AA. AC P11576; P70198; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein eta (Protein kinase C inhibitor protein-1) (KCIP-1). GN YWHAH. OS Mus musculus (Mouse), OS Rattus norvegicus (Rat), and OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090, 10116, 9913; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC SPECIES=Bovine; TISSUE=Cerebellum; RX MEDLINE=89017142; PubMed=2902623; RA Ichimura T., Isobe T., Okuyama T., Takahashi N., Araki K., RA Kuwano R., Takahashi Y.; RT "Molecular cloning of cDNA coding for brain-specific 14-3-3 protein, RT a protein kinase-dependent activator of tyrosine and tryptophan RT hydroxylases."; RL Proc. Natl. Acad. Sci. U.S.A. 85:7084-7088(1988). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Rat; RX MEDLINE=91304265; PubMed=1649368; RA Watanabe M., Isobe T., Okuyama T., Ichimura T., Kuwano R., RA Takahashi Y., Kondo H.; RT "Molecular cloning of cDNA to rat 14-3-3 eta chain polypeptide and RT the neuronal expression of the mRNA in the central nervous system."; RL Brain Res. Mol. Brain Res. 10:151-158(1991). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; TISSUE=Brain; RX MEDLINE=97340943; PubMed=9197417; RA Sladeczek F., Camonis J.H., Burnol A.F., Lebouffant F.; RT "The Cdk-like protein PCTAIRE-1 from mouse brain associates with p11 RT and 14-3-3 proteins."; RL Mol. Gen. Genet. 254:571-577(1997). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=129/SV; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., RA Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RX MEDLINE=98411340; PubMed=9738002; RA Tang S.J., Seun T.-C., McInnes R.R., Buchwald M.; RT "Association of the TLX-2 homeodomain and 14-3-3eta signaling RT proteins."; RL J. Biol. Chem. 273:25356-25363(1998). RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Strausberg R.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [7] RP SIMILARITY TO KINASE INHIBITOR. RX MEDLINE=90220866; PubMed=1970123; RA Aitken A., Ellis C.A., Harris A., Sellers L.A., Toker A.; RT "Kinase and neurotransmitters."; RL Nature 344:594-594(1990). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J03868; AAA30347.1; -. DR EMBL; D17445; BAA04259.1; -. DR EMBL; U57311; AAC53256.1; -. DR EMBL; D87661; BAA13422.1; -. DR EMBL; AF077002; AAC36290.1; -. DR EMBL; BC008187; AAH08187.1; -. DR PIR; A40484; A40484. DR PIR; S23305; S23305. DR PIR; A60031; A60031. DR HSSP; P29312; 1A38. DR MGD; MGI:109194; Ywhah. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT CONFLICT 14 15 EQ -> DE (IN REF. 4). SQ SEQUENCE 245 AA; 28080 MW; A10492B4ABB8B931 CRC64; GDREQLLQRA RLAEQAERYD DMASAMKAVT ELNEPLSNED RNLLSVAYKN VVGARRSSWR VISSIEQKTM ADGNEKKLEK VKAYREKIEK ELETVCNDVL ALLDKFLIKN CNDFQYESKV FYLKMKGDYY RYLAEVASGE KKNSVVEASE AAYKEAFEIS KEHMQPTHPI RLGLALNFSV FYYEIQNAPE QACLLAKQAF DDAIAELDTL NEDSYKDSTL IMQLLRDNLT LWTSDQQDEE AGEGN // ID 143F_TOBAC STANDARD; PRT; 258 AA. AC O49998; DT 15-DEC-1998 (Rel. 37, Created) DT 15-DEC-1998 (Rel. 37, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 14-3-3-like protein F. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=98105599; PubMed=9443388; RA Piotrowski M., Oecking C.; RT "Five new 14-3-3 isoforms from Nicotiana tabacum L.: implications for RT the phylogeny of plant 14-3-3 proteins."; RL Planta 204:127-130(1998). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U91727; AAC49895.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 258 AA; 29225 MW; 7A1DF2A7056F94E0 CRC64; MSSSRDEFVY MAKLAEQAER YEEMVDFMEK VVTAADGGEE LTIEERNLLS VAYKNVIGAR RASWRIISSI EQKEESRGNE DHVTSIKTYR SKIESELTSI CNGILKLLDS NLIRAASTGD SKVFYLKMKG DYHRYLAEFK TGAERKEAAE NTLSSYKSAQ DIANAELAPT HPIRLGLALN FSVFYYEILN SPDRACNLAK QAFDEAIAEL DTLGEESYKD STLIMQLLRD NLTLWTSDMQ DEGTEEMKEV AKPDNEEH // ID 143G_BOVIN STANDARD; PRT; 246 AA. AC P29359; DT 01-DEC-1992 (Rel. 24, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein gamma (Protein kinase C inhibitor protein-1) (KCIP-1). GN YWHAG. OS Bos taurus (Bovine), and OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913, 9940; RN [1] RP SEQUENCE OF 1-245. RC SPECIES=Bovine; RX MEDLINE=91108808; PubMed=1671102; RA Isobe T., Ichimura T., Sunaya T., Okuyama T., Takahashi N., Kuwano R., RA Takahashi Y.; RT "Distinct forms of the protein kinase-dependent activator of tyrosine RT and tryptophan hydroxylases."; RL J. Mol. Biol. 217:125-132(1991). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Bovine; RA Jones J.M., Niikura T., Pinke R.M., Guo W., Molday L., Leykam J., RA McConnell D.G.; RT "Expression of 14-3-3 proteins in bovine retinal photoreceptors."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 23-70; 121-185 AND 198-242. RC SPECIES=Sheep; TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF043737; AAC02091.1; -. DR PIR; S13610; S13610. DR PIR; S23302; S23302. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. SQ SEQUENCE 246 AA; 28121 MW; 648148CDFAF45A89 CRC64; VDREQLVQKA RLAEQAERYD DMAAAMKNVT ELNEPLSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTS ADGNEKKIEM VRAYREKIEK ELEAVCQDVL SLLDNYLIKN CSETQIESKV FYLKMKGDYY RYLAEVATGE KRATVVESSE KAYSEAHEIS KEHMQPTHPI RLGLALNYSV FYYEIQNAPE QACHLAKTAF DDAIAELDTL NEDSYKDSTL IMQLLRDNLT LWTSDQQDDD GGEGNN // ID 143G_HUMAN STANDARD; PRT; 246 AA. AC P35214; Q9UN99; Q9UDP2; O70457; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein gamma (Protein kinase C inhibitor protein-1) (KCIP-1). GN YWHAG. OS Homo sapiens (Human), OS Mus musculus (Mouse), and OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 10090, 10116; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Vascular smooth muscle; RX MEDLINE=99360936; PubMed=10433554; RA Autieri M.V., Carbone C.J.; RT "14-3-3gamma interacts with and is phosphorylated by multiple protein RT kinase C isoforms in PDGF-stimulated human vascular smooth muscle RT cells."; RL DNA Cell Biol. 18:555-564(1999). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Fetal brain; RX PubMed=10486217; RA Horie M., Suzuki M., Takahashi E., Tanigami A.; RT "Cloning, expression, and chromosomal mapping of the human 14-3-3gamma RT gene (YWHAG) to 7q11.23."; RL Genomics 60:241-243(1999). RN [3] RP SEQUENCE OF 29-246 FROM N.A. RC SPECIES=Human; RA Kozlowicz A., Bauer C., Ames M., Godfrey J.; RL Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=C57BL/6J; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Strausberg R.; RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Rat; RX MEDLINE=93164855; PubMed=8381897; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., RA Kondo H.; RT "Molecular cloning of rat cDNAs for beta and gamma subtypes of 14-3-3 RT protein and developmental changes in expression of their mRNAs in the RT nervous system."; RL Brain Res. Mol. Brain Res. 17:135-146(1993). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF142498; AAD48408.1; -. DR EMBL; AB024334; BAA85184.1; -. DR EMBL; AC006388; AAF19232.1; -. DR EMBL; AF058799; AAC14345.1; -. DR EMBL; BC008129; AAH08129.1; -. DR EMBL; D17447; BAA04261.1; -. DR EMBL; S55305; AAA13844.1; -. DR PIR; B49023; B49023. DR HSSP; P29312; 1A38. DR MIM; 605356; -. DR MGD; MGI:108109; Ywhag. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT CONFLICT 3 3 R -> P (IN REF. 1). FT CONFLICT 18 18 R -> G (IN REF. 1). FT CONFLICT 77 77 MISSING (IN REF. 1). FT CONFLICT 88 88 I -> V (IN REF. 1). FT CONFLICT 103 103 L -> V (IN REF. 1). FT CONFLICT 108 108 I -> Y (IN REF. 1). FT CONFLICT 118 121 SKVF -> RKDL (IN REF. 1). FT CONFLICT 143 144 AT -> GD (IN REF. 1). FT CONFLICT 149 149 S -> F (IN REF. 4). FT CONFLICT 156 157 AH -> R (IN REF. 1). FT CONFLICT 199 201 AFD -> EFE (IN REF. 1). FT CONFLICT 213 213 D -> E (IN REF. 1). FT CONFLICT 239 239 D -> DH (IN REF. 1). SQ SEQUENCE 246 AA; 28171 MW; 70D1479DE1F45A89 CRC64; VDREQLVQKA RLAEQAERYD DMAAAMKNVT ELNEPLSNEE RNLLSVAYKN VVGARRSSWR VISSIEQKTS ADGNEKKIEM VRAYREKIEK ELEAVCQDVL SLLDNYLIKN CSETQYESKV FYLKMKGDYY RYLAEVATGE KRATVVESSE KAYSEAHEIS KEHMQPTHPI RLGLALNYSV FYYEIQNAPE QACHLAKTAF DDAIAELDTL NEDSYKDSTL IMQLLRDNLT LWTSDQQDDD GGEGNN // ID 143H_ARATH STANDARD; PRT; 267 AA. AC P46077; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 phi (General regulatory factor 4). GN GRF4. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95062733; PubMed=7972511; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP REVISIONS TO 23 AND 245. RA Ferl R.J.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09111; AAB06231.1; -. DR EMBL; AF001414; AAB62224.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 267 AA; 30194 MW; 18FA010F752CC134 CRC64; MAAPPASSSA REEFVYLAKL AEQAERYEEM VEFMEKVAEA VDKDELTVEE RNLLSVAYKN VIGARRASWR IISSIEQKEE SRGNDDHVTT IRDYRSKIES ELSKICDGIL KLLDTRLVPA SANGDSKVFY LKMKGDYHRY LAEFKTGQER KDAAEHTLTA YKAAQDIANA ELAPTHPIRL GLALNFSVFY YEILNSPDRA CNLAKQAFDE AIAELDTLGE ESYKDSTLIM QLLRDNLTLW TSDMQDESPE EIKEAAAPKP AEEQKEI // ID 143K_ARATH STANDARD; PRT; 248 AA. AC P48348; Q9SWP7; DT 01-FEB-1996 (Rel. 33, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 kappa (General regulatory factor 8). GN GRF8 OR AT5G65430 OR MNA5.16. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (In) Plant Gene Register PGR99-114. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=98344145; PubMed=9679202; RA Kaneko T., Kotani H., Nakamura Y., Sato S., Asamizu E., Miyajima N., RA Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. V. Sequence RT features of the regions of 1,381,565 bp covered by twenty one RT physically assigned P1 and TAC clones."; RL DNA Res. 5:131-145(1998). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U36447; AAA79700.1; -. DR EMBL; AF145300; AAD51783.1; -. DR EMBL; AB011479; BAB11565.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 53 53 V -> G (IN REF. 1). FT CONFLICT 72 72 I -> L (IN REF. 1). FT CONFLICT 103 103 C -> F (IN REF. 1). FT CONFLICT 121 121 S -> R (IN REF. 1). FT CONFLICT 154 154 T -> A (IN REF. 1). FT CONFLICT 243 244 MISSING (IN REF. 3). SQ SEQUENCE 248 AA; 28028 MW; 848897CE6DB6BA37 CRC64; MATTLSRDQY VYMAKLAEQA ERYEEMVQFM EQLVSGATPA GELTVEERNL LSVAYKNVIG SLRAAWRIVS SIEQKEESRK NEEHVSLVKD YRSKVETELS SICSGILRLL DSHLIPSATA SESKVFYLKM KGDYHRYLAE FKSGDERKTA AEDTMIAYKA AQDVAVADLA PTHPIRLGLA LNFSVFYYEI LNSSEKACSM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQEQMDEA // ID 143L_ARATH STANDARD; PRT; 248 AA. AC P48349; P42647; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 lambda (General regulatory factor 6) DE (14-3-3-like protein RCI2) (14-3-3-like protein AFT1). GN GRF6 OR RCI2 OR AFT1. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94339482; PubMed=7520301; RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., RA Salinas J.; RT "Two related low-temperature-inducible genes of Arabidopsis encode RT proteins showing high homology to 14-3-3 proteins, a family of RT putative kinase regulators."; RL Plant Mol. Biol. 25:693-704(1994). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; TISSUE=Leaf; RX MEDLINE=95234749; PubMed=7718616; RA Zhang H., Wang J., Hwang I., Goodman H.M.; RT "Isolation and expression of an Arabidopsis 14-3-3-like protein RT gene."; RL Biochim. Biophys. Acta 1266:113-116(1995). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (In) Plant Gene Register PGR99-114. CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES (BY SIMILARITY). CC -!- INDUCTION: BY COLD. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X74141; CAA52238.1; -. DR EMBL; U02565; AAA74737.1; -. DR EMBL; U68545; AAB08482.1; -. DR EMBL; AF145298; AAD51781.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 241 248 MQEQMDEA -> YAGADGRGLRI (IN REF. 1). SQ SEQUENCE 248 AA; 27975 MW; 4017D23098E74891 CRC64; MAATLGRDQY VYMAKLAEQA ERYEEMVQFM EQLVTGATPA EELTVEERNL LSVAYKNVIG SLRAAWRIVS SIEQKEESRK NDEHVSLVKD YRSKVESELS SVCSGILKLL DSHLIPSAGA SESKVFYLKM KGDYHRYMAE FKSGDERKTA AEDTMLAYKA AQDIAAADMA PTHPIRLGLA LNFSVFYYEI LNSSDKACNM AKQAFEEAIA ELDTLGEESY KDSTLIMQLL RDNLTLWTSD MQEQMDEA // ID 143M_ARATH STANDARD; PRT; 263 AA. AC Q96299; O80367; DT 15-JUL-1998 (Rel. 36, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 mu (General regulatory factor 9). GN GRF9 OR AT2G42590 OR F14N22.14. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP SEQUENCE FROM N.A. RA Kuromori T., Yamamoto M.; RT "Members of the Arabidopsis 14-3-3 gene family trans-complement two RT types of defects in fission yeast."; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (In) Plant Gene Register PGR99-114. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083487; PubMed=10617197; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., VanAken S.E., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60444; AAB49334.1; -. DR EMBL; AB011545; BAA32735.1; -. DR EMBL; AF145301; AAD51784.1; -. DR EMBL; AC007087; AAD23005.1; -. DR HSSP; P29312; 1A38. DR Mendel; 31031; Arath;1020;31031. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 213 213 N -> S (IN REF. 1). SQ SEQUENCE 263 AA; 29520 MW; B70A45DF64DFD926 CRC64; MGSGKERDTF VYLAKLSEQA ERYEEMVESM KSVAKLNVDL TVEERNLLSV GYKNVIGSRR ASWRIFSSIE QKEAVKGNDV NVKRIKEYME KVELELSNIC IDIMSVLDEH LIPSASEGES TVFFNKMKGD YYRYLAEFKS GNERKEAADQ SLKAYEIATT AAEAKLPPTH PIRLGLALNF SVFYYEIMNA PERACHLAKQ AFDEAISELD TLNEESYKDS TLIMQLLRDN LTLWTSDISE EGGDDAHKTN GSAKPGAGGD DAE // ID 143N_ARATH STANDARD; PRT; 265 AA. AC Q96300; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 nu (General regulatory factor 7). GN GRF7 OR F16B3.15. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Chung H.-J., Shanker S., Ferl R.J.; RT "Sequences of five Arabidopsis general regulatory factor (GRF) genes RT encoding 14-3-3 proteins."; RL (In) Plant Gene Register PGR99-114. RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Lin X., Kaul S., Town C.D., Benito M., Creasy T.H., Haas B., Wu D., RA Ronning C.M., Koo H., Fujii C.Y., Utterback T.R., Barnstead M.E., RA Bowman C.L., White O., Nierman W.C., Fraser C.M.; RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U60445; AAB49335.1; -. DR EMBL; AF145299; AAD51782.1; -. DR EMBL; AC021640; AAF32459.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 265 AA; 29824 MW; BF76ECB7F76E166A CRC64; MSSSREENVY LAKLAEQAER YEEMVEFMEK VAKTVDTDEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNDD HVSIIKDYRG KIETELSKIC DGILNLLDSH LVPTASLAES KVFYLKMKGD YHRYLAEFKT GAERKEAAES TLVAYKSAQD IALADLAPTH PIRLGLALNF SVFYYEILNS PDRACSLAKQ AFDEAISELD TLGEESYKDS TLIMQLLRDN LTLWNSDIND EAGGDEIKEA SKHEPEEGKP AETGQ // ID 143O_ARATH STANDARD; PRT; 259 AA. AC Q01525; DT 01-JUL-1993 (Rel. 26, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 omega (General regulatory factor 2). GN GRF2 OR GF14 OR F3F9.16. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=93087554; PubMed=1454838; RA Lu G., Delisle A.J., de Vetten N.C., Ferl R.J.; RT "Brain proteins in plants: an Arabidopsis homolog to neurotransmitter RT pathway activators is part of a DNA binding complex."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11490-11494(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95175611; PubMed=7870824; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). RN [3] RP SEQUENCE FROM N.A. RA Chao Q., Brooks S., Buehler E., Johnson-Hopson C., Khan S., Kim C., RA Shinn P., Altafi H., Bei Q., Chin C., Chiou J., Choi E., Conn L., RA Conway A., Gonzales A., Hansen N., Howng B., Koo T., Lam B., Lee J., RA Lenz C., Li J., Liu A., Liu K., Liu S., Mukharsky N., Nguyen M., RA Palm C., Pham P., Sakano H., Schwartz J., Southwick A., Thaveri A., RA Toriumi M., Vaysberg M., Yu G., Federspiel N.A., Theologis A., RA Ecker J.R.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96855; AAA32798.1; -. DR EMBL; U09376; AAA96253.1; -. DR EMBL; AC013430; AAF71808.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 8 8 F -> L (IN REF. 2). SQ SEQUENCE 259 AA; 29161 MW; 9CCE5043A707918A CRC64; MASGREEFVY MAKLAEQAER YEEMVEFMEK VSAAVDGDEL TVEERNLLSV AYKNVIGARR ASWRIISSIE QKEESRGNDD HVTAIREYRS KIETELSGIC DGILKLLDSR LIPAAASGDS KVFYLKMKGD YHRYLAEFKT GQERKDAAEH TLAAYKSAQD IANAELAPTH PIRLGLALNF SVFYYEILNS PDRACNLAKQ AFDEAIAELD TLGEESYKDS TLIMQLLRDN LTLWTSDMQD DAADEIKEAA APKPTEEQQ // ID 143P_ARATH STANDARD; PRT; 255 AA. AC P42644; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 psi (General regulatory factor 3) DE (14-3-3-like protein RCI1). GN GRF3 OR RCI1 OR AT5G38480 OR MXI10.21. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95062733; PubMed=7972511; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94339482; PubMed=7520301; RA Jarillo J.A., Capel J., Leyva A., Martinez Zapater J.M., RA Salinas J.; RT "Two related low-temperature-inducible genes of Arabidopsis encode RT proteins showing high homology to 14-3-3 proteins, a family of RT putative kinase regulators."; RL Plant Mol. Biol. 25:693-704(1994). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95175611; PubMed=7870824; RA Rooney M.F., Ferl R.J.; RT "Sequences of three Arabidopsis general regulatory factor genes RT encoding GF14 (14-3-3) proteins."; RL Plant Physiol. 107:283-284(1995). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=97471969; PubMed=9330910; RA Sato S., Kotani H., Nakamura Y., Kaneko T., Asamizu E., Fukami M., RA Miyajima N., Tabata S.; RT "Structural analysis of Arabidopsis thaliana chromosome 5. I. Sequence RT features of the 1.6 Mb regions covered by twenty physically assigned RT P1 clones."; RL DNA Res. 4:215-230(1997). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- INDUCTION: BY COLD. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09110; AAA32799.1; -. DR EMBL; X74140; CAA52237.1; -. DR EMBL; U09375; AAA96252.1; -. DR EMBL; AB005231; BAB10138.1; -. DR EMBL; AB005248; BAB10138.1; JOINED. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 90 90 E -> K (IN REF. 2 AND 4). SQ SEQUENCE 255 AA; 28607 MW; 20F6CEFC2B5E333B CRC64; MSTREENVYM AKLAEQAERY EEMVEFMEKV AKTVDVEELS VEERNLLSVA YKNVIGARRA SWRIISSIEQ KEESKGNEDH VAIIKDYRGE IESELSKICD GILNVLEAHL IPSASPAESK VFYLKMKGDY HRYLAEFKAG AERKEAAEST LVAYKSASDI ATAELAPTHP IRLGLALNFS VFYYEILNSP DRACSLAKQA FDDAIAELDT LGEESYKDST LIMQLLRDNL TLWTSDMTDE AGDEIKEASK PDGAE // ID 143S_HUMAN STANDARD; PRT; 248 AA. AC P31947; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein sigma (Stratifin) (Epithelial cell marker protein 1). GN SFN OR HME1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC TISSUE=Keratinocytes; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=93002614; PubMed=1390337; RA Prasad G.L., Valverius E.M., McDuffie E., Cooper H.L.; RT "Complementary DNA cloning of a novel epithelial cell marker protein, RT HME1, that may be down-regulated in neoplastic mammary cells."; RL Cell Growth Differ. 3:507-513(1992). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=98324083; PubMed=9659898; RA Hermeking H., Lengauer C., Polyak K., He T.-C., Zhang L., RA Thiagalingam S., Kinzler K.W., Vogelstein B.; RT "14-3-3 sigma is a p53-regulated inhibitor of G2/M progression."; RL Mol. Cell 1:3-11(1997). RN [4] RP SEQUENCE FROM N.A. RA Wilson S.; RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC TISSUE=Lung, and Placenta; RA Strausberg R.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 42-49 AND 118-122. RC TISSUE=Keratinocytes; RX MEDLINE=93162043; PubMed=1286667; RA Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., RA Vandekerckhove J.; RT "Microsequences of 145 proteins recorded in the two-dimensional gel RT protein database of normal human epidermal keratinocytes."; RL Electrophoresis 13:960-969(1992). CC -!- FUNCTION: P53-REGULATED INHIBITOR OF G2/M PROGRESSION. CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC OR MAY BE SECRETED BY A NON- CC CLASSICAL SECRETORY PATHWAY. CC -!- TISSUE SPECIFICITY: PRESENT MAINLY IN TISSUES ENRICHED IN CC STRATIFIED SQUAMOUS KERATINISING EPITHELIUM. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X57348; CAA40623.1; -. DR EMBL; M93010; AAA59546.1; -. DR EMBL; AF029081; AAC52029.1; -. DR EMBL; AF029082; AAC52030.1; -. DR EMBL; AL034380; CAB92118.1; -. DR EMBL; BC000329; AAH00329.1; -. DR EMBL; BC000995; AAH00995.1; -. DR EMBL; BC002995; AAH02995.1; -. DR PIR; S29340; S29340. DR PIR; S34753; S34753. DR HSSP; P29312; 1A38. DR SWISS-2DPAGE; P31947; HUMAN. DR Aarhus/Ghent-2DPAGE; 9109; IEF. DR MIM; 601290; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. FT CONFLICT 120 120 Y -> H (IN REF. 2). FT CONFLICT 242 242 A -> V (IN REF. 2). SQ SEQUENCE 248 AA; 27774 MW; 7F4B44E3AA59ECE6 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKGAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VREYREKVET ELQGVCDTVL GLLDSHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPQEPQS // ID 143S_MOUSE STANDARD; PRT; 248 AA. AC O70456; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein sigma (Stratifin). GN SFN. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=FVB/N; RA Karpitskiy V.V., Shaw A.S.; RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: P53-REGULATED INHIBITOR OF G2/M PROGRESSION (BY CC SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC OR MAY BE SECRETED BY A NON- CC CLASSICAL SECRETORY PATHWAY (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF058798; AAC14344.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 248 AA; 27713 MW; D433390433FB3F48 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EEGSEEKGPE VKEYREKVET ELRGVCDTVL GLLDSHLIKG AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADSAGEEGG EAPDDPHI // ID 143S_SHEEP STANDARD; PRT; 248 AA. AC O77642; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein sigma (Stratifin). GN SFN. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND WILTSHIRE; TISSUE=Skin; RA Rufaut N.W.; RT "Ovine stratifin."; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: P53-REGULATED INHIBITOR OF G2/M PROGRESSION (BY CC SIMILARITY). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC OR MAY BE SECRETED BY A NON- CC CLASSICAL SECRETORY PATHWAY (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF071008; AAC24036.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 248 AA; 27849 MW; F1166FB40B23A9B3 CRC64; MERASLIQKA KLAEQAERYE DMAAFMKSAV EKGEELSCEE RNLLSVAYKN VVGGQRAAWR VLSSIEQKSN EESSEEKGPE VQEYREKVET ELRGVCDTVL GLLDTHLIKE AGDAESRVFY LKMKGDYYRY LAEVATGDDK KRIIDSARSA YQEAMDISKK EMPPTNPIRL GLALNFSVFH YEIANSPEEA ISLAKTTFDE AMADLHTLSE DSYKDSTLIM QLLRDNLTLW TADNAGEEGG EAPEEPQS // ID 143T_HUMAN STANDARD; PRT; 245 AA. AC P27348; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14-3-3 protein tau (14-3-3 protein theta) (14-3-3 protein T-cell) DE (HS1 protein). GN YWHAQ. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=T-cell; RX MEDLINE=91198149; PubMed=2015305; RA Nielsen P.J.; RT "Primary structure of a human protein kinase regulator protein."; RL Biochim. Biophys. Acta 1088:425-428(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Keratinocytes; RX MEDLINE=93294871; PubMed=8515476; RA Leffers H., Madsen P., Rasmussen H.H., Honore B., Andersen A.H., RA Walbum E., Vandekerckhove J., Celis J.E.; RT "Molecular cloning and expression of the transformation sensitive RT epithelial marker stratifin. A member of a protein family that has RT been involved in the protein kinase C signalling pathway."; RL J. Mol. Biol. 231:982-998(1993). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX MEDLINE=95327195; PubMed=7603573; RA Xiao B., Smerdon S.J., Jones D.H., Dodson G.G., Soneji Y., RA Aitken A., Gamblin S.J.; RT "Structure of a 14-3-3 protein and implications for coordination of RT multiple signalling pathways."; RL Nature 376:188-191(1995). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X56468; CAA39840.1; -. DR EMBL; X57347; CAA40622.1; -. DR PIR; S15076; S15076. DR PIR; S29342; S29342. DR PIR; S34754; S34754. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Multigene family. SQ SEQUENCE 245 AA; 27764 MW; 175534325E9E37C4 CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIDNSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 143T_MOUSE STANDARD; PRT; 245 AA. AC P35216; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14-3-3 protein tau (14-3-3 protein theta). GN YWHAQ. OS Mus musculus (Mouse), and OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090, 10116; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Rat; STRAIN=WISTAR; TISSUE=Brain; RX MEDLINE=95075231; PubMed=7984035; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., RA Inoue Y.; RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of RT 14-3-3 protein and differential distributions of their mRNAs in the RT brain."; RL Brain Res. Mol. Brain Res. 25:113-121(1994). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; TISSUE=Brain; RA Sladeczek F., Camonis J.H., Burnol A.F., Lebouffant F.; RL Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=129/SV; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., RA Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Berruti G., Perego L.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D17614; BAA04533.1; -. DR EMBL; U57312; AAC53257.1; -. DR EMBL; D87662; BAA13423.1; -. DR EMBL; U56243; AAB72023.1; -. DR HSSP; P29312; 1A38. DR MGD; MGI:891963; Ywhaq. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Multigene family. SQ SEQUENCE 245 AA; 27778 MW; E30471260E8B366E CRC64; MEKTELIQKA KLAEQAERYD DMATCMKAVT EQGAELSNEE RNLLSVAYKN VVGGRRSAWR VISSIEQKTD TSDKKLQLIK DYREKVESEL RSICTTVLEL LDKYLIANAT NPESKVFYLK MKGDYFRYLA EVACGDDRKQ TIENSQGAYQ EAFDISKKEM QPTHPIRLGL ALNFSVFYYE ILNNPELACT LAKTAFDEAI AELDTLNEDS YKDSTLIMQL LRDNLTLWTS DSAGEECDAA EGAEN // ID 143U_ARATH STANDARD; PRT; 268 AA. AC P42645; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein GF14 upsilon (General regulatory factor 5). GN GRF5 OR AT5G16050 OR F1N13_190. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=95062733; PubMed=7972511; RA Lu G., Rooney M.F., Wu K., Ferl R.J.; RT "Five cDNAs encoding Arabidopsis GF14 proteins."; RL Plant Physiol. 105:1459-1460(1994). RN [2] RP REVISIONS TO 73; 182 AND C-TERMINUS. RC STRAIN=CV. COLUMBIA; RA Ferl R.J., Lu G.; RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=97422888; PubMed=9276953; RA Wu K., Rooney M.F., Ferl R.J.; RT "The Arabidopsis 14-3-3 multigene family."; RL Plant Physiol. 114:1421-1431(1997). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=21016721; PubMed=11130714; RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E., RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., RA Kohara M., Matsumoto M., Matsuno A., Muraki A., Nakayama S., RA Nakazaki N., Naruo K., Okumura S., Shinpo S., Takeuchi C., Wada T., RA Watanabe A., Yamada M., Yasuda M., Sato S., de la Bastide M., RA Huang E., Spiegel L., Gnoj L., O'Shaughnessy A., Preston R., RA Habermann K., Murray J., Johnson D., Rohlfing T., Nelson J., RA Stoneking T., Pepin K., Spieth J., Sekhon M., Armstrong J., Becker M., RA Belter E., Cordum H., Cordes M., Courtney L., Courtney W., Dante M., RA Du H., Edwards J., Fryman J., Haakensen B., Lamar E., Latreille P., RA Leonard S., Meyer R., Mulvaney E., Ozersky P., Riley A., Strowmatt C., RA Wagner-McPherson C., Wollam A., Yoakum M., Bell M., Dedhia N., RA Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D., Baker J., RA Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M., RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I., RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T., RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., RA Langham S.-A., McCullagh B., Robben J., Grymonprez B., Zimmermann W., RA Ramsperger U., Wedler H., Balke K., Wedler E., Peters S., RA van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., RA Weitzenegger T., Bothe G., Rose M., Hauf J., Berneiser S., Hempel S., RA Feldpausch M., Lamberth S., Villarroel R., Gielen J., Ardiles W., RA Bents O., Lemcke K., Kolesov G., Mayer K.F.X., Rudd S., Schoof H., RA Schueller C., Zaccaria P., Mewes H.-W., Bevan M., Fransz P.F.; RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis RT thaliana."; RL Nature 408:823-826(2000). CC -!- FUNCTION: IS ASSOCIATED WITH A DNA BINDING COMPLEX THAT BINDS TO CC THE G BOX, A WELL-CHARACTERIZED CIS-ACTING DNA REGULATORY ELEMENT CC FOUND IN PLANTS GENES. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09109; AAB06585.1; -. DR EMBL; AF001415; AAB62225.1; -. DR EMBL; AL391145; CAC01804.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Multigene family. SQ SEQUENCE 268 AA; 30181 MW; ECB35B7E53F688FF CRC64; MSSDSSREEN VYLAKLAEQA ERYEEMVEFM EKVAKTVETE ELTVEERNLL SVAYKNVIGA RRASWRIISS IEQKEDSRGN SDHVSIIKDY RGKIETELSK ICDGILNLLE AHLIPAASLA ESKVFYLKMK GDYHRYLAEF KTGAERKEAA ESTLVAYKSA QDIALADLAP THPIRLGLAL NFSVFYYEIL NSSDRACSLA KQAFDEAISE LDTLGEESYK DSTLIMQLLR DNLTLWTSDL NDEAGDDIKE APKEVQKVDE QAQPPPSQ // ID 143X_MAIZE STANDARD; PRT; 61 AA. AC P29306; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein (Fragment). OS Zea mays (Maize). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; PACC clade; OC Panicoideae; Andropogoneae; Zea. OX NCBI_TaxID=4577; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. B73; RX MEDLINE=94105294; PubMed=8278499; RA Keith C.S., Hoang D.O., Barrett B.M., Feigelman B., Nelson M.C., RA Thai H., Baysdorfer C.; RT "Partial sequence analysis of 130 randomly selected maize cDNA RT clones."; RL Plant Physiol. 101:329-332(1993). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M95066; AAA18553.2; -. DR HSSP; P29312; 1A38. DR MaizeDB; 25467; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; PARTIAL. DR PROSITE; PS00797; 1433_2; PARTIAL. KW Multigene family. FT NON_TER 1 1 FT NON_TER 61 61 SQ SEQUENCE 61 AA; 6758 MW; E999A5A3079D6FCA CRC64; ILNSPDRACN LAKQAFDEAI SELDSLGEES YKDSTLIMQL LXDNLTLWTS DTNEDGGDEI K // ID 143Z_DROME STANDARD; PRT; 248 AA. AC P29310; O01665; Q9V5G6; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3-like protein (Leonardo protein) (14-3-3 zeta). GN 14-3-3-ZETA OR 14-3-3EZ OR LEO OR 14-3-3 OR THAP OR CG17870. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. (ISOFORM VI). RC STRAIN=OREGON-R; TISSUE=Head; RX MEDLINE=92241667; PubMed=1349290; RA Swanson K.D., Ganguly R.; RT "Characterization of a Drosophila melanogaster gene similar to the RT mammalian genes encoding the tyrosine/tryptophan hydroxylase RT activator and protein kinase C inhibitor proteins."; RL Gene 113:183-190(1992). RN [2] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RC STRAIN=OREGON-R; RX MEDLINE=97302964; PubMed=9159395; RA Kockel L., Vorbrueggen G., Jaeckle H., Mlodzik M., Bohmann D.; RT "Requirement for Drosophila 14-3-3 zeta in Raf-dependent RT photoreceptor development."; RL Genes Dev. 11:1140-1147(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORM VI). RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: REQUIRED IN RAF-DEPENDENT CELL PROLIFERATION AND CC PHOTORECEPTOR DIFFERENTIAITON DURING EYE DEVELOPMENT. ACTS CC UPSTREAM OF RAF AND DOWNSTREAM OF RAS, AND IS ESSENTIAL FOR CC VIABILITY. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; VI (SHOWN HERE) AND VI'; ARE CC PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: PREDOMINANTLY EXPRESSED IN THE VENTRAL NERVE CC CORD OF THE EMBRYO, AND IN THE NEURAL TISSUES OF THE HEAD. ALSO CC FOUND IN THE REGION POSTERIOR TO THE MORPHOGENETIC FURROW OF THE CC EYE IMAGINAL DISK WHERE CELLS DIFFERENTIATE AS PHOTORECEPTORS. CC -!- DEVELOPMENTAL STAGE: EXPRESSED THROUGHOUT ALL STAGES OF EMBRYONIC CC AND LARVAL DEVELOPMENT. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77518; AAA28324.1; -. DR EMBL; Y12573; CAA73152.1; -. DR EMBL; Y12573; CAA73153.1; -. DR EMBL; AE003831; AAF58843.2; -. DR PIR; JC1122; JC1122. DR HSSP; P29312; 1A38. DR FlyBase; FBgn0004907; 14-3-3-zeta. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Neurogenesis; Multigene family; Alternative splicing. FT VARSPLIC 149 161 QTAYQDAFDISKG -> KNAYQEAFDIAKT (IN FT ISOFORM VI'). SQ SEQUENCE 248 AA; 28227 MW; C645CF3B10C6701A CRC64; MSTVDKEELV QKAKLAEQSE RYDDMAQAMK SVTETGVELS NEERNLLSVA YKNVVGARRS SWRVISSIEQ KTEASARKQQ LAREYRERVE KELREICYEV LGLLDKYLIP KASNPESKVF YLKMKGDYYR YLAEVATGDA RNTVVDDSQT AYQDAFDISK GKMQPTHPIR LGLALNFSVF YYEILNSPDK ACQLAKQAFD DAIAELDTLN EDSYKDSTLI MQLLRDNLTL WTSDTQGDEA EPQEGGDN // ID 143Z_HUMAN STANDARD; PRT; 245 AA. AC P29312; P29213; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein-1) DE (KCIP-1) (Factor activating exoenzyme S) (FAS). GN YWHAZ. OS Homo sapiens (Human), and OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 9913; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Placenta; RX MEDLINE=92250445; PubMed=1577711; RA Zupan L.A., Steffens D.L., Berry C.A., Landt M.L., Gross R.W.; RT "Cloning and expression of a human 14-3-3 protein mediating RT phospholipolysis. Identification of an arachidonoyl-enzyme RT intermediate during catalysis."; RL J. Biol. Chem. 267:8707-8710(1992). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Bone marrow; RX PubMed=9512661; RA Seluja G.A., Pietromonaco S.F., Elias L.; RT "Two unique 5' untranslated regions in mRNAs encoding human 14-3-3 RT zeta: differential expression in hemopoietic cells."; RL Biochim. Biophys. Acta 1395:281-287(1998). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Colon; RA Strausberg R.; RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A., AND SEQUENCE OF 104-115; 140-157 AND 194-212. RC SPECIES=Bovine; TISSUE=Brain; RX MEDLINE=93211953; PubMed=8460141; RA Fu H., Coburn J., Collier R.J.; RT "The eukaryotic host factor that activates exoenzyme S of Pseudomonas RT aeruginosa is a member of the 14-3-3 protein family."; RL Proc. Natl. Acad. Sci. U.S.A. 90:2320-2324(1993). RN [5] RP SEQUENCE. RC SPECIES=Bovine; TISSUE=Brain; RX MEDLINE=92362864; PubMed=1499718; RA Isobe T., Hiyane Y., Ichimura T., Okuyama T., Takahashi N., Nakajo S., RA Nakaya K.; RT "Activation of protein kinase C by the 14-3-3 proteins homologous RT with Exo1 protein that stimulates calcium-dependent exocytosis."; RL FEBS Lett. 308:121-124(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RC SPECIES=Human; RX MEDLINE=95327196; PubMed=7603574; RA Liu D., Blenkowska J., Petosa C., Collier R.J., Fu H., Liddington R.; RT "Crystal structure of the zeta isoform of the 14-3-3 protein."; RL Nature 376:191-194(1995). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. ACTIVATES THE ADP-RIBOSYLTRANSFERASE (EXOS) ACTIVITY OF CC BACTERIAL ORIGIN. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM DELTA DIFFERS FROM ISOFORM ZETA IN BEING CC PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -!- CAUTION: WAS ORIGINALLY (REF.1) THOUGHT TO HAVE PHOSPHOLIPASE A2 CC ACTIVITY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86400; AAA36446.1; -. DR EMBL; U28964; AAC52052.1; -. DR EMBL; BC003623; AAH03623.1; -. DR EMBL; L07955; AAA30514.1; -. DR PIR; A38246; PSHUAM. DR PIR; A47389; A47389. DR PDB; 1A37; 02-MAR-99. DR PDB; 1A38; 02-MAR-99. DR PDB; 1A4O; 02-MAR-99. DR MIM; 601288; -. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family; KW 3D-structure. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 184 184 PHOSPHORYLATION (BY SIMILARITY). FT CONFLICT 25 25 C -> A (IN REF. 4). SQ SEQUENCE 245 AA; 27745 MW; D464DF2286BBFE60 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QAESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 143Z_MOUSE STANDARD; PRT; 245 AA. AC P35215; P70197; P97286; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein-1) DE (KCIP-1) (Mitochondrial import stimulation factor S1 subunit). GN YWHAZ. OS Mus musculus (Mouse), and OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090, 10116; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Rat; STRAIN=WISTAR; TISSUE=Brain; RX MEDLINE=95075231; PubMed=7984035; RA Watanabe M., Isobe T., Ichimura T., Kuwano R., Takahashi Y., Kondo H., RA Inoue Y.; RT "Molecular cloning of rat cDNAs for the zeta and theta subtypes of RT 14-3-3 protein and differential distributions of their mRNAs in the RT brain."; RL Brain Res. Mol. Brain Res. 25:113-121(1994). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Rat; STRAIN=SPRAGUE-DAWLEY; TISSUE=Hippocampus; RX MEDLINE=97128314; PubMed=8972907; RA Murakami K., Situ S.Y., Eshete F.; RT "A gene variation of 14-3-3 zeta isoform in rat hippocampus."; RL Gene 179:245-249(1996). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=Rat; TISSUE=Liver; RX MEDLINE=95122474; PubMed=7822263; RA Alam R., Hachiya N., Sakaguchi M., Shun-Ichiro K., Iwanaga S., RA Kitajima M., Mihara K., Omura T.; RT "cDNA cloning and characterization of mitochondrial import RT stimulation factor (MSF) purified from rat liver cytosol."; RL J. Biochem. 116:416-425(1994). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=C57BL/6; TISSUE=Brain; RX MEDLINE=96216731; PubMed=8645260; RA Kajiwara K., Nagasawa H., Shimizu-Nishikawa K., Ookura T., RA Kimura M., Sugaya E.; RT "Molecular characterization of seizure-related genes isolated by RT differential screening."; RL Biochem. Biophys. Res. Commun. 219:795-799(1996). RN [5] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; STRAIN=129/SV; RA Takihara Y., Irie K., Nomura M., Motaleb M., Matsumoto K., RA Shimada K.; RL Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RA Sladeczek F., Camonis J.H., Burnol A.F., Lebouffant F.; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. RC SPECIES=Mouse; RX MEDLINE=97168955; PubMed=9016762; RA Honda R., Ohba Y., Yasuda H.; RT "14-3-3 zeta protein binds to the carboxyl half of mouse wee1 RT kinase."; RL Biochem. Biophys. Res. Commun. 230:262-265(1997). RN [8] RP SEQUENCE OF 58-245 FROM N.A. RC SPECIES=Rat; STRAIN=SPRAGUE-DAWLEY; TISSUE=Pineal gland; RX MEDLINE=94296566; PubMed=8024705; RA Roseboom P.H., Weller J.L., Babila T., Aitken A., Sellers L.A., RA Moffet J.R., Namboodiri M.A., Klein D.C.; RT "Cloning and characterization of the epsilon and zeta isoforms of the RT 14-3-3 proteins."; RL DNA Cell Biol. 13:629-640(1994). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. BINDS TO THE C-TERMINAL PART OF WEE1 KINASE. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM DELTA DIFFERS FROM ISOFORM ZETA IN BEING CC PHOSPHORYLATED (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D17615; BAA04534.1; -. DR EMBL; U37252; AAA80544.1; -. DR EMBL; D30740; BAA06402.1; -. DR EMBL; L07913; AAC37660.1; -. DR EMBL; D87660; BAA13421.1; -. DR EMBL; U79231; AAC53254.1; -. DR EMBL; D83037; BAA11751.1; -. DR EMBL; D78647; BAA11464.1; -. DR HSSP; P29312; 1A4O. DR MGD; MGI:109484; Ywhaz. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 184 184 PHOSPHORYLATION (BY SIMILARITY). FT CONFLICT 78 78 M -> V (IN REF. 7). FT CONFLICT 88 88 T -> M (IN REF. 2). FT CONFLICT 109 109 A -> R (IN REF. 8). FT CONFLICT 218 219 MQ -> IE (IN REF. 5). FT CONFLICT 236 236 E -> D (IN REF. 7). SQ SEQUENCE 245 AA; 27771 MW; 2164DF3793B45B7A CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNAS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 143Z_SHEEP STANDARD; PRT; 245 AA. AC P29361; DT 01-DEC-1992 (Rel. 24, Created) DT 01-DEC-1992 (Rel. 24, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 14-3-3 protein zeta/delta (Protein kinase C inhibitor protein-1) DE (KCIP-1). GN YWHAZ. OS Ovis aries (Sheep). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Caprinae; Ovis. OX NCBI_TaxID=9940; RN [1] RP SEQUENCE. RC TISSUE=Brain; RX MEDLINE=92283271; PubMed=1317796; RA Toker A., Sellers L.A., Amess B., Patel Y., Harris A., Aitken A.; RT "Multiple isoforms of a protein kinase C inhibitor (KCIP-1/14-3-3) RT from sheep brain. Amino acid sequence of phosphorylated forms."; RL Eur. J. Biochem. 206:453-461(1992). RN [2] RP SEQUENCE OF 1-22 AND 122-137. RC TISSUE=Brain; RX MEDLINE=90345949; PubMed=2143472; RA Toker A., Ellis C.A., Sellers L.A., Aitken A.; RT "Protein kinase C inhibitor proteins. Purification from sheep brain RT and sequence similarity to lipocortins and 14-3-3 protein."; RL Eur. J. Biochem. 191:421-429(1990). RN [3] RP PHOSPHORYLATION. RX MEDLINE=95197587; PubMed=7890696; RA Aitken A., Howell S., Jones D., Madrazo J., Patel Y.; RT "14-3-3 alpha and delta are the phosphorylated forms of RT raf-activating 14-3-3 beta and zeta. In vivo stoichiometric RT phosphorylation in brain at a Ser-Pro-Glu-Lys motif."; RL J. Biol. Chem. 270:5706-5709(1995). RN [4] RP POST-TRANSLATIONAL MODIFICATIONS. RA Aitken A., Patel Y., Martin H., Jones D., Robinson K., Madrazo J., RA Howell S.; RT "Electrospray mass spectroscopy analysis with online trapping of RT posttranslationally modified mammalian and avian brain 14-3-3 RT isoforms."; RL J. Protein Chem. 13:463-465(1994). CC -!- FUNCTION: ACTIVATES TYROSINE AND TRYPTOPHAN HYDROXYLASES IN THE CC PRESENCE OF CA(2+)/CALMODULIN-DEPENDENT PROTEIN KINASE II, AND CC STRONGLY ACTIVATES PROTEIN KINASE C. IS PROBABLY A MULTIFUNCTIONAL CC REGULATOR OF THE CELL SIGNALING PROCESSES MEDIATED BY BOTH CC KINASES. CC -!- SUBUNIT: HOMODIMER. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: 14-3-3 PROTEINS ARE LOCALIZED IN NEURONS, AND CC ARE AXONALLY TRANSPORTED TO THE NERVE TERMINALS. THEY MAY BE ALSO CC PRESENT, AT LOWER LEVELS, IN VARIOUS OTHER EUKARYOTIC TISSUES. CC -!- PTM: ISOFORM DELTA DIFFERS FROM ISOFORM ZETA IN BEING CC PHOSPHORYLATED. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. DR PIR; S10805; S10805. DR PIR; S23304; S23304. DR HSSP; P29312; 1A4O. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Brain; Neurone; Phosphorylation; Acetylation; Multigene family. FT MOD_RES 1 1 ACETYLATION. FT MOD_RES 184 184 PHOSPHORYLATION. SQ SEQUENCE 245 AA; 27856 MW; 292158A893B44CE5 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKSVT EQGAELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQQMAR EYREKIETEL RDICNDVLSL LEKFLIPNRS QPESKVFYLK MKGDYYRYLA EVAAGDDKKG IVDQSQQAYQ EAFEISKKEM QPTHPIRLGL ALNFSVFYYE ILNSPEKACS LAKTAFDEAI AELDTLSEES YKDSTLIMQL LRDNLTLWTS DTQGDEAEAG EGGEN // ID 143Z_XENLA STANDARD; PRT; 247 AA. AC Q91896; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 15-JUL-1998 (Rel. 36, Last annotation update) DE 14-3-3 protein zeta. OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus. OX NCBI_TaxID=8355; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=97341071; PubMed=9197545; RA Kousteni S., Tura F., Sweeney G.E., Ramji D.P.; RT "Sequence and expression analysis of a Xenopus laevis cDNA which RT encodes a homologue of mammalian 14-3-3 zeta protein."; RL Gene 190:279-285(1997). CC -!- SUBUNIT: HOMODIMER (BY SIMILARITY). CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: PRESENT IN ALL ADULT TISSUES EXAMINED WITH THE CC HIGHEST LEVELS IN THE BRAIN. CC -!- SIMILARITY: BELONGS TO THE 14-3-3 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X95519; CAA64773.1; -. DR HSSP; P29312; 1A38. DR InterPro; IPR000308; 14-3-3. DR Pfam; PF00244; 14-3-3; 1. DR PRINTS; PR00305; 1433ZETA. DR ProDom; PD000600; 14-3-3; 1. DR SMART; SM00101; 14_3_3; 1. DR PROSITE; PS00796; 1433_1; 1. DR PROSITE; PS00797; 1433_2; 1. KW Phosphorylation; Acetylation; Multigene family. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT MOD_RES 184 184 PHOSPHORYLATION (BY SIMILARITY). SQ SEQUENCE 247 AA; 27784 MW; E53BCC4EAED0FD77 CRC64; MDKNELVQKA KLAEQAERYD DMAACMKRVT EEGGELSNEE RNLLSVAYKN VVGARRSSWR VVSSIEQKTE GAEKKQEMSR EYREKIEAEL REICNDVLNL LDKFLIANAT QPESKVFYLK MKGDYYRYLA EVAAGNAKTE IVGQSQKAYQ DAFDISKTEM QPTHPIRLGL ALKLLCVLTN EESSTVQDKA CALAKAAFDE AIAELDTLSE ESYKDSTLIM QLLRDNLTLW TSDTQGDEAE QGEGGEN // ID 14KD_DAUCA STANDARD; PRT; 137 AA. AC P14009; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 14 kDa proline-rich protein DC2.15 precursor. OS Daucus carota (Carrot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids II; Apiales; Apiaceae; Daucus. OX NCBI_TaxID=4039; RN [1] RP SEQUENCE FROM N.A. RA Aleith F., Richter G.; RT "Gene expression during induction of somatic embryogenesis in carrot RT cell suspensions."; RL Planta 183:17-24(1990). RN [2] RP SEQUENCE OF 1-8 FROM N.A. RA Kaldenhoff R., Holk A., Richter G.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: MAY BE CONNECTED WITH THE INITIATION OF EMBRYOGENESIS CC OR WITH THE METABOLIC CHANGES PRODUCED BY THE REMOVAL OF AUXINS. CC -!- DEVELOPMENTAL STAGE: TRANSIENTLY EXPRESSED DURING EARLY CC EMBRYOGENESIS. CC -!- INDUCTION: BY THE REMOVAL OF AUXINS. CC -!- SIMILARITY: STRONG, TO MAIZE CORTICAL CELL DELINEATING PROTEIN CC (ZRP3). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X15436; CAA33476.1; -. DR EMBL; X75806; CAA53441.1; -. DR EMBL; X75807; CAA53442.1; -. DR EMBL; X75808; CAA53443.1; -. DR EMBL; X75809; CAA53444.1; -. DR EMBL; X75810; CAA53445.1; -. DR PIR; S35714; S35714. DR HSSP; P24337; 1HYP. DR InterPro; IPR003612; AAI. DR InterPro; IPR000528; Plant_LTP. DR Pfam; PF00279; LTP; 1. DR SMART; SM00499; AAI; 1. KW Transmembrane; Signal. FT SIGNAL 1 25 POTENTIAL. FT CHAIN 26 137 14 KDA PROLINE-RICH PROTEIN DC2.15. FT TRANSMEM 88 104 POTENTIAL. FT DOMAIN 30 49 PRO-RICH. SQ SEQUENCE 137 AA; 14392 MW; CAED1BDB3949F890 CRC64; MGSKNSASVA LFFTLNILFF ALVSSTEKCP DPYKPKPKPT PKPTPTPYPS AGKCPRDALK LGVCADVLNL VHNVVIGSPP TLPCCSLLEG LVNLEAAVCL CTAIKANILG KNLNLPIALS LVLNNCGKQV PNGFECT // ID 14KD_MYCTU STANDARD; PRT; 143 AA. AC P30223; DT 01-APR-1993 (Rel. 25, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14 kDa antigen (16 kDa antigen) (HSP 16.3). GN HSPX OR RV2031C OR MT2090 OR MTV018.18C. OS Mycobacterium tuberculosis. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1773; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ERDMANN, AND H37RV; RX MEDLINE=92138631; PubMed=1370952; RA Verbon A., Hartskeerl R.A., Schuitema A., Kolk A.H.J., Young D.B., RA Lathigra R.; RT "The 14,000-molecular-weight antigen of Mycobacterium tuberculosis is RT related to the alpha-crystallin family of low-molecular-weight heat RT shock proteins."; RL J. Bacteriol. 174:1352-1359(1992). RN [2] RP SEQUENCE, AND CHARACTERIZATION. RC STRAIN=ERDMANN; RX MEDLINE=92225631; PubMed=1563797; RA Lee B.-Y., Hefta S.A., Brennan P.J.; RT "Characterization of the major membrane protein of virulent RT Mycobacterium tuberculosis."; RL Infect. Immun. 60:2066-2074(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=H37RV; RX MEDLINE=98295987; PubMed=9634230; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., RA Badcock K., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., RA Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., RA Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., RA Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CDC 1551 / Oshkosh; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J., DeBoy R., Dodson R., Gwinn M.L., Haft D., Hickey E., RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A., RA Bishai W.; RT "Whole genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: PROBABLY THE EXTERNAL SIDE OF THE CELL WALL. CC -!- MASS SPECTROMETRY: MW=16100; METHOD=ELECTROSPRAY. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; S79751; AAB21317.1; -. DR EMBL; M76712; AAA25342.1; -. DR EMBL; AL021899; CAA17245.1; -. DR EMBL; AE007059; AAK46369.1; -. DR PIR; A42651; A42651. DR PIR; A43823; A43823. DR TIGR; MT2090; -. DR TubercuList; Rv2031c; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Complete proteome. FT INIT_MET 0 0 SQ SEQUENCE 143 AA; 16096 MW; 751AD94203226CE9 CRC64; ATTLPVQRHP RSLFPEFSEL FAAFPSFAGL RPTFDTRLMR LEDEMKEGRY EVRAELPGVD PDKDVDIMVR DGQLTIKAER TEQKDFDGRS EFAYGSFVRT VSLPVGADED DIKATYDKGI LTVSVAVSEG KPTEKHIQIR STN // ID 14KD_RHOSH STANDARD; PRT; 124 AA. AC P16536; DT 01-AUG-1990 (Rel. 15, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 14 kDa peptide of ubiquinol-cytochrome C2 oxidoreductase complex. OS Rhodobacter sphaeroides (Rhodopseudomonas sphaeroides). OC Bacteria; Proteobacteria; alpha subdivision; Rhodobacter group; OC Rhodobacter. OX NCBI_TaxID=1063; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91340695; PubMed=1651916; RA Usui S., Yu L.; RT "Subunit IV (Mr = 14,384) of the cytochrome b-c1 complex from RT Rhodobacter sphaeroides. Cloning, DNA sequencing, and ubiquinone RT binding domain."; RL J. Biol. Chem. 266:15644-15649(1991). RN [2] RP SEQUENCE OF 61-108. RX MEDLINE=90110107; PubMed=2153104; RA Purvis D.J., Theiler R., Niederman R.A.; RT "Chromatographic and protein chemical analysis of the ubiquinol- RT cytochrome c2 oxidoreductase isolated from Rhodobacter sphaeroides."; RL J. Biol. Chem. 265:1208-1215(1990). CC -!- FUNCTION: COMPONENT OF THE UBIQUINOL-CYTOCHROME C REDUCTASE CC COMPLEX (COMPLEX III OR CYTOCHROME B-C1 COMPLEX), WHICH IS A CC RESPIRATORY CHAIN THAT GENERATES AN ELECTROCHEMICAL POTENTIAL CC COUPLED TO ATP SYNTHESIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M68939; AAA26107.1; -. DR PIR; B34935; B34935. DR PIR; A40794; A40794. KW Oxidoreductase; Electron transport; Inner membrane; Transmembrane; KW Oxidative phosphorylation; Respiratory chain. FT TRANSMEM 85 102 POTENTIAL. SQ SEQUENCE 124 AA; 14393 MW; E390C856C1D752F3 CRC64; MFSFIDDIPS FEQIKARVRD DLRKHGWEKR WNDSRLVQKS RELLNDEELK IDPATWIWKR MPSREEVAAR RQRDFETVWK YRYRLGGFAS GALLALALAG IFSTGNFGGS SDAGNRPSVV YPIE // ID 14P_ARATH STANDARD; PRT; 211 AA. AC O64628; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein At2g18990. GN AT2G18990 OR F19F24.19. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083487; PubMed=10617197; RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D., RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V., RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., RA Moffat K.S., Cronin L.A., Shen M., VanAken S.E., Umayam L., RA Tallon L.J., Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., RA Goodman H.M., Somerville C.R., Copenhaver G.P., Preuss D., RA Nierman W.C., White O., Eisen J.A., Salzberg S.L., Fraser C.M., RA Venter J.C.; RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis RT thaliana."; RL Nature 402:761-768(1999). CC -!- SIMILARITY: BELONGS TO THE UPF0071 FAMILY. SOME SIMILARITY TO THE CC THIOREDOXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AC002392; AAF18603.1; -. DR InterPro; IPR000063; Thioredoxin. SQ SEQUENCE 211 AA; 24451 MW; 43B26F01CF7F6D14 CRC64; MANPIQEILE KQVLTVAKAM EDKIDDEIAS LEKLDEDDLE VLRERRLKQM KKMAEKKKRW ISLGHGEYSE IHSEKDFFSV VKASERVVCH FYRENWPCKV MDKHMSILAK QHIETRFVKI QAEKSPFLAE RLKIVVLPTL ALIKNTKVDD YVVGFNELGG KDDFSTEDLE ERIARAQVIH YDGESSSLKP KSTTQVRRNV RQSARSDSDS E // ID 14P_BOVIN STANDARD; PRT; 179 AA. AC O18883; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein 1-4 (Fragment). GN APACD. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Corpus luteum; RA Brule S., Lussier J.G.; RT "Bovine ATP binding protein."; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE UPF0071 FAMILY. SOME SIMILARITY TO THE CC THIOREDOXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF027733; AAB84006.1; -. DR InterPro; IPR000063; Thioredoxin. DR Pfam; PF00085; thiored; 1. FT NON_TER 1 1 SQ SEQUENCE 179 AA; 21051 MW; 6873189499AD494C CRC64; GEYREIPSER DFFQEVKESK KVVCHFYRDS TFRCKILDRH LVILSKKHLE TKFLKLNVEK APFLCERLRI KVIPTLALVK DGKTQDFVVG FSDLGNTDDF TTETLEWRLG CSDILNYSGN LMEPPFQSQK KFGTNFTKLE KKLFGERNMI QTLMMIRKLV TILCKSSFYF SLLHTRCVF // ID 14P_HUMAN STANDARD; PRT; 226 AA. AC O14530; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein 1-4 (ATP binding protein associated with cell DE differentiation). GN APACD. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Leukemia; RA Shiosaka T.; RT "Differential expression of 1-4 gene in functionally distinct ME-1 RT subclones."; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: NOT KNOWN, ASSOCIATED WITH CELL DIFFERENTIATION. CC -!- SIMILARITY: BELONGS TO THE UPF0071 FAMILY. SOME SIMILARITY TO THE CC THIOREDOXIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AB006679; BAA21881.1; -. DR InterPro; IPR000063; Thioredoxin. DR Pfam; PF00085; thiored; 1. SQ SEQUENCE 226 AA; 26538 MW; 2325E74279405382 CRC64; MEADASVDMF SKVLEHQLLQ TTKLVEEHLD SEIQKLDQMD EDELERLKEK RLQALRKAQQ QKQEWLSKGH GEYREIPSER DFFQEVKESE NVVCHFYRDS TFRCKILDRH LAILSKKHLE TNFLKLNVEK APFLCERLHI KVIPTLALLK DGKTQDYVVG FTDLGNTDDF TTETLEWRLG SSDILNYSGN LMEPPFQNQK KFGTNFTKLE KKTMRGKKYD SDSDDD // ID 15E1_ARATH STANDARD; PRT; 92 AA. AC Q9SMZ9; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative protein 15E1.1 homolog At4g33100. GN AT4G33100 OR F4I10.30. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=20083488; PubMed=10617198; RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., RA Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., RA Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., RA Weichselgartner M., de Simone V., Obermaier B., Mache R., Mueller M., RA Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., RA Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., RA Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., RA Langham S.-A., McCullagh B., Bilham L., Robben J., RA Van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., RA Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., RA Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., RA Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., RA Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., RA De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., RA Van Montagu M., Rogers J., Cronin A., Quail M., Bray-Allen S., RA Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., RA Pettett A., Rajandream M.-A., Lyne M., Benes V., Rechmann S., RA Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., RA Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., RA Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., RA Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., RA Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., RA Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., RA Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., RA Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., RA Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., RA Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., RA Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., RA Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., RA Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., RA Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., RA Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L., RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., RA Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., RA Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., RA Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., RA Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., RA Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., RA Chen E., Marra M., Martienssen R., McCombie W.R.; RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis RT thaliana."; RL Nature 402:769-777(1999). CC -!- SIMILARITY: BELONGS TO THE 15E1.1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AL035525; CAB36784.1; -. DR EMBL; AL161582; CAB80027.1; -. KW Hypothetical protein. SQ SEQUENCE 92 AA; 10540 MW; CF3BFCD387064FE2 CRC64; MGLLKKKDST SARSSTSPCA DLRNAYHNCF NKWYSEKFVK GQWDKEECVA EWKKYRDCLS ENLDGKLLTR ILEVDGELNP TKQATDSKES SS // ID 15E1_HUMAN STANDARD; PRT; 76 AA. AC O43715; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein 15E1.1 (Protein HSPC132). GN 15E1.1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RA Murphy L.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=20499367; PubMed=11042152; RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.; RT "Cloning and functional analysis of cDNAs with open reading frames for RT 300 previously undefined genes expressed in CD34+ hematopoietic RT stem/progenitor cells."; RL Genome Res. 10:1546-1560(2000). CC -!- SIMILARITY: BELONGS TO THE 15E1.1 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AL021546; CAA16495.1; -. DR EMBL; AF161481; AAF29096.1; -. SQ SEQUENCE 76 AA; 8786 MW; 00B41AC399D76590 CRC64; MNSVGEACTD MKREYDQCFN RWFAEKFLKG DSSGDPCTDL FKRYQQCVQK AIKEKEIPIE GLEFMGHGKE KPENSS // ID 15E2_HUMAN STANDARD; PRT; 136 AA. AC O43716; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Putative protein 15E1.2. GN 15E1.2. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RA Murphy L.; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE GATC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AL021546; CAA16496.1; -. DR InterPro; IPR003837; Glu-tRNAGln. DR Pfam; PF02686; Glu-tRNAGln; 1. KW Hypothetical protein. SQ SEQUENCE 136 AA; 15086 MW; 113118E9507234E4 CRC64; MWSRLVWLGL RAPLGGRQGF TSKADPQGSG RITAAVIEHL ERLALVDFGS REAVARLEKA IAFADRLRAV DTDGVEPMES VLEDRCLYLR SDNVVEGNCA DELLQNSHRV VEEYFVAPPG NISLPKLDEQ EPFPHS // ID 170K_TRVPS STANDARD; PRT; 179 AA. AC P05079; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 13-AUG-1987 (Rel. 05, Last annotation update) DE Potential 170 kDa protein (Fragment). OS Tobacco rattle virus (strain PSG). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Tobravirus. OX NCBI_TaxID=12297; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86176720; PubMed=3960718; RA Cornelissen B.J.C., Linthorst H.J.M., Brederode F.T., Bol J.F.; RT "Analysis of the genome structure of tobacco rattle virus strain RT PSG."; RL Nucleic Acids Res. 14:2157-2169(1986). CC -!- MISCELLANEOUS: RESIDUES 8 TO 173 ARE IDENTICAL TO RESIDUES 86 TO CC 251 IN POTENTIAL 194 KDA PROTEIN IN SYM. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03685; CAA27319.1; -. DR PIR; A05248; A05248. DR InterPro; IPR001788; RNA_dep_RNApol2. DR Pfam; PF00978; RNA_dep_RNApol2; 1. FT NON_TER 1 1 SQ SEQUENCE 179 AA; 19950 MW; A321512687CA92D4 CRC64; GAHLVPTKSG DADTYNANSD RTLCALLSEL PLEKAVMVTY GGDDSLIAFP RGTQFVDPCP KLATKWNFEC KIFKYDVPMF CGKFLLKTSS CYEFVPDPVK VLTKLGKKSI KDVQHLAEIY ISLNDSNRAL GNYMVVSKLS ESVSDRYLYK GDSVHALCAL WKHIKSFTAL CTLLPRRKG // ID 17KD_RICAM STANDARD; PRT; 154 AA. AC P50927; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor (Fragment). GN OMP. OS Rickettsia amblyommii. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=33989; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MO 85-1084; RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11013; AAB07704.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 >154 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15879 MW; E4FBE4C29D943581 CRC64; MKLLSKIMII ALAASTLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ VGAGMDEQDR RIAELTSQKA LETAPNGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQ // ID 17KD_RICAU STANDARD; PRT; 154 AA. AC P50928; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor (Fragment). GN OMP. OS Rickettsia australis. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=787; RN [1] RP SEQUENCE FROM N.A. RA Baird R.W., Ross B., Dwyer B.; RL Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M74042; AAA26394.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 >154 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15967 MW; E3AA833346FAC320 CRC64; MKLLSKIMII ALAASMLQAC NSPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSNGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQ // ID 17KD_RICCA STANDARD; PRT; 80 AA. AC P29697; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen (Fragment). GN OMP. OS Rickettsia canada. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=788; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92108069; PubMed=1729713; RA Azad A.F., Sacci J.B. Jr., Nelson W.M., Dasch G.A., RA Schmidtmann E.T., Carl M.; RT "Genetic characterization and transovarial transmission of a RT typhus-like rickettsia found in cat fleas."; RL Proc. Natl. Acad. Sci. U.S.A. 89:43-46(1992). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M82879; -; NOT_ANNOTATED_CDS. DR InterPro; IPR000437; Prok_lipoprot. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; PARTIAL. KW Outer membrane; Lipoprotein; Antigen. FT NON_TER 1 1 FT NON_TER 80 80 SQ SEQUENCE 80 AA; 8372 MW; AD289A48EAB19E0E CRC64; GSQFGKGKGQ LIGVGAGALL GAILGNQIGA GMDEQDRRLA ELTSQRALET TPSGTSIEWR NPDNGNYGYV TPSKTYKNST // ID 17KD_RICCN STANDARD; PRT; 159 AA. AC P05372; DT 01-NOV-1988 (Rel. 09, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 17 kDa surface antigen precursor. GN OMP OR RC1287. OS Rickettsia conorii, and OS Rickettsia rickettsii. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=781, 783; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=R.conorii, and R.rickettsii; RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=R.conorii; STRAIN=Malish 7; RX MEDLINE=21442074; PubMed=11557893; RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V., RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., RA Raoult D.; RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii."; RL Science 293:2093-2098(2001). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=R.rickettsii; RX MEDLINE=87222152; PubMed=3108232; RA Anderson B.E., Regnery R.L., Carlone G.M., Tzianabos T., McDade J.E., RA Fu Z.Y., Bellini W.J.; RT "Sequence analysis of the 17-kilodalton-antigen gene from Rickettsia RT rickettsii."; RL J. Bacteriol. 169:2385-2390(1987). RN [4] RP SEQUENCE OF 1-30 FROM N.A. RC SPECIES=R.rickettsii; RX MEDLINE=89008059; PubMed=3139629; RA Anderson B.E., Baumstark B.R., Bellini W.J.; RT "Expression of the gene encoding the 17-kilodalton antigen from RT Rickettsia rickettsii: transcription and posttranslational RT modification."; RL J. Bacteriol. 170:4493-4500(1988). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28479; AAA26379.1; -. DR EMBL; M28480; AAA26376.1; -. DR EMBL; AE008675; AAL03825.1; -. DR EMBL; M16486; AAA26381.1; -. DR EMBL; J03371; -; NOT_ANNOTATED_CDS. DR PIR; A25972; A25972. DR PIR; A31836; A31836. DR PIR; A33971; A33971. DR PIR; B33971; B33971. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 FT CHAIN 20 159 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT CONFLICT 146 146 N -> D (IN REF. 3). FT CONFLICT 153 153 G -> E (IN REF. 3). SQ SEQUENCE 159 AA; 16581 MW; 206A2BBF74FCE169 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICJA STANDARD; PRT; 159 AA. AC Q52764; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE 17 kDa surface antigen precursor. GN OMP. OS Rickettsia japonica. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=35790; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=YH; RX MEDLINE=95229950; PubMed=7714214; RA Furuya Y., Katayama T., Yoshida Y., Kaiho I.; RT "Specific amplification of Rickettsia japonica DNA from clinical RT specimens by PCR."; RL J. Clin. Microbiol. 33:487-489(1995). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D16515; BAA03965.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 159 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). SQ SEQUENCE 159 AA; 16554 MW; CDDCE7CEBDCD6B41 CRC64; MKLLSKIMII ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG TGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACRQ PDGQWQVVN // ID 17KD_RICMO STANDARD; PRT; 154 AA. AC P50929; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor (Fragment). GN OMP. OS Rickettsia montana. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=33991; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OHIO 83-441; RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11017; AAB07705.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 >154 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15881 MW; A09C53B8769E31DA CRC64; MKLLSKIMII ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGQG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICPA STANDARD; PRT; 154 AA. AC P50930; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor (Fragment). GN OMP. OS Rickettsia parkeri. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=35792; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MACULATUM; RA Pretzman C.I., Stothard D.R., Ralph D., Clark J.B., Fuerst P.A.; RL Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U17008; AAA82040.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 >154 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15897 MW; 5D06F45F9DBD5EEC CRC64; MKLLSKIMVI ALATSMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICPR STANDARD; PRT; 159 AA. AC P16624; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 17 kDa surface antigen precursor. GN OMP OR RP833. OS Rickettsia prowazekii. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=782; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MADRID E; RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=MADRID E; RX MEDLINE=99039499; PubMed=9823893; RA Andersson S.G.E., Zomorodipour A., Andersson J.O., RA Sicheritz-Ponten T., Alsmark U.C.M., Podowski R.M., Naeslund A.K., RA Eriksson A.-S., Winkler H.H., Kurland C.G.; RT "The genome sequence of Rickettsia prowazekii and the origin of RT mitochondria."; RL Nature 396:133-140(1998). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28482; AAA26378.1; ALT_SEQ. DR EMBL; AJ235273; CAA15258.1; -. DR PIR; D33971; D33971. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal; Complete proteome. FT SIGNAL 1 19 FT CHAIN 20 159 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). SQ SEQUENCE 159 AA; 16672 MW; A33D404B65EEB071 CRC64; MKLLSKIMII ALAASMLQAC NGQSGMNKQG TGTLLGGAGG ALLGSQFGQG KGQLVGVGVG ALLGAVLGGQ IGASMDEQDR RLLELTSQRA LESAPSGSNI EWRNPDNGNH GYVTPNKTYR NSAGQYCREY TQTVIIGGKQ QKTYGNACRQ PDGQWQVVN // ID 17KD_RICRH STANDARD; PRT; 154 AA. AC P50931; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor (Fragment). GN OMP. OS Rickettsia rhipicephali. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=33992; RN [1] RP SEQUENCE FROM N.A. RA Stothard D.R., Ralph D.A., Clark J.B., Fuerst P.A., Pretzman C.; RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U11020; AAB07706.1; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 BY SIMILARITY. FT CHAIN 20 >154 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). FT NON_TER 154 154 SQ SEQUENCE 154 AA; 15895 MW; 0CF85AD5D96DFEFB CRC64; MKLLSKIMII ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGKG KGQLVGVGVG ALLGAVLGGQ IGAGMDEQDR RLAELTSQRA LETAPSGSNV EWRNPDNGNY GYITPNKTYR NSTGQYCREY TQTVVIGGKQ QKAYGNACLQ PDGQ // ID 17KD_RICTY STANDARD; PRT; 159 AA. AC P22882; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 01-OCT-1996 (Rel. 34, Last annotation update) DE 17 kDa surface antigen precursor. GN OMP. OS Rickettsia typhi. OC Bacteria; Proteobacteria; alpha subdivision; Rickettsiales; OC Rickettsiaceae; Rickettsieae; Rickettsia. OX NCBI_TaxID=785; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89359171; PubMed=2768201; RA Anderson B.E., Tzianabos T.; RT "Comparative sequence analysis of a genus-common rickettsial antigen RT gene."; RL J. Bacteriol. 171:5199-5201(1989). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE OUTER MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28481; AAA26377.1; -. DR PIR; C33971; C33971. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Outer membrane; Lipoprotein; Antigen; Signal. FT SIGNAL 1 19 FT CHAIN 20 159 17 KDA SURFACE ANTIGEN. FT LIPID 20 20 N-ACYL DIGLYCERIDE (PROBABLE). SQ SEQUENCE 159 AA; 16549 MW; 08973E2648FD8CD8 CRC64; MKLLSKVMIL ALAASMLQAC NGPGGMNKQG TGTLLGGAGG ALLGSQFGHG KGQLVGVGVG ALLGAVLGGQ IGASLDEQDR KLLELTSQRA LESAPSGSNI EWRNPDNGNH GYVTPNKTYR NSTGQYCREY TQTVVIGGKQ QTTYGNACRQ PDGQWQVVN // ID 18C_DROME STANDARD; PRT; 215 AA. AC P16909; Q9VPA8; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Histone-like protein 18C. GN MST77F OR ANON-77F OR 18C OR CG3354. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CANTON-S; RX MEDLINE=89107990; PubMed=3215511; RA Kalderon D., Rubin G.M.; RT "Isolation and characterization of Drosophila cAMP-dependent protein RT kinase genes."; RL Genes Dev. 2:1539-1556(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: NOT KNOWN. ENCODED IN THE INTRON OF CAMP-DEPENDENT CC PROTEIN KINASE REGULATORY CHAIN TYPE I. CC -!- DEVELOPMENTAL STAGE: IN PUPAE AND IN ADULTS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X16962; CAA34836.1; -. DR EMBL; AE003592; AAF51647.1; -. DR PIR; B31751; B31751. DR FlyBase; FBgn0000093; Mst77F. SQ SEQUENCE 215 AA; 24472 MW; 8199C152FA39ACEF CRC64; MSNLKQKDSK PEVAVTKSVK TYKKSIEYVN SDASDIEEDI NRAEDEYASS SGFVNFLRDF KKRYGEYYSN NEIRRAAETR WNEMSFRHRC QYSAEPLDTF HVEPNSVSSL QRSSEGEHRM HSEISGCADT FFGAGGSNSC TPRKENKCSK PRVRKSCPKP RAKTSKQRRS CGKPKPKGAR PRKACPRPRK KMECGKAKAK PRCLKPKSSK PKCSM // ID 18K1_MYCAV STANDARD; PRT; 147 AA. AC P46729; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 18 kDa antigen 1 (Clone MAVC124). OS Mycobacterium avium. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1764; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SEROVAR 2; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: NOT KNOWN. THIS PROTEIN IS ONE OF THE MAJOR IMMUNE CC REACTIVE PROTEINS IN MYCOBACTERIA. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12236; AAA25341.1; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Multigene family. SQ SEQUENCE 147 AA; 16544 MW; 4EFCBD131AB53999 CRC64; MLMRSDPFRE LDRLTNQVLG TPTRPAVMPM DAWRVGRRLV VEFDLPGIDA ESLDIDIERN VLTVRAERPA LDPNREMLAT ERPRGVFSRE LVLGDNLDTD KIEASYRDGV LSLHIPVDEK ARPRKIAVGA ARHPEPSPKT AREVVNA // ID 18K1_MYCIT STANDARD; PRT; 149 AA. AC P46730; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 18 kDa antigen 1 (Clone MINTC73). OS Mycobacterium intracellulare. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1767; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DARDEN / SEROVAR 19; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: NOT KNOWN. THIS PROTEIN IS ONE OF THE MAJOR IMMUNE CC REACTIVE PROTEINS IN MYCOBACTERIA. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12240; AAA25348.1; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Multigene family. SQ SEQUENCE 149 AA; 16509 MW; 7101A31AC98964D4 CRC64; MLMRSDPFRE LDRFAHQVLG TAARPAVMPM DAWRQGEEFV VEFDLPGIDA DSLDIDIERN VVTVRAERPA LDPNREMLAT ERPRGVFSRQ LVLGENLDTD KIQASYSEGV LSLHIPVAEK AKPRKIAVGR GDGHHAVAEG AAQREVINA // ID 18K2_MYCAV STANDARD; PRT; 138 AA. AC P46731; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 18 kDa antigen 2 (Clone MAVC83). OS Mycobacterium avium. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1764; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SEROVAR 2; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: NOT KNOWN. THIS PROTEIN IS ONE OF THE MAJOR IMMUNE CC REACTIVE PROTEINS IN MYCOBACTERIA. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12237; AAA25349.1; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Multigene family. SQ SEQUENCE 138 AA; 15949 MW; 568CCB098A67E769 CRC64; MVLMRTDPFR DLDRWTQQVL GTRRPAVMPM DAWRDGDQFV VEFDLPGVNA DSLDLDVERN VLTVRAERPD LDQNREMVSA ERPRGVFSRQ LFLGDNLDTD KIEANYHDGV LRLTIPVAEK AKPRRIEINH NHRTAINA // ID 18K2_MYCIT STANDARD; PRT; 140 AA. AC P46732; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 18 kDa antigen 2 (Clone MINTC541). OS Mycobacterium intracellulare. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1767; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DARDEN / SEROVAR 19; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- FUNCTION: NOT KNOWN. THIS PROTEIN IS ONE OF THE MAJOR IMMUNE CC REACTIVE PROTEINS IN MYCOBACTERIA. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12239; AAA25347.1; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Multigene family. SQ SEQUENCE 140 AA; 15749 MW; 4CCCB07BE235600E CRC64; MLVRSDPFRD LDRFTQQLSG TAARPAAMPM DAWRDGEQFV VEFDLPGIDE QSLDLDIERN VVTVRAERPD VDPSREMLAT ERARGVFSRQ LVLGDNLDTE HIDACYDAGV LRLRIPVAEK AKPRKIAVNR GDRQQTAISA // ID 18KD_MYCLE STANDARD; PRT; 148 AA. AC P12809; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 18 kDa antigen (HSP 16.7). GN HSP18 OR ML1795. OS Mycobacterium leprae. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89053927; PubMed=3056923; RA Nerland A.H., Mustafa A.S., Sweetser D., Godal T., Young R.A.; RT "A protein antigen of Mycobacterium leprae is related to a family of RT small heat shock proteins."; RL J. Bacteriol. 170:5919-5921(1988). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88088878; PubMed=2447183; RA Booth R.J., Harris D.P., Love J.M., Watson J.D.; RT "Antigenic proteins of Mycobacterium leprae. Complete sequence of the RT gene for the 18-kDa protein."; RL J. Immunol. 140:597-601(1988). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C., Harris D., RA Mungall K., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L., Oliver K., Quail M.A., Rajandream M.-A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- FUNCTION: NOT KNOWN. THIS PROTEIN IS ONE OF THE MAJOR IMMUNE CC REACTIVE PROTEINS IN MYCOBACTERIA. CC -!- SIMILARITY: BELONGS TO THE SMALL HEAT SHOCK PROTEIN (HSP20) CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22587; AAA25343.1; -. DR EMBL; M19058; AAA88229.1; -. DR EMBL; AL583923; CAC30748.1; -. DR PIR; A27586; A27586. DR PIR; A27649; A27649. DR Leproma; ML1795; -. DR InterPro; IPR002068; Crystallin_HSP20. DR Pfam; PF00011; HSP20; 1. DR PROSITE; PS01031; HSP20; 1. KW Antigen; Complete proteome. FT CONFLICT 13 20 RFAEQVLG -> LRRASVS (IN REF. 1). FT CONFLICT 100 100 E -> Q (IN REF. 1). SQ SEQUENCE 148 AA; 16707 MW; 82B11CC40845C391 CRC64; MLMRTDPFRE LDRFAEQVLG TSARPAVMPM DAWREGEEFV VEFDLPGIKA DSLDIDIERN VVTVRAERPG VDPDREMLAA ERPRGVFNRQ LVLGENLDTE RILASYQEGV LKLSIPVAER AKPRKISVDR GNNGHQTINK TAHEIIDA // ID 194K_TRVSY STANDARD; PRT; 1707 AA. AC P05080; DT 13-AUG-1987 (Rel. 05, Created) DT 01-JUL-1989 (Rel. 11, Last sequence update) DT 01-JUL-1989 (Rel. 11, Last annotation update) DE Potential 194 kDa protein (Putative replicase) [Contains: 134 kDa DE protein]. OS Tobacco rattle virus (strain SYM). OC Viruses; ssRNA positive-strand viruses, no DNA stage; Tobravirus. OX NCBI_TaxID=12298; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88034943; PubMed=3668507; RA Hamilton W.D.O., Boccara M., Robinson D.J., Baulcombe D.C.; RT "The complete nucleotide sequence of tobacco rattle virus RNA-1."; RL J. Gen. Virol. 68:2563-2575(1987). RN [2] RP PARTIAL SEQUENCE FROM N.A. RA Boccara M., Hamilton W.D.O., Baulcombe D.C.; RT "The organisation and interviral homologies of genes at the 3' end of RT tobacco rattle virus RNA1."; RL EMBO J. 5:223-229(1986). CC -!- SIMILARITY: THIS PROTEIN IS HOMOLOG TO PUTATIVE REPLICASE OF CC TOBACCO MOSAIC VIRUS (TMV) AND TRICORNAVIRUSES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X06172; CAA29537.1; -. DR EMBL; D00155; BAA00110.1; -. DR PIR; S01865; S01865. DR InterPro; IPR001788; RNA_dep_RNApol2. DR InterPro; IPR002588; V_methyltransf. DR InterPro; IPR000606; Viral_helicase1. DR Pfam; PF00978; RNA_dep_RNApol2; 1. DR Pfam; PF01443; Viral_helicase1; 1. DR Pfam; PF01660; Vmethyltransf; 1. FT CHAIN 1 1187 134 KDA PROTEIN. FT CHAIN 1 1707 194 KDA PROTEIN. SQ SEQUENCE 1707 AA; 194328 MW; F4DABDB6C7F51F04 CRC64; MANGNFKLSQ LLNVDEMSAE QRSHFFDLML TKPDCEIGQM MQRVVVDKVD DMIRERKTKD PVIVHEVLSQ KEQNKLMEIY PEFNIVFKDD KNMVHGFAAA ERKLQALLLL DRVPALQEVD DIGGQWSFWV TRGEKRIHSC CPNLDIRDDQ REISRQIFLT AIGDQARSGK RQMSENELWM YDQFRKNIAA PNAVRCNNTY QGCTCRGFSD GKKKGAQYAI ALHSLYDFKL KDLMATMVEK KTKVVHAAML FAPESMLVDE GPLPSVDGYY MKKNGKIYFG FEKDPSFSYI HDWEEYKKYL LGKPVSYQGN VFYFEPWQVR GDTMLFSIYR IAGVPRRSLS SQEYYRRIYI SRWENMVVVP IFDLVESTRE LVKKDLFVEK QFMDKCLDYI ARLSDQQLTI SNVKSYLSSN NWVLFINGAA VKNKQSVDSR DLQLLAQTLL VKEQVARPVM RELREAILTE TKPITSLTDV LGLISRKLWK QFANKIAVGG FVGMVGTLIG FYPKKVLTWA KDTPNGPELC YENSHKTKVI VFLSVVYAIG GITLMRRDIR DGLVKKLCDM FDIKRGAHVL DVENPCRYYE INDFFSSLYS ASESGETVLP DLSEVKAKSD KLLQQKKEIA DEFLSAKFSN YSGSSVRTSP PSVVGSSRSG LGLLLEDSNV LTQARVGVSR KVDDEEIMEQ FLSGLIDTEA EIDEVVSAFS AECERGETSG TKVLCKPLTP PGFENVLPAV KPLVSKGKTV KRVDYFQVMG GERLPKRPVV SGDNSVDARR EFLYYLDAER VAQNDEIMSL YRDYSRGVIR TGGQNYPHGL GVWDVEMKNW CIRPVVTEHA YVFQPDKRMD DWSGYLEVAV WERGMLVNDF AVERMSDYVI VCDQTYLCNN RLILDNLSAL DLGPVNCSFE LVDGVPGCGK STMIVNSANP CVDVVLSTGR AATDDLIERF ASKGFPCKLK RRVKTVDSFL MHCVDGSLTG DVLHFDEALM AHAGMVYFCA QIAGAKRCIC QGDQNQISFK PRVSQVDLRF SSLVGKFDIV TEKRETYRSP ADVAAVLNKY YTGDVRTHNA TANSMTVRKI VSKEQVSLKP GAQYITFLQS EKKELVNLLA LRKVAAKVST VHESQGETFK DVVLVRTKPT DDSIARGREY LIVALSRHTQ SLVYETVKED DVSKEIRESA ALTKAALARF FVTETVLXRF RSRFDVFRHH EGPCAVPDSG TITDLEMWYD ALFPGNSLRD SSLDGYLVAT TDCNLRLDNV TIKSGNWKDK FAEKETFLKP VIRTAMPDKR KTTQLESLLA LQKRNQAAPD LQENVHATVL IEETMKKLKS VVYDVGKIRA DPIVNRAQME RWWRNQSTAV QAKVVADVRE LHEIDYSSYM YMIKSDVKPK TDLTPQFEYS ALQTVVYHEK LINSLFGPIF KEINERKLDA MQPHFVFNTR MTSSDLNDRV KFLNTEAAYD FVEIDMSKFD KSANRFHLQL QLEIYRLFGL DEWAAFLWEV SHTQTTVRDI QNGMMAHIWY QQKSGDADTY NANSDRTLCA LLSELPLEKA VMVTYGGDDS LIAFPRGTQF VDPCPKLATK WNFECKIFKY DVPMFCGKFL LKTSSCYEFV PDPVKVLTKL GKKSIKDVQH LAEIYISLND SNRALGNYMV VSKLSESVSD RYLYKGDSVH ALCALWKHIK SFTALCTLFR DENDKELNPA KVDWKKAQRA VSNFYDW // ID 19KD_MYCAV STANDARD; PRT; 161 AA. AC P46733; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 19 kDa lipoprotein antigen precursor. OS Mycobacterium avium. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1764; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SEROVAR 2; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -!- SIMILARITY: TO OTHER MYCOBACTERIUM 19 KDA ANTIGEN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12235; AAA25346.1; -. DR InterPro; IPR000437; Prok_lipoprot. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; FALSE_NEG. KW Antigen; Membrane; Lipoprotein; Signal. FT SIGNAL 1 21 PROBABLE. FT CHAIN 22 161 19 KDA LIPOPROTEIN ANTIGEN. FT LIPID 22 22 N-ACYL DIGLYCERIDE (PROBABLE). SQ SEQUENCE 161 AA; 15504 MW; 78A180B1A1C100E4 CRC64; MNRQLRFAVA GPEILAAVVS GCSSGNKSAP SSSASSSSTS PSASSGGAAG TKVIIDGKDQ NVSGSVVCTN AGGTVNIAIG GAATGIAAVL SDGNPPQVKS VGLGNVNGVT LGYTSGTGQG NASAEKNGNS YKITGTATGV DMANPLQPVN KPFEIDVTCN S // ID 19KD_MYCIT STANDARD; PRT; 162 AA. AC P31502; DT 01-JUL-1993 (Rel. 26, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 01-FEB-1996 (Rel. 33, Last annotation update) DE 19 kDa lipoprotein antigen precursor (22 kDa lipoprotein antigen) DE (MI22 antigen). GN MI22. OS Mycobacterium intracellulare. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1767; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DARDEN / SEROVAR 19; RX MEDLINE=93202760; PubMed=8454357; RA Booth R.J., Williams D.L., Moudgil K.D., Noonan L.C., RA Grandison P.M., McKee J.J., Prestidge R.L., Watson J.D.; RT "Homologs of Mycobacterium leprae 18-kilodalton and Mycobacterium RT tuberculosis 19-kilodalton antigens in other mycobacteria."; RL Infect. Immun. 61:1509-1515(1993). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=SEROVAR 14; RX MEDLINE=92326626; PubMed=1445568; RA Nair J., Rouse D.A., Morris S.L.; RT "Nucleotide sequence analysis and serologic characterization of the RT Mycobacterium intracellulare homologue of the Mycobacterium RT tuberculosis 19 kDa antigen."; RL Mol. Microbiol. 6:1431-1439(1992). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -!- SIMILARITY: TO OTHER MYCOBACTERIUM 19 KDA ANTIGEN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L12238; AAA25344.1; -. DR EMBL; X65483; CAA46469.1; -. DR PIR; S22630; S22630. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal. FT SIGNAL 1 21 PROBABLE. FT CHAIN 22 162 19 KDA LIPOPROTEIN ANTIGEN. FT LIPID 22 22 N-ACYL DIGLYCERIDE (PROBABLE). FT CONFLICT 37 37 N -> S (IN REF. 2). FT CONFLICT 42 48 TRRLAPG -> SASASTGG (IN REF. 2). SQ SEQUENCE 162 AA; 15517 MW; A38EC8100D8870C5 CRC64; MKRQLTVAVA GAAILAAGIS GCSGGNKSGT SASSSANSSG TTRRLAPGAA GTKVTIDGKD QNVSGSVVCT NAGGTINIAI GGAATGIAAV LSDGNPPQVK SVGLGNVNGV TLGYTSGTGQ GNATASKDGN SYKISGTATG VDMANPMQPV NKPFEINVTC NS // ID 19KD_MYCTU STANDARD; PRT; 159 AA. AC P11572; DT 01-OCT-1989 (Rel. 12, Created) DT 01-OCT-1989 (Rel. 12, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 19 kDa lipoprotein antigen precursor. GN LPQH OR RV3763 OR MT3870 OR MTV025.111. OS Mycobacterium tuberculosis, and OS Mycobacterium bovis. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1773, 1765; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=M.tuberculosis; STRAIN=ERDMANN; RX MEDLINE=89160253; PubMed=2493628; RA Ashbridge K.R.; RT "Nucleotide sequence of the 19 kDa antigen gene from Mycobacterium RT tuberculosis."; RL Nucleic Acids Res. 17:1249-1249(1989). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=M.tuberculosis; RX MEDLINE=88248003; PubMed=3132709; RA Young D., Lathigra R., Hendrix R., Sweetser D., Young R.A.; RT "Stress proteins are immune targets in leprosy and tuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4267-4270(1988). RN [3] RP SEQUENCE FROM N.A. RC SPECIES=M.tuberculosis; STRAIN=H37RV; RX MEDLINE=98295987; PubMed=9634230; RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., RA Badcock K., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R., Devlin K., Feltwell T., Gentles S., Hamlin N., Holroyd S., RA Hornsby T., Jagels K., Krogh A., McLean J., Moule S., Murphy L., RA Oliver S., Osborne J., Quail M.A., Rajandream M.A., Rogers J., RA Rutter S., Seeger K., Skelton S., Squares S., Squares R., RA Sulston J.E., Taylor K., Whitehead S., Barrell B.G.; RT "Deciphering the biology of Mycobacterium tuberculosis from the RT complete genome sequence."; RL Nature 393:537-544(1998). RN [4] RP SEQUENCE FROM N.A. RC SPECIES=M.tuberculosis; STRAIN=CDC 1551 / Oshkosh; RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O., RA Peterson J., DeBoy R., Dodson R., Gwinn M.L., Haft D., Hickey E., RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L., RA Delcher A., Utterback T., Weidman J., Khouri H., Gill J., Mikula A., RA Bishai W.; RT "Whole genome comparison of Mycobacterium tuberculosis clinical and RT laboratory strains."; RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE FROM N.A. RC SPECIES=M.bovis; STRAIN=ISOLATE 381/79; RX MEDLINE=91037946; PubMed=2230723; RA Collins M., Patki A., Wall S., Nolan A., Goodger J., Woodward M., RA Dale J.; RT "Cloning and characterization of the gene for the '19 kDa' antigen of RT Mycobacterium bovis."; RL J. Gen. Microbiol. 136:1429-1436(1990). CC -!- SUBCELLULAR LOCATION: ATTACHED TO THE MEMBRANE BY A LIPID CC ANCHOR (PROBABLE). CC -!- SIMILARITY: TO OTHER MYCOBACTERIUM 19 KDA ANTIGEN. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X07945; CAA30766.1; -. DR EMBL; J03838; AAA25353.1; -. DR EMBL; AL022121; CAA18085.1; -. DR EMBL; AE007181; AAK48234.1; -. DR EMBL; X15803; CAA33802.1; -. DR PIR; S02753; S02753. DR PIR; S11234; S11234. DR TIGR; MT3870; -. DR TubercuList; Rv3763; -. DR PROSITE; PS00013; PROKAR_LIPOPROTEIN; 1. KW Antigen; Membrane; Lipoprotein; Signal; Complete proteome. FT SIGNAL 1 21 PROBABLE. FT CHAIN 22 159 19 KDA LIPOPROTEIN ANTIGEN. FT LIPID 22 22 N-ACYL DIGLYCERIDE (PROBABLE). FT CONFLICT 158 158 C -> S (IN REF. 4). SQ SEQUENCE 159 AA; 15147 MW; CB1A5090E14867BB CRC64; MKRGLTVAVA GAAILVAGLS GCSSNKSTTG SGETTTAAGT TASPGAASGP KVVIDGKDQN VTGSVVCTTA AGNVNIAIGG AATGIAAVLT DGNPPEVKSV GLGNVNGVTL GYTSGTGQGN ASATKDGSHY KITGTATGVD MANPMSPVNK SFEIEVTCS // ID 1A01_GORGO STANDARD; PRT; 365 AA. AC P30375; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-A0101 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60258; CAA42810.1; -. DR PIR; JH0534; JH0534. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-A0101 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40829 MW; FB1B14BCD4DF63A8 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGTCVE WLRRHLENGK ETLQRTDAPK THMTHHAVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A01_HUMAN STANDARD; PRT; 365 AA. AC P30443; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-1 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*0101). RX MEDLINE=88234547; PubMed=3375250; RA Parham P., Lomen C.E., Lawlor D.A., Ways J.P., Holmes N., Coppin H.L., RA Salter R.D., Wan A.M., Ennis P.D.; RT "Nature of polymorphism in HLA-A, -B, and -C molecules."; RL Proc. Natl. Acad. Sci. U.S.A. 85:4005-4009(1988). RN [2] RP SEQUENCE FROM N.A. (A*0101). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [3] RP SEQUENCE FROM N.A. (A*0101). RA Warren E.; RL Submitted (APR-1989) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (A*0101). RX MEDLINE=91067475; PubMed=2251137; RA Girdlestone J.; RT "Nucleotide sequence of an HLA-A1 gene."; RL Nucleic Acids Res. 18:6701-6701(1990). RN [5] RP SEQUENCE FROM N.A. (A*0101). RX MEDLINE=98007773; PubMed=9349617; RA Laforet M., Froelich N., Parissiadis A., Pfeiffer B., Schell A., RA Faller B., Woehl-Jaegle M.L., Cazenave J.P., Tongio M.M.; RT "A nucleotide insertion in exon 4 is responsible for the absence of RT expression of an HLA-A*01 allele."; RL Tissue Antigens 50:347-350(1997). RN [6] RP SEQUENCE FROM N.A. (A*0101). RA Waller M.J.; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. (A*0102). RX MEDLINE=95282145; PubMed=7761977; RA Browning M.J., Madrigal J.A., Krausa P., Kowalski H., RA Allsopp C.E., Little A.M., Turner S., Adams E.J., Arnett K.L., RA Bodmer W.F., Parham P.; RT "The HLA-A,B,C genotype of the class I negative cell line Daudi RT reveals novel HLA-A and -B alleles."; RL Tissue Antigens 45:177-187(1995). RN [8] RP SULFATION. RX MEDLINE=88088800; PubMed=3121736; RA Sant A.J., Zacheis M., Rumbarger T., Giacoletto K.S., Schwartz B.D.; RT "Human Ia alpha- and beta-chains are sulfated."; RL J. Immunol. 140:155-160(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- PTM: SULFATED. CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-1 ARE KNOWN: A*0101 AND CC A*0102. THE SEQUENCE SHOWN IS THAT OF A*0101. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24043; AAA59652.1; -. DR EMBL; X55710; CAA39243.1; -. DR EMBL; Z93949; CAB07989.1; -. DR EMBL; U07161; AAA80569.1; -. DR EMBL; AJ278305; CAB93537.1; -. DR PIR; S14189; S14189. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Sulfation; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-1 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT MOD_RES 83 83 SULFATION (POTENTIAL). FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 33 33 F -> S (IN A*0102). FT /FTId=VAR_004332. FT VARIANT 41 41 R -> S (IN A*0102). FT /FTId=VAR_004333. SQ SEQUENCE 365 AA; 40846 MW; 8667AFF3F06C4932 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR RVYLEGRCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A01_PANTR STANDARD; PRT; 365 AA. AC P16209; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, A-2 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30678; AAA87970.1; -. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-2 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40848 MW; FC452786BD038D3E CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETRS AKAHSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQR RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A01_PONPY STANDARD; PRT; 365 AA. AC P16211; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Class I histocompatibility antigen, A-1 alpha chain precursor. OS Pongo pygmaeus (Orangutan). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pongo. OX NCBI_TaxID=9600; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30680; AAA88835.1; -. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-1 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40658 MW; 11A5BC183009CF70 CRC64; MAIMAPRTLL LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRTPWMEQEG PEYWDRETRS VKAHAQTNRV DLGTLRGYYN QSDGGSHTIQ RMFGCDVGPD GRFLRGYEQH AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAGAAEQD RAYLEGLCVE SLRRYLENGK ETLQRTDAPK THMTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGKEQR YTCHVQHEGL PEPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRRNSDRK GGSYSQAASN DSAQGSDVSL TACKV // ID 1A01_SAGOE STANDARD; PRT; 365 AA. AC P30515; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, A alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Platyrrhini; Callitrichidae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33475; AAA36951.1; -. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40973 MW; B34B24FB6848E373 CRC64; MTVMAPRTLL LLLSGALVLT ETWAGSHSMR YFETSVSRPG RGEPRYISVG YVDDTQFVRF DSDAASPRME PRAPWMEQEG PEYWEEETRK GKADAQTFRV DLQTLLGYYN QSEAGSHTIQ WMYGCDLGPD GRLLRGYDQH AYDGKDYIAL NEDLRSWTAT DVAAQITQRK WEAANEAERT RAYLEGTCVE WLHRYLENGK ETLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITVT WQRDGEDQTQ DMELVETRPA GDGTFQKWAA VVVLSGEEQR YTCHVQHEGL PEPLTLRWEP PSQPTIPIMG IVAILAILGV VVTGAVVAAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1A02_GORGO STANDARD; PRT; 365 AA. AC P30376; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-A0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60259; CAA42811.1; -. DR PIR; JH0535; JH0535. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-A0201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40895 MW; 09E0E5FCD8E58507 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEE PEYWDGETRK VKAHSQTDRV NLGTLRGYYN QSEAGSHTIQ KMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGECVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHESL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVIAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A02_HUMAN STANDARD; PRT; 365 AA. AC P01892; P06338; P30514; P30444; P30445; P30446; Q29680; Q29899; AC Q95352; Q29837; Q95380; DT 21-JUL-1986 (Rel. 01, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-2 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*0201). RX MEDLINE=85132727; PubMed=2982951; RA Koller B.H., Orr H.T.; RT "Cloning and complete sequence of an HLA-A2 gene: analysis of two RT HLA-A alleles at the nucleotide level."; RL J. Immunol. 134:2727-2733(1985). RN [2] RP SEQUENCE FROM N.A. (A*0201). RX MEDLINE=89122144; PubMed=2914713; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., RA Boccoli G., Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [3] RP SEQUENCE FROM N.A. (A*0201). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [4] RP SEQUENCE FROM N.A. (A*0201/A*0211/A*0212). RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP SEQUENCE OF 39-365 FROM N.A. (A*0201). RX MEDLINE=85230571; PubMed=3874058; RA Krangel M.S.; RT "Unusual RNA splicing generates a secreted form of HLA-A2 in a RT mutagenized B lymphoblastoid cell line."; RL EMBO J. 4:1205-1210(1985). RN [6] RP SEQUENCE OF 25-295 (A*0201). RX MEDLINE=80056745; PubMed=92029; RA Orr H.T., Lopez de Castro J.A., Parham P., Ploegh H.L., RA Strominger J.L.; RT "Comparison of amino acid sequences of two human histocompatibility RT antigens, HLA-A2 and HLA-B7: location of putative alloantigenic RT sites."; RL Proc. Natl. Acad. Sci. U.S.A. 76:4395-4399(1979). RN [7] RP REVISIONS (A*0201). RX MEDLINE=82247941; PubMed=6179086; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [8] RP SEQUENCE OF 26-298 FROM N.A. (A*0202/A*0203). RX MEDLINE=87306734; PubMed=3497874; RA Mattson D.H., Handy D.E., Bradley D.A., Coligan J.E., Cowan E.P., RA Biddison W.E.; RT "DNA sequences of the genes that encode the CTL-defined HLA-A2 RT variants M7 and DK1."; RL Immunogenetics 26:190-192(1987). RN [9] RP SEQUENCE FROM N.A. (A*0203/A*0205). RX MEDLINE=87252273; PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of RT the HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [10] RP SEQUENCE FROM N.A. (A*0203/A*0205). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [11] RP SEQUENCE OF 9-365 FROM N.A. (A*0204). RX MEDLINE=92039809; PubMed=1937577; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0204 antigen, found in South American RT Indians. Spatial clustering of HLA-A2 subtype polymorphism."; RL Immunogenetics 34:281-285(1991). RN [12] RP SEQUENCE OF 9-365 FROM N.A. (A*0204). RX MEDLINE=92269956; PubMed=1589035; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [13] RP SEQUENCE FROM N.A. (A*0206). RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [14] RP PARTIAL SEQUENCE (A*0206). RX MEDLINE=86305811; PubMed=3489037; RA Ezquerra A., Domenech N., van der Poel J., Strominger J.L., Vega M.A., RA Lopez de Castro J.A.; RT "Molecular analysis of an HLA-A2 functional variant CLA defined by RT cytolytic T lymphocytes."; RL J. Immunol. 137:1642-1649(1986). RN [15] RP PARTIAL SEQUENCE (A*0207). RX MEDLINE=88113844; PubMed=2448239; RA Domenech N., Ezquerra A., Castano R., Lopez de Castro J.A.; RT "Structural analysis of HLA-A2.4 functional variant KNE. Implications RT for the mapping of HLA-A2-specific T-cell epitopes."; RL Immunogenetics 27:196-202(1988). RN [16] RP PARTIAL SEQUENCE (A*0208). RX MEDLINE=88314183; PubMed=2457548; RA Domenech N., Castano R., Goulmy E., Lopez de Castro J.A.; RT "Molecular analysis of HLA-A2.4 functional variant KLO: close RT structural and evolutionary relatedness to the HLA-A2.2 subtype."; RL Immunogenetics 28:143-152(1988). RN [17] RP PARTIAL SEQUENCE (A*0209). RX MEDLINE=88186100; PubMed=3258580; RA Castano R., Ezquerra A., Domenech N., Lopez de Castro J.A.; RT "An HLA-A2 population variant with structural polymorphism in the RT alpha 3 region."; RL Immunogenetics 27:345-355(1988). RN [18] RP SEQUENCE FROM N.A. (A*0210). RX MEDLINE=89122133; PubMed=2783680; RA Epstein H., Kennedy L., Holmes N.; RT "An Oriental HLA-A2 subtype is closely related to a subset of RT Caucasoid HLA-A2 alleles."; RL Immunogenetics 29:112-116(1989). RN [19] RP SEQUENCE OF 9-365 FROM N.A. (A*0211). RX MEDLINE=92218010; PubMed=1559719; RA Castano A.R., Lopez de Castro J.A.; RT "Structure of the HLA-A*0211 (A2.5) subtype: further evidence for RT selection-driven diversification of HLA-A2 antigens."; RL Immunogenetics 35:344-346(1992). RN [20] RP SEQUENCE FROM N.A. (A*0213). RX MEDLINE=94222455; PubMed=8168863; RA Barber D.F., Fernandez J.M., Lopez de Castro J.A.; RT "Primary structure of a new HLA-A2 subtype: HLA-A*0213."; RL Immunogenetics 39:378-378(1994). RN [21] RP SEQUENCE FROM N.A. (A*0216). RX MEDLINE=95278976; PubMed=7759139; RA Barouch D., Krausa P., Bodmer J., Browning M.J., McMichael A.J.; RT "Identification of a novel HLA-A2 subtype, HLA-A*0216."; RL Immunogenetics 41:388-388(1995). RN [22] RP SEQUENCE FROM N.A. (A*0217). RC TISSUE=Blood; RX MEDLINE=95381236; PubMed=7652742; RA Selvakumar A., Granja C.B., Salazar M., Alosco S.M., Yunis E.J., RA Dupont B.; RT "A novel subtype of A2 (A*0217) isolated from the South American RT Indian B-cell line AMALA."; RL Tissue Antigens 45:343-347(1995). RN [23] RP SEQUENCE FROM N.A. (A*0218). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Oohashi H., Hashimoto M., RA Akaza T., Tadokoro K., Juji T.; RT "A new A2 sequence HLA-A2K from Japanese."; RL Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases. RN [24] RP SEQUENCE FROM N.A. (A*0220). RC TISSUE=Blood; RX MEDLINE=97161038; PubMed=9008310; RA Fleischhauer K., Zino E., Mazzi B., Severini G.M., Benazzi E., RA Bordignon C.; RT "HLA-A*02 subtype distribution in Caucasians from northern Italy: RT identification of A*0220."; RL Tissue Antigens 48:673-679(1996). RN [25] RP SEQUENCE FROM N.A. (A*0221). RC TISSUE=Blood; RA Szmania S., Baxter-Lowe L.A.; RT "Nucleotide sequence of a novel HLA-A2 gene."; RL Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases. RN [26] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF A*0201. RX MEDLINE=88014204; PubMed=3309677; RA Bjorkman P.J., Saper M.A., Samraoui B., Bennett W.S., RA Strominger J.L., Wiley D.C.; RT "Structure of the human class I histocompatibility antigen, HLA-A2."; RL Nature 329:506-512(1987). RN [27] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF A*0201. RX MEDLINE=91245570; PubMed=2038058; RA Saper M.A., Bjorkman P.J., Wiley D.C.; RT "Refined structure of the human histocompatibility antigen HLA-A2 at RT 2.6-A resolution."; RL J. Mol. Biol. 219:277-319(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-2 ARE KNOWN: A*0201, CC A*0202, A*0203, A*0204, A*0205, A*0206 (A2.4A), A*0207, A*0208, CC A*0209, A*0210, A*0211 (A2.5), A*0212, A*0213 (A*02SLU), A*0216, CC A*0217, A*0218 (A2K), A*0219, A*0220 AND A*0221. THE SEQUENCE CC SHOWN IS THAT OF A*0201. CC -!- CAUTION: REF.6 AND REF.7 SEQUENCES DIFFER FROM THAT SHOWN CC EXTENSIVELY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; K02883; AAA98727.1; -. DR EMBL; M84379; AAA59606.1; -. DR EMBL; X02457; CAA26297.1; -. DR EMBL; M19670; AAA03683.2; -. DR EMBL; M17690; AAB02120.1; -. DR EMBL; U03863; AAA03604.1; -. DR EMBL; M86404; -; NOT_ANNOTATED_CDS. DR EMBL; X57954; CAA41022.1; ALT_SEQ. DR EMBL; U03862; AAA03603.1; -. DR EMBL; M24042; AAA59653.1; -. DR EMBL; Z23071; CAA80612.1; -. DR EMBL; M84377; AAA59603.1; -. DR EMBL; X60764; -; NOT_ANNOTATED_CDS. DR EMBL; M84378; AAA59604.1; -. DR EMBL; Z27120; CAA81644.1; -. DR EMBL; Z46633; CAA86602.1; -. DR EMBL; U18930; AAA87076.1; -. DR EMBL; D83515; BAA11935.1; -. DR EMBL; X96724; CAA65501.1; -. DR EMBL; U56825; AAB17465.1; -. DR PIR; A02188; HLHUA2. DR PIR; A02191; HLHU2A. DR PIR; E35997; E35997. DR PIR; S19020; S19020. DR PIR; S23593; S23593. DR PDB; 1HLA; 15-JUL-90. DR PDB; 3HLA; 15-APR-90. DR PDB; 1HHG; 31-OCT-93. DR PDB; 1HHH; 31-OCT-93. DR PDB; 1HHI; 31-OCT-93. DR PDB; 1HHJ; 31-OCT-93. DR PDB; 1HHK; 31-OCT-93. DR PDB; 1AQD; 28-JAN-98. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism; KW 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-2 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 33 33 F -> Y (IN A*0205, A*0206, A*0208, A*0210 FT AND A*0221). FT /FTId=VAR_004334. FT VARIANT 54 54 D -> N (IN A*0221). FT /FTId=VAR_004335. FT VARIANT 67 67 Q -> R (IN A*0202, A*0205 AND A*0208). FT /FTId=VAR_004336. FT VARIANT 90 90 K -> N (IN A*0208 AND A*0220). FT /FTId=VAR_004337. FT VARIANT 97 98 TH -> ID (IN A*0211). FT /FTId=VAR_004338. FT VARIANT 119 119 V -> L (IN A*0202, A*0205, A*0208 AND FT A*0217). FT /FTId=VAR_004339. FT VARIANT 121 121 R -> M (IN A*0204 AND A*0217). FT /FTId=VAR_004340. FT VARIANT 123 123 Y -> C (IN A*0207 AND A*0218). FT /FTId=VAR_004341. FT VARIANT 123 123 Y -> F (IN A*0210 AND A*0217). FT /FTId=VAR_004342. FT VARIANT 131 131 W -> G (IN A*0210). FT /FTId=VAR_004343. FT VARIANT 162 162 M -> K (IN A*0218). FT /FTId=VAR_004344. FT VARIANT 173 173 A -> T (IN A*0203). FT /FTId=VAR_004345. FT VARIANT 176 176 V -> E (IN A*0203 AND A*0213). FT /FTId=VAR_004346. FT VARIANT 180 180 L -> W (IN A*0202, A*0203, A*0205 AND FT A*0208). FT /FTId=VAR_004347. FT VARIANT 180 180 L -> Q (IN A*0212 AND A*0213). FT /FTId=VAR_004348. FT VARIANT 187 187 T -> E (IN A*0216). FT /FTId=VAR_004349. FT VARIANT 260 260 A -> E (IN A*0209). FT /FTId=VAR_004350. FT STRAND 27 36 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 70 71 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 159 FT TURN 163 163 FT HELIX 164 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 207 207 FT STRAND 210 219 FT TURN 220 221 FT STRAND 222 233 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 247 FT HELIX 249 251 FT STRAND 253 254 FT STRAND 258 259 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 297 SQ SEQUENCE 365 AA; 40922 MW; B54A97B24B337C08 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDGETRK VKAHSQTHRV DLGTLRGYYN QSEAGSHTVQ RMYGCDVGSD WRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A02_PANTR STANDARD; PRT; 362 AA. AC P16210; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, A-5 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30679; AAA87971.1; -. DR HSSP; P30685; 1A9E. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-5 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40487 MW; 9B5A674445037056 CRC64; MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NQDLSSWTAA DTAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1A03_GORGO STANDARD; PRT; 365 AA. AC P30377; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-A0401 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60257; CAA42809.1; -. DR PIR; JH0536; JH0536. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-A0401 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40933 MW; 9207ABBDF9B406C9 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEE PEYWDGETRN MKARSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAHEAEQL RAYLEGTCVE WLRRYLENGK ETLQLTDAPK THMTHHPVSD HEAILRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A03_HUMAN STANDARD; PRT; 370 AA. AC P04439; DT 13-AUG-1987 (Rel. 05, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-3 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*0301). RX MEDLINE=84207948; PubMed=6609814; RA Strachan T., Sodoyer R., Damotte M., Jordan B.R.; RT "Complete nucleotide sequence of a functional class I HLA gene, RT HLA-A3: implications for the evolution of HLA genes."; RL EMBO J. 3:887-894(1984). RN [2] RP SEQUENCE FROM N.A. (A*0302). RX MEDLINE=85290871; PubMed=2993417; RA Cowan E.P., Jordan B.E., Coligan J.E.; RT "Molecular cloning and DNA sequence analysis of genes encoding RT cytotoxic T lymphocyte-defined HLA-A3 subtypes: the E1 subtype."; RL J. Immunol. 135:2835-2841(1985). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-3 ARE KNOWN: A*0301 (A- CC 3.1) AND A*0302. THE SEQUENCE SHOWN IS THAT OF A*0301. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00492; CAA25162.1; ALT_TERM. DR PIR; A02192; HLHUA3. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 29 FT CHAIN 30 370 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-3 ALPHA CHAIN. FT DOMAIN 30 119 EXTRACELLULAR ALPHA-1. FT DOMAIN 120 211 EXTRACELLULAR ALPHA-2. FT DOMAIN 212 303 EXTRACELLULAR ALPHA-3. FT DOMAIN 304 313 CONNECTING PEPTIDE. FT TRANSMEM 314 337 FT DOMAIN 338 370 CYTOPLASMIC TAIL. FT CARBOHYD 115 115 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 130 193 BY SIMILARITY. FT DISULFID 232 288 BY SIMILARITY. FT VARIANT 181 181 E -> V (IN A*0302). FT /FTId=VAR_004351. FT VARIANT 185 185 L -> Q (IN A*0302). FT /FTId=VAR_004352. SQ SEQUENCE 370 AA; 41368 MW; ABB1FA77460318A2 CRC64; MARGDQAVMA PRTLLLLLSG ALALTQTWAG SHSMRYFFTS VSRPGRGEPR FIAVGYVDDT QFVRFDSDAA SQRMEPRAPW IEQEGPEYWD QETRNVKAQS QTDRVDLGTL RGYYNQSEAG SHTIQIMYGC DVGSDGRFLR GYRQDAYDGK DYIALNEDLR SWTAADMAAQ ITKRKWEAAH EAEQLRAYLD GTCVEWLRRY LENGKETLQR TDPPKTHMTH HPISDHEATL RCWALGFYPA EITLTWQRDG EDQTQDTELV ETRPAGDGTF QKWAAVVVPS GEEQRYTCHV QHEGLPKPLT LRWELSSQPT IPIVGIIAGL VLLGAVITGA VVAAVMWRRK SSDRKGGSYT QAASSDSAQG SDVSLTACKV // ID 1A03_PANTR STANDARD; PRT; 365 AA. AC P13748; DT 01-JAN-1990 (Rel. 13, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, A-108 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., RA Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13113; CAA31505.1; ALT_INIT. DR PIR; S03535; S03535. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-108 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40822 MW; 48CC757055221FC3 CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN MKASAQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA AMAAQITKRK WEAAHAAEQL RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAVITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A04_GORGO STANDARD; PRT; 365 AA. AC P30378; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-A0501 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60256; CAA42808.1; -. DR PIR; JH0537; JH0537. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-A0501 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40895 MW; 340DAD21F9B3B8AB CRC64; MAVVAPRTLL LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWMEQEE PEYWDRQTQI SKTNAQIELE SLRIALRYYN QSEDGSHTIQ RMYGCDVGSD GRFLRGYQQD AYDGKDYIAS NEDLRSWTAA DMAAEITKRK WEAAHFAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THTTHQAVSD HEATLKCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A04_PANTR STANDARD; PRT; 365 AA. AC P13749; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, A-126 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., RA Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13114; CAA31506.1; -. DR PIR; S01171; S01171. DR HSSP; Q95352; 1HHH. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-126 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40656 MW; D3C9A810B22A768F CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETRS VKASAQTDRV DLGTLRGYYN QSEDGSHTIQ LMFGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAAHAAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD REATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A11_CUCMA STANDARD; PRT; 493 AA. AC P23599; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase CMW33 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS1 OR ACCW. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP SEQUENCE FROM N.A. RA Nakajima N., Mori H., Yamazaki K., Imaseki H.; RT "Molecular cloning and sequence of a complementary DNA encoding 1- RT aminocyclopropane-1-carboxylate synthase induced by tissue wounding."; RL Plant Cell Physiol. 31:1021-1029(1990). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: BY TISSUE WOUNDING. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D01032; BAA00838.1; -. DR PIR; JQ0926; JQ0926. DR HSSP; P37821; 1B8G. DR Mendel; 244; CUCma;Acs;1. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 493 AA; 55895 MW; F39234AC99CBEF6B CRC64; MEFHQIDERN QALLSKIAVD DGHGENSPYF DGWKAYDNDP FHPEDNPLGV IQMGLAENQL SFDMIVDWIR KHPEASICTP KGLERFKSIA NFQDYHGLPE FRNGIASFMG KVRGGRVQFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IRVHCNSSNN FQVTKAALEI AYKKAQEANI KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFISIAQIV EEMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL AERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRRRENKLR LSFSFSGRRY DEGNVLNSPH TMSPHSPLVI AKN // ID 1A11_CUCPE STANDARD; PRT; 493 AA. AC P23279; DT 01-NOV-1991 (Rel. 20, Created) DT 01-NOV-1991 (Rel. 20, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase 1 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACC1A. OS Cucurbita pepo (Vegetable marrow) (Summer squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3663; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91139670; PubMed=1995630; RA Sato T., Oeller P.W., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase of Cucurbita. RT Purification, properties, expression in Escherichia coli, and primary RT structure determination by DNA sequence analysis."; RL J. Biol. Chem. 266:3752-3759(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91334397; PubMed=1871117; RA Huang P.-L., Parks J.E., Rottman W.H., Theologis A.; RT "Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in RT zucchini (Cucurbita pepo) are clustered and similar but RT differentially regulated."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: BY WOUNDING IN FRUIT AND ETIOLATED HYPOCOTYLS. BY CC INDOLEACETIC ACID (IAA)/BENYLADENINE/LICL ONLY IN FRUIT TISSUE. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58323; AAA33113.1; -. DR EMBL; M61195; AAA33111.1; -. DR PIR; A38649; A38649. DR PIR; A41141; A41141. DR HSSP; P37821; 1B8G. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 279 279 PYRIDOXAL PHOSPHATE. FT CONFLICT 177 177 G -> R (IN REF. 2). SQ SEQUENCE 493 AA; 55779 MW; 921DC3DFB17A8769 CRC64; MGFHQIDERN QALLSKIALD DGHGENSPYF DGWKAYDNDP FHPENNPLGV IQMGLAENQL SFDMIVDWIR KHPEASICTP EGLERFKSIA NFQDYHGLPE FRNAIANFMG KVRGGRVKFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAGFDR DLKWRTRAQI IRVHCNGSNN FQVTKAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRV GERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DEGNVLNSPH TMSPHSPLVI AKN // ID 1A11_HUMAN STANDARD; PRT; 365 AA. AC P13746; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-11 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*1101/A*1102). RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., RA Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP SEQUENCE FROM N.A. (A*1101/A*1102). RX MEDLINE=94287401; PubMed=8016845; RA Lin L., Tokunaga K., Ishikawa Y., Bannai M., Kashiwase K., RA Kuwata S., Akaza T., Tadokoro K., Shibata Y., Juji T.; RT "Sequence analysis of serological HLA-A11 split antigens, A11.1 and RT A11.2."; RL Tissue Antigens 43:78-82(1994). RN [3] RP SEQUENCE OF 26-365 FROM N.A. (A*1101). RX MEDLINE=87192928; PubMed=2437024; RA Cowan E.P., Jelachich M.L., Biddison W.E., Coligan J.E.; RT "DNA sequence of HLA-A11: remarkable homology with HLA-A3 allows RT identification of residues involved in epitopes recognized by RT antibodies and T cells."; RL Immunogenetics 25:241-250(1987). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-11 ARE KNOWN: A*1101 (A- CC 11E) AND A*1102 (A-11K). THE SEQUENCE SHOWN IS THAT OF A*1101. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13111; CAA31503.1; -. DR EMBL; X13112; CAA31504.1; -. DR EMBL; D16841; BAA04117.1; -. DR EMBL; D16842; BAA04118.1; -. DR EMBL; M16010; AAA65449.1; -. DR EMBL; M16007; AAA65449.1; JOINED. DR EMBL; M16008; AAA65449.1; JOINED. DR EMBL; M16009; AAA65449.1; JOINED. DR PIR; S03536; S03536. DR PIR; S03694; S03694. DR PIR; A47636; A47636. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-11 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 43 43 E -> K (IN A*1102). FT /FTId=VAR_004353. SQ SEQUENCE 365 AA; 40937 MW; FE449CE2D4BF6CC5 CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAAHAAEQQ RAYLEGRCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A11_ORYSA STANDARD; PRT; 487 AA. AC Q07215; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 01-OCT-1994 (Rel. 30, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase 1 (EC 4.4.1.14) (ACC DE synthase 1) (S-adenosyl-L-methionine methylthioadenosine-lyase 1). GN ACC1. OS Oryza sativa (Rice). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; OC Ehrhartoideae; Oryzeae; Oryza. OX NCBI_TaxID=4530; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93283732; PubMed=8389618; RA Zarembinski T.I., Theologis A.; RT "Anaerobiosis and plant growth hormones induce two genes encoding 1- RT aminocyclopropane-1-carboxylate synthase in rice (Oryza sativa L.)."; RL Mol. Biol. Cell 4:363-373(1993). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: BY ANAEROBIOSIS AND INDOLEACETIC ACID (IAA) + CC BENZYLADENINE (BA) + LICL TREATMENT. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M96672; AAA33887.1; -. DR EMBL; M96673; AAA33888.1; -. DR HSSP; P37821; 1B8G. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 286 286 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 129 129 N -> T. FT VARIANT 151 151 F -> L. FT VARIANT 273 273 G -> D. SQ SEQUENCE 487 AA; 53101 MW; 90F8B0DEF3524009 CRC64; MVSQVVAEEK PQLLSKKAGC NSHGQDSSYF LGWQEYEKNP FDPVSNPSGI IQMGLAENQL SFDLLEEWLE KNPHALGLRR EGGGASVFRE LALFQDYHGL PAFKNALARF MSEQRGYKVV FDPSNIVLNA GATSANEALM FCLADHGDAF FIPTPYYPGF DRDLKWRTGA EIVPVHCASA NGFRVTRAAL DDAYRRAQKR RLRVKGVLIT NPSNPLGTAS PRADLETIVD FVAAKGIHLI SDEIYAGTAF AEPPAGFVSA LEVVAGRDGG GAGVSDRVHV VYSLSKDLGL PGFRVGAIYS ANAAVVSAAT KMSSFGLVSS QTQYLLAALL GDRDFTRSYV AENKRRIKER HDQLVDGLRE IGIGCLPSNA GLFCWVDMSH LMRSRSFAGE MELWKKVVFE VGLNISPGSS CHCREPGWFR VCFANMSAKT LDVAMQRLRS FVDSATGGGD NAALRRAAVP VRSVSCPLAI KWALRLTPSI ADRKAER // ID 1A12_ARATH STANDARD; PRT; 496 AA. AC Q06402; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-aminocyclopropane-2-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase 2) (S-adenosyl-L-methionine methylthioadenosine-lyase 2). GN ACS2 OR ACC1 OR AT1G01480 OR F22L4.4. OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids II; Brassicales; Brassicaceae; Arabidopsis. OX NCBI_TaxID=3702; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=93028584; PubMed=1357670; RA van der Straeten D., Rodrigues-Pousada R.A., Villarroel R., Hanley S., RA Goodman H.M., van Montagu M.; RT "Cloning, genetic mapping, and expression analysis of an Arabidopsis RT thaliana gene that encodes 1-aminocyclopropane-1-carboxylate RT synthase."; RL Proc. Natl. Acad. Sci. U.S.A. 89:9969-9973(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=93066381; PubMed=1438312; RA Liang X.-W., Abel S., Keller J.A., Shen N.F., Theologis A.; RT "The 1-aminocyclopropane-1-carboxylate synthase gene family of RT Arabidopsis thaliana."; RL Proc. Natl. Acad. Sci. U.S.A. 89:11046-11050(1992). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RA Terryn N.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. RC STRAIN=CV. COLUMBIA; RX MEDLINE=21016719; PubMed=11130712; RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., RA White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., RA Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., RA Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K., RA Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., RA Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L., RA Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E., RA Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., RA Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P., RA Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A., RA Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I., RA Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D., RA Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M., RA Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D., RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., RA Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.; RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis RT thaliana."; RL Nature 408:816-820(2000). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- TISSUE SPECIFICITY: HIGH IN DEVELOPING LEAVES AND IN FLOWERS. CC -!- INDUCTION: BY ETHYLENE. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z12614; CAA78260.1; -. DR EMBL; M95595; AAB59298.1; -. DR EMBL; M95594; AAA97516.1; -. DR EMBL; Y12776; CAA73310.1; -. DR EMBL; AC061957; AAF81308.1; -. DR PIR; S31646; S31646. DR PIR; A47199; A47199. DR PIR; S46190; S46190. DR HSSP; P37821; 1B8G. DR Mendel; 15544; ARAth;Acs;mn15544. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 136 136 M -> I. SQ SEQUENCE 496 AA; 55531 MW; 766318AE9B5F1566 CRC64; MGLPGKNKGA VLSKIATNNQ HGENSEYFDG WKAYDKDPFH LSRNPHGIIQ MGLAENQLCL DLIKDWVKEN PEASICTLEG IHQFSDIANF QDYHGLKKFR QAIAHFMGKA RGGRVTFDPE RVVMSGGATG ANETIMFCLA DPGDVFLIPS PYYAAFDRDL RWRTGVEIIP VPCSSSDNFK LTVDAAEWAY KKAQESNKKV KGLILTNPSN PLGTMLDKDT LTNLVRFVTR KNIHLVVDEI YAATVFAGGD FVSVAEVVND VDISEVNVDL IHIVYSLSKD MGLPGFRVGI VYSFNDSVVS CARKMSSFGL VSSQTQLMLA SMLSDDQFVD NFLMESSRRL GIRHKVFTTG IKKADIACLT SNAGLFAWMD LRHLLRDRNS FESEIELWHI IIDRVKLNVS PGSSFRCTEP GWFRICFANM DDDTLHVALG RIQDFVSKNK NKIVEKASEN DQVIQNKSAK KLKWTQTNLR LSFRRLYEDG LSSPGIMSPH SPLLRA // ID 1A12_CUCMA STANDARD; PRT; 475 AA. AC Q00257; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase CMA101 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS2 OR PCVV4A. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3661; RN [1] RP SEQUENCE FROM N.A. RA Nakagawa N., Mori H., Yamazaki K., Imaseki H.; RT "Cloning of a complementary DNA for auxin-induced 1-aminocyclopropane- RT 1-carboxylate synthase and differential expression of the gene by RT auxin and wounding."; RL Plant Cell Physiol. 32:1153-1163(1991). RN [2] RP SEQUENCE FROM N.A. RA Nakagawa N., Kamiya Y., Imaseki H.; RT "Nucleotide sequence of an auxin-regulated 1-aminocyclopropane-1- RT carboxylic acid synthase gene from Cucurbita maxima Duch."; RL (In) Plant Gene Register PGR95-110. CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: BY TISSUE WOUNDING AND BY AUXIN. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37774; AAA91152.1; -. DR EMBL; D01033; BAA00839.1; -. DR PIR; JQ2214; JQ2214. DR HSSP; P37821; 1B8G. DR Mendel; 245; CUCma;Acs;2. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 272 272 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 475 AA; 53481 MW; D02A666E137F44A0 CRC64; MKMLSTKATC NSHGQDSSYF LGWEAYENNP FHHTSNPNGI IQMGLAENQL SFDLLESWLS KNPDAASFKR DGKSIFRELA LFQDYHGLPA FKKALVEFMA EIRGNKVSFE ANNIVLTAGA TSANETLMFC LAEAGDAFLL PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITQSALEQ AYKDAQTRNL RVKGVLVTNP SNPLGTTMNR DELNLVFDFI TSKGIHLISD EIYSGTVFGS PGFVSAMEVL KERSSEDEEV WKRVHIVYSL SKDLGLPGFR VGAIYSNDDM VVAAATKMSS FGLVSSQTQY LLSAMLSDKK FTISYISENQ KRLKQRQKML VSGLQKAGIN CLDSNAGLFC WVDMRHLLES DKFESELELW KKIVYEVGLN ISPGSSCHCT EPGWFRVCFA NMSESTLKLA VRRLKSFVTE LRSTTTSNHR NHDNKICKNI KKNIFTKWVF RQSAQEANRK MQAER // ID 1A12_CUCPE STANDARD; PRT; 494 AA. AC Q00379; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS2 OR ACC1B. OS Cucurbita pepo (Vegetable marrow) (Summer squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Cucurbitales; Cucurbitaceae; Cucurbita. OX NCBI_TaxID=3663; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91334397; PubMed=1871117; RA Huang P., Parks J.E., Rottman W.H., Theologis A.; RT "Two genes encoding 1-aminocyclopropane-1-carboxylate synthase in RT zucchini (Cucurbita pepo) are clustered and similar but RT differentially regulated."; RL Proc. Natl. Acad. Sci. U.S.A. 88:7021-7025(1991). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: HORMONES, SUCH AS AUXIN, ENVIRONMENTAL FACTORS, SUCH AS CC MECHANICAL WOUNDING AND A NUMBER OF CHEMICALS. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M61195; AAA33112.1; -. DR PIR; B41141; B41141. DR HSSP; P37821; 1B8G. DR Mendel; 247; CUCpe;Acs;2. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 345 345 A -> AS (IN REF. 1; AAA33112). SQ SEQUENCE 494 AA; 55922 MW; 02AE029AA4912C36 CRC64; MGFHQIDERN QALLSKIAID DGHGENSAYF DGWKAYDNNP FHPENNPLGV IQMGLAENQL SFGMIVDWIR KHPEASICTP EGLEKFKSIA NFQDYHGLQE FRKAMASFMG KVRGGRVKFD PSRIVMGGGA TGASETVIFC LADPGDAFLV PSPYYAAFDR DLKWRTRAQI IPVHCNSSNN FQVTEAALEI AYKKAQEANM KVKGVIITNP SNPLGTTYDR DTLKTLVTFV NQHDIHLICD EIYSATVFKA PTFTSIAEIV EQMEHCKKEL IHILYSLSKD MGLPGFRVGI IYSYNDVVVR RARQMSSFGL VSSQTQHLLA AMLSDEDFVD KFLAENSKRL GERHARFTKE LDKMGITCLN SNAGVFVWMD LRRLLKDQTF KAEMELWRVI INEVKLNVSP GSSFHVTEPG WFRVCFANMD DNTVDVALNR IHSFVENIDK KEDNTVAMPS KTRHRDNKLR LSFSFSGRRY DKGNVLNSPH TMSPHSPLVR ARTY // ID 1A12_LYCES STANDARD; PRT; 485 AA. AC P18485; DT 01-NOV-1990 (Rel. 16, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase 2 (EC 4.4.1.14) (ACC DE synthase 2) (S-adenosyl-L-methionine methylthioadenosine-lyase 2) DE (ACS-2). GN ACS2 OR ACC2 OR PCVV4A. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Etiolated hypocotyl; RX MEDLINE=92106351; PubMed=1762159; RA Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., RA Nagy B.P., Taylor L.P., Campbell A.D., Theologis A.; RT "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a RT multigene family whose transcription is induced during fruit and RT floral senescence."; RL J. Mol. Biol. 222:937-961(1991). RN [2] RP SEQUENCE FROM N.A., AND PARTIAL SEQUENCE. RC STRAIN=CV. ORLANDO; TISSUE=Fruit; RX MEDLINE=90280476; PubMed=2191304; RA van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.; RT "Cloning and sequence of two different cDNAs encoding 1- RT aminocyclopropane-1-carboxylate synthase in tomato."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: HORMONES, SUCH AS AUXIN, ENVIRONMENTAL FACTORS, SUCH AS CC MECHANICAL WOUNDING AND A NUMBER OF CHEMICALS. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X59139; CAA41855.1; -. DR EMBL; X59145; CAA41856.1; -. DR EMBL; M34289; AAA81580.1; -. DR PIR; S19677; S19677. DR PIR; S19678; S19678. DR PIR; A35516; A35516. DR HSSP; P37821; 1B8G. DR Mendel; 509; LYCes;Acs;2. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 278 278 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 124 124 A -> V (IN REF. 1; CAA41856). FT CONFLICT 322 322 L -> P (IN REF. 2). FT CONFLICT 399 399 P -> L (IN REF. 2). SQ SEQUENCE 485 AA; 54662 MW; 40B3F55B5EF0D9C7 CRC64; MGFEIAKTNS ILSKLATNEE HGENSPYFDG WKAYDSDPFH PLKNPNGVIQ MGLAENQLCL DLIEDWIKRN PKGSICSEGI KSFKAIANFQ DYHGLPEFRK AIAKFMEKTR GGRVRFDPER VVMAGGATGA NETIIFCLAD PGDAFLVPSP YYPAFNRDLR WRTGVQLIPI HCESSNNFKI TSKAVKEAYE NAQKSNIKVK GLILTNPSNP LGTTLDKDTL KSVLSFTNQH NIHLVCDEIY AATVFDTPQF VSIAEILDEQ EMTYCNKDLV HIVYSLSKDM GLPGFRVGII YSFNDDVVNC ARKMSSFGLV STQTQYFLAA MLSDEKFVDN FLRESAMRLG KRHKHFTNGL EVVGIKCLKN NAGLFCWMDL RPLLRESTFD SEMSLWRVII NDVKLNVSPG SSFECQEPGW FRVCFANMDD GTVDIALARI RRFVGVEKSG DKSSSMEKKQ QWKKNNLRLS FSKRMYDESV LSPLSSPIPP SPLVR // ID 1A14_LYCES STANDARD; PRT; 476 AA. AC P29535; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase 4 (EC 4.4.1.14) (ACC DE synthase 4) (S-adenosyl-L-methionine methylthioadenosine-lyase 4) DE (ACS-4). GN ACS4 OR ACC4 OR PCVV4B. OS Lycopersicon esculentum (Tomato). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Solanum. OX NCBI_TaxID=4081; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. CARUSO; TISSUE=Etiolated hypocotyl; RX MEDLINE=93374928; PubMed=8366090; RA Lincoln J.E., Campbell A.D., Oetiker J., Rottmann W.H., Oeller P.W., RA Shen N.F., Theologis A.; RT "LE-ACS4, a fruit ripening and wound-induced 1-aminocyclopropane-1- RT carboxylate synthase gene of tomato (Lycopersicon esculentum). RT Expression in Escherichia coli, structural characterization, RT expression characteristics, and phylogenetic analysis."; RL J. Biol. Chem. 268:19422-19430(1993). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Etiolated hypocotyl; RX MEDLINE=92106351; PubMed=1762159; RA Rottmann W.H., Peter G.F., Oeller P.W., Keller J.A., Shen N.F., RA Nagy B.P., Taylor L.P., Campbell A.D., Theologis A.; RT "1-aminocyclopropane-1-carboxylate synthase in tomato is encoded by a RT multigene family whose transcription is induced during fruit and RT floral senescence."; RL J. Mol. Biol. 222:937-961(1991). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=91271385; PubMed=1711229; RA Olson D.C., White J.A., Edelman L., Harkins R.N., Kende H.; RT "Differential expression of two genes for 1-aminocyclopropane-1- RT carboxylate synthase in tomato fruits."; RL Proc. Natl. Acad. Sci. U.S.A. 88:5340-5344(1991). RN [4] RP SEQUENCE OF 20-159 FROM N.A. RC STRAIN=CV. ORLANDO; TISSUE=Fruit; RX MEDLINE=90280476; PubMed=2191304; RA van der Straeten D., van Wiemeersch L., Goodman H.M., van Montagu M.; RT "Cloning and sequence of two different cDNAs encoding 1- RT aminocyclopropane-1-carboxylate synthase in tomato."; RL Proc. Natl. Acad. Sci. U.S.A. 87:4859-4863(1990). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: HORMONES, SUCH AS AUXIN, ENVIRONMENTAL FACTORS, SUCH AS CC MECHANICAL WOUNDING, A NUMBER OF CHEMICALS AND ANAEROBIOSIS. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M88487; AAA03164.1; -. DR EMBL; X59146; CAA41857.1; -. DR EMBL; M63490; AAA34131.1; -. DR EMBL; M38705; AAA81581.1; -. DR PIR; A40960; A40960. DR PIR; S19679; S19679. DR HSSP; P37821; 1B8G. DR Mendel; 511; LYCes;Acs;4. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 282 282 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT CONFLICT 15 15 V -> A (IN REF. 2). FT CONFLICT 82 82 T -> A (IN REF. 4). FT CONFLICT 253 253 S -> P (IN REF. 2). SQ SEQUENCE 476 AA; 53537 MW; 9BC7D97BD64CB044 CRC64; MDLETSEISN YKSSVVLSKL ASNEQHGENS PYFDGWKAYD NDPFHLVNNL NGVIQMGLAE NQLSVDLIEE WIKRNPKASI CTNDGIESFR RIANFQDYHG LPEFTNAIAK FMEKTRGGKV KFDAKRVVMA GGATGANETL ILCLADPGDA FLVPTPYYPG FNRDLRWRSG VQLLPISCKS CNNFKITIEA IEEAYEKGQQ ANVKIKGLIL TNPCNPLGTI LDRDTLKKIS TFTNEHNIHL VCDEIYAATV FNSPKFVSIA EIINEDNCIN KDLVHIVSSL SKDLGFPGFR VGIVYSFNDD VVNCARKMSS FGLVSTQTQH LLAFMLSDDE FVEEFLIESA KRLRERYEKF TRGLEEIGIK CLESNAGVYC WMDLRSLLKE ATLDAEMSLW KLIINEVKLN VSPGSSFNCS EVGWFRVCFA NIDDQTMEIA LARIRMFMDA YNNVNKNGVM KNKHNGRGTT YDLTPQMGST MKMLLA // ID 1A1C_DIACA STANDARD; PRT; 517 AA. AC P27486; DT 01-AUG-1992 (Rel. 23, Created) DT 01-AUG-1992 (Rel. 23, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS2 OR CARACC. OS Dianthus caryophyllus (Carnation) (Clove pink). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllidae; Caryophyllales; Caryophyllaceae; Dianthus. OX NCBI_TaxID=3570; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Petal; RX MEDLINE=92119258; PubMed=1731995; RA Park K.Y., Drory A., Woodson W.R.; RT "Molecular cloning of an 1-aminocyclopropane-1-carboxylate synthase RT from senescing carnation flower petals."; RL Plant Mol. Biol. 18:377-386(1992). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M66619; AAA33275.1; -. DR PIR; S19252; S19252. DR HSSP; P37821; 1B8G. DR Mendel; 8016; DIAca;Acs;2. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 277 277 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT DOMAIN 453 470 POLY-THR. SQ SEQUENCE 517 AA; 58057 MW; C31BA10732E940AE CRC64; MGSYKGVYDR EILSKIATND GHGENLEYFD GWKAYDRDPY HSTKNSNGVI QMGLAENQLC FDLVTEWLLK NPQASICTNE GVNKFMDIAI FQDYHGLPEF RSAVAKFMGK ARDEKVIFNP DRIVMSGGAS ASETLLFCLA NPGDAFLIPS PYYPAFNRDL RWRTGVNLIP FTCSSSNNFK ITKEALQSAY EDALKKNIKV KGIIVTNPSN PLGTVLDKDT LKMLLTFVNA KNIHLVCDEI YATTVFNSPS FISVAEVIKD MPHVNQDLVH ILYSLSKDMG MPGFRVGIIY SYNDRVVSTA RRMSSFGLVS SQTQFMIAAL LSDDDFVRRF LVESRDRLFR RHQHFTSELA KIGIGCLQGN AALFVWMDLR HLLDEATVER ELKLWRVIIN EVKINVSPGS SFLCSEPGWF RVCFANMDNA TLDVALNRIR SFVTRGRVDN STMTTTSARA AATTTTTTTT TTTTTTTTTT IKKKRGQMEL RLSFNNRRFE DGLMSPHSIL LSPHSPMPQS PLVKART // ID 1A1C_MALDO STANDARD; PRT; 473 AA. AC P37821; Q40278; O04993; DT 01-OCT-1994 (Rel. 30, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS-1. OS Malus domestica (Apple) (Malus sylvestris). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Rosales; Rosaceae; Maloideae; Malus. OX NCBI_TaxID=3750; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. GOLDEN DELICIOUS; TISSUE=Fruit cortical tissue; RX MEDLINE=95232185; PubMed=7716231; RA Lay-Yee M., Knighton M.L.; RT "A full-length cDNA encoding 1-aminocyclopropane-1-carboxylate RT synthase from apple."; RL Plant Physiol. 107:1017-1018(1995). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=CV. GOLDEN DELICIOUS; RA Harada T., Sunako T., Sakuraba W., Goto S., Senda M., Akada S., RA Ishikawa R., Niizeki M.; RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 10-473 FROM N.A. RC STRAIN=CV. GOLDEN DELICIOUS; TISSUE=Fruit; RA Dong J.G., Kim W.T., Yip W.K., Thompson G.A., Li L., Bennett A.B., RA Yang S.F.; RT "Cloning of a cDNA encoding 1-aminocyclopropane-1-carboxylate synthase RT and expression of its mRNA in ripening apple fruit."; RL Planta 185:38-45(1991). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS). RX MEDLINE=20079531; PubMed=10610793; RA Capitani G., Hohenester E., Feng L., Storici P., Kirsch J.F., RA Jansonius J.N.; RT "Structure of 1-aminocyclopropane-1-carboxylate synthase, a key RT enzyme in the biosynthesis of the plant hormone ethylene."; RL J. Mol. Biol. 294:745-756(1999). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L31347; AAA73941.1; -. DR EMBL; U89156; AAB68617.1; -. DR EMBL; U03294; AAA03472.1; -. DR PDB; 1B8G; 26-JAN-00. DR Mendel; 251; MALdo;Acs;1. DR Mendel; 9005; MALdo;Acs;2. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family; 3D-structure. FT BINDING 273 273 PYRIDOXAL PHOSPHATE. FT CONFLICT 15 15 Q -> E (IN REF. 3). FT CONFLICT 101 101 E -> K (IN REF. 3). SQ SEQUENCE 473 AA; 53250 MW; 6ACA20759615E75D CRC64; MRMLSRNATF NSHGQDSSYF LGWQEYEKNP YHEVHNTNGI IQMGLAENQL CFDLLESWLA KNPEAAAFKK NGESIFAELA LFQDYHGLPA FKKAMVDFMA EIRGNKVTFD PNHLVLTAGA TSANETFIFC LADPGEAVLI PTPYYPGFDR DLKWRTGVEI VPIHCTSSNG FQITETALEE AYQEAEKRNL RVKGVLVTNP SNPLGTTMTR NELYLLLSFV EDKGIHLISD EIYSGTAFSS PSFISVMEVL KDRNCDENSE VWQRVHVVYS LSKDLGLPGF RVGAIYSNDD MVVAAATKMS SFGLVSSQTQ HLLSAMLSDK KLTKNYIAEN HKRLKQRQKK LVSGLQKSGI SCLNGNAGLF CWVDMRHLLR SNTFEAEMEL WKKIVYEVHL NISPGSSCHC TEPGWFRVCF ANLPERTLDL AMQRLKAFVG EYYNVPEVNG GSQSSHLSHS RRQSLTKWVS RLSFDDRGPI PGR // ID 1A1C_PHAAU STANDARD; PRT; 368 AA. AC Q01912; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase) DE (Fragment). GN ACS5. OS Phaseolus aureus (Mung bean) (Vigna radiata). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Vigna. OX NCBI_TaxID=3916; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. BERKEN / RWILCZ; TISSUE=Hypocotyl; RX MEDLINE=93043033; PubMed=1421146; RA Botella J.R., Arteca J.M., Schlagnhaufer C.D., Arteca R.N., RA Phillips A.T.; RT "Identification and characterization of a full-length cDNA encoding RT for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from RT etiolated mung bean hypocotyl segments and expression of its mRNA in RT response to indole-3-acetic acid."; RL Plant Mol. Biol. 20:425-436(1992). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- INDUCTION: HORMONES, SUCH AS AUXIN, ENVIRONMENTAL FACTORS, SUCH AS CC MECHANICAL WOUNDING AND A NUMBER OF CHEMICALS. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z11562; CAA77655.1; -. DR HSSP; P37821; 1B8G. DR Mendel; 9876; PHAau;Acs;5. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT NON_TER 1 1 FT BINDING 230 230 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT NON_TER 368 368 SQ SEQUENCE 368 AA; 41477 MW; 31BA61D5FC2D4CB8 CRC64; QMGLAENQLT SDLVEDWILN NPEASICTPE GINDFRAIAN FQDYHGLAEF RNAVAKFMAR TRGNRITFDP DRIVMSGGAT GAHEVTAFCL ADPGEAFLVP IPYYPGFDRD LRWRTGVKLV PVMCDSSNNF VLTKEALEDA YEKAREDNIR VKGLLITNPS NPLGTIMDRK TLRTVVSFIN EKRIHLVCDE IYAATVFSQP GFISIAEILE DETDIECDRN LVHIVYSLSK DMGFPGFRVG IIYSYNDAVV NCARKMSSFG LVSTQTQYLL ASMLNDDEFV ERFLAESAKR LAQRFRVFTG GLAKVGIKCL QSNAGLFVWM DLRQLLKKPT FDSETELWKV IIHEVKINVS PGYSFHCTEP GWFRVCFA // ID 1A1C_SOYBN STANDARD; PRT; 484 AA. AC P31531; DT 01-JUL-1993 (Rel. 26, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS1. OS Glycine max (Soybean). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Phaseoleae; Glycine. OX NCBI_TaxID=3847; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. CENTURY; TISSUE=Leaf; RA Liu D., Li N., Mattoo A.K.; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67100; CAA47474.1; -. DR PIR; S25002; S25002. DR HSSP; P37821; 1B8G. DR Mendel; 8361; GLYma;Acs;1. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate; KW Multigene family. FT BINDING 279 279 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 484 AA; 54730 MW; 152F7AD12B992987 CRC64; MGLMDVDQTQ LLSKMVIGDG HGEASPYFDG WKAYDENPFH PKENPNGVIQ MGLAENQLTS DLVEDWILNN PEASICTPEG INDFRAIANF QDYHGLPEFR NAVAKFMGRT RGNRVTFDPD RIVMSGGATG AHEVTTFCLA DPGDAFLVPI PYYPGFDRDL RWRTGIKLVP VMCDSSNNFK LTKQALEDAY EKAKEDNIRV KGLLITNPSN PLGTVMDRNT LRTVMSFINE KRIHLVSDEI YSATVFSHPS FISIAEILEE DTDIECDRNL VHIVYSLSKD MGFPGFRVGI IYSYNDAVVH CARKMSSFGL VSTQTQYLLA SMLNDDEFVE SFLVESAKRL AQRHRVFTGG LAKVGIKCLQ SNAGLFVWMD LRQLLKKPTL DSEMELWRVI IDEVKINVSP GSSFHCTEPG WFRVCYANMD DMAVQIALQR IRNFVLQNKE IMVPNKKHCW HSNLRLSLKT RRFDDIMMSP HSPIPQSPLV KATI // ID 1A1C_TOBAC STANDARD; PRT; 491 AA. AC Q07262; DT 01-OCT-1994 (Rel. 30, Created) DT 01-OCT-1994 (Rel. 30, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (ACC DE synthase) (S-adenosyl-L-methionine methylthioadenosine-lyase). GN ACS1. OS Nicotiana tabacum (Common tobacco). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids I; Solanales; Solanaceae; Nicotiana. OX NCBI_TaxID=4097; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. XANTHI; RA Bailey B.A., Avni A., Li N., Matoo A.K., Anderson J.D.; RT "Nucleotide sequence of the Nicotiana tabacum cv Xanthi gene encoding RT 1-aminocyclopropane-1-carboxylate synthase."; RL Plant Physiol. 100:1615-1616(1992). CC -!- FUNCTION: CATALYZES THE FORMATION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE, A DIRECT PRECURSOR OF ETHYLENE IN HIGHER PLANTS. CC -!- CATALYTIC ACTIVITY: S-ADENOSYL-L-METHIONINE = 1-AMINOCYCLOPROPANE- CC 1-CARBOXYLATE + METHYLTHIOADENOSINE. CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- PATHWAY: FIRST, AND RATE LIMITING STEP OF ETHYLENE BIOSYNTHESIS. CC -!- SUBUNIT: HOMODIMER. CC -!- SIMILARITY: BELONGS TO CLASS-I OF PYRIDOXAL-PHOSPHATE-DEPENDENT CC AMINOTRANSFERASES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X65982; CAA46797.1; -. DR HSSP; P37821; 1B8G. DR Mendel; 252; NICta;Acs;1. DR InterPro; IPR001176; ACC_synthase. DR InterPro; IPR001511; Aminotran_1. DR Pfam; PF00155; aminotran_1_2; 1. DR PRINTS; PR00753; ACCSYNTHASE. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. KW Fruit ripening; Ethylene biosynthesis; Lyase; Pyridoxal phosphate. FT BINDING 278 278 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 491 AA; 55290 MW; 57B9FF4306686DFD CRC64; MGFENEKNSS ILSKLATNEE LGENSPYFDG WKAYDNDPFH PLKNPNGVIQ MGLAENQLCF DLIEEWIKRN PNASICTTEG IKSFRAIANF QDYHGLPEFR SAIAKFMEKT RGGRVTFDPE RVVMAGGATG ANETIIFCLA DTGDAFLVPS PYYPAFNRDL RWRTGVQLIP IPCDSSNNFQ ITTKAVREAY ENAQKSNIKV KGLILTNPSN PLGTTLDRDT LKNLLTFTNQ HNIHLVCDEI YAATVFNTPQ FVSIAEILDD ETSHCNKDLV HIVYSLSKDM GLPGFRVGIV YSFNDAVVNC ARKMSSFGLV STQTQYLLAE MLSDERFVSN FLTESSKRLA KRHKHFTNGL EEVGIKCLRS NAGLFCWMDL RPLLKESTFD SEMSLWRVII NDVKLNVSPG SSFDCQEPGF FRVCFANMDD ETVDIALARI RSFVGVKKSG DESTPILMEK KQQWKKNNLR LSFSKRMYDE SVNLSPLSSP IPHSPLVRAR T // ID 1A1D_ECOLI STANDARD; PRT; 328 AA. AC P76316; O08478; O08479; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) DE (ACC deaminase). GN YEDO OR B1919. OS Escherichia coli. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Escherichia. OX NCBI_TaxID=562; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=K12 / MG1655; RX MEDLINE=97426617; PubMed=9278503; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., RA Mau B., Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1474(1997). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=K12; RX MEDLINE=97251358; PubMed=9097040; RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y., RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., RA Yamamoto Y., Horiuchi T.; RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome RT corresponding to the 40.1-50.0 min region on the linkage map."; RL DNA Res. 3:379-392(1996). CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE000284; AAC74986.1; ALT_INIT. DR EMBL; D90832; BAA15739.1; ALT_INIT. DR EMBL; D90833; BAA15746.1; ALT_INIT. DR EcoGene; EG14038; yedO. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Hypothetical protein; Lyase; Pyridoxal phosphate; Complete proteome. FT BINDING 51 51 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 328 AA; 35153 MW; 4179DE645C0B32D8 CRC64; MPLHNLTRFP RLEFIGAPTP LEYLPRFSDY LGREIFIKRD DVTPMAMGGN KLRKLEFLAA DALREGADTL ITAGAIQSNH VRQTAAVAAK LGLHCVALLE NPIGTTAENY LTNGNRLLLD LFNTQIEMCD ALTDPNAQLE ELATRVEAQG FRPYVIPVGG SNALGALGYV ESALEIAQQC EGAVNISSVV VASGSAGTHA GLAVGLEHLM PESELIGVTV SRSVADQLPK VVNLQQAIAK ELELTASAEI LLWDDYFAPG YGVPNDEGME AVKLLARLEG ILLDPVYTGK AMAGLIDGIS QKRFKDEGPI LFIHTGGAPA LFAYHPHV // ID 1A1D_ENTCL STANDARD; PRT; 338 AA. AC Q9ZHW3; Q9ZHW4; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) (ACC DE deaminase). OS Enterobacter cloacae. OC Bacteria; Proteobacteria; gamma subdivision; Enterobacteriaceae; OC Enterobacter. OX NCBI_TaxID=550; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CAL2, AND UW4; RX MEDLINE=99068011; PubMed=9851025; RA Shah S., Li J., Moffatt B.A., Glick B.R.; RT "Isolation and characterization of ACC deaminase genes from two RT different plant growth-promoting rhizobacteria."; RL Can. J. Microbiol. 44:833-843(1998). CC -!- FUNCTION: CATALYSES THE CONVERSION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE (ACC), THE PRECURSOR TO THE PHYTOHORMONE ETHYLENE, TO CC AMMONIA AND ALPHA-KETOBUTYRATE. ALLOWS GROWTH ON ACC AS A NITROGEN CC SOURCE. CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF047840; AAD05070.1; -. DR EMBL; AF047710; AAD05069.1; -. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Lyase; Pyridoxal phosphate. FT BINDING 51 51 PYRIDOXAL PHOSPHATE (BY SIMILARITY). FT VARIANT 26 26 Q -> E (IN STRAIN UW4). FT VARIANT 151 151 Q -> R (IN STRAIN UW4). FT VARIANT 178 178 K -> E (IN STRAIN UW4). FT VARIANT 185 185 E -> D (IN STRAIN UW4). FT VARIANT 191 191 N -> D (IN STRAIN UW4). FT VARIANT 313 313 E -> D (IN STRAIN UW4). FT VARIANT 337 337 D -> N (IN STRAIN UW4). SQ SEQUENCE 338 AA; 36871 MW; 0B94C8C887772AF8 CRC64; MNLNRFERYP LTFGPSPITP LKRLSQHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMSDVVE QGGKPFPIPA GCSEHPYGGL GFVGFAKKLR QQEKELGFKF NYIVVCSVTG STQAGMVVGF AADGRSKNVI GVDASAKPEQ TKAQILRIAR HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRDG // ID 1A1D_PSEFL STANDARD; PRT; 338 AA. AC Q51813; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) (ACC DE deaminase). OS Pseudomonas fluorescens. OC Bacteria; Proteobacteria; gamma subdivision; Pseudomonadaceae; OC Pseudomonas. OX NCBI_TaxID=294; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=17; RX MEDLINE=96242319; PubMed=9026447; RA Campbell B.G., Thompson J.A.; RT "1-aminocyclopropane-1-carboxylate deaminase genes from Pseudomonas RT strains."; RL FEMS Microbiol. Lett. 138:207-210(1996). CC -!- FUNCTION: CATALYSES THE CONVERSION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE (ACC), THE PRECURSOR TO THE PHYTOHORMONE ETHYLENE, TO CC AMMONIA AND ALPHA-KETOBUTYRATE. ALLOWS GROWTH ON ACC AS A NITROGEN CC SOURCE. CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMOTRIMER (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37103; AAC44163.1; -. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Lyase; Pyridoxal phosphate. FT BINDING 51 51 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 338 AA; 36855 MW; E6E98B3EB6FE6144 CRC64; MNLNRFKRYP LTFGPSPITP LKRLSEHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EALEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMNDVVE RGGKPFPIPA GCSEHPYGGL GFVGFAEEVR EQEKQLGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GIDASAKPEK TKAQILRIAR HTAELVELGR EITEDDVVLD TPFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRNG // ID 1A1D_PSES0 STANDARD; PRT; 338 AA. AC P30297; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) (ACC DE deaminase). OS Pseudomonas sp. (strain 6G5). OC Bacteria; Proteobacteria. OX NCBI_TaxID=29439; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92338840; PubMed=1821764; RA Klee H.J., Hayford M.B., Kretzmer K.A., Barry G.F., Kishore G.M.; RT "Control of ethylene synthesis by expression of a bacterial enzyme in RT transgenic tomato plants."; RL Plant Cell 3:1187-1193(1991). CC -!- FUNCTION: CATALYSES THE CONVERSION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE (ACC), THE PRECURSOR TO THE PHYTOHORMONE ETHYLENE, TO CC AMMONIA AND ALPHA-KETOBUTYRATE. ALLOWS GROWTH ON ACC AS A NITROGEN CC SOURCE. CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMOTRIMER. CC -!- BIOTECHNOLOGY: INTRODUCED BY GENETIC MANIPULATION AND EXPRESSED IN CC IMPROVED RIPENING TOMATO BY MONSANTO. ACC IS THE IMMEDIATE CC PRECURSOR OF THE PHYTOHORMONE ETHYLENE WHO IS INVOLVED IN THE CC CONTROL OF RIPENING. ACC DEAMINASE REDUCES ETHYLENE BIOSYNTHESIS CC AND THUS EXTEND THE SHELF LIFE OF FRUITS AND VEGETABLES. CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M80882; AAA73153.1; -. DR PIR; JQ1330; JQ1330. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Lyase; Pyridoxal phosphate; Genetically modified food. FT BINDING 51 51 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 338 AA; 36873 MW; F496374E7C12B6AD CRC64; MNLNRFERYP LTFGPSPITP LKRLSQHLGG KVELYAKRED CNSGLAFGGN KTRKLEYLIP EAIEQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIEMSR IMGADVRLDA AGFDIGIRPS WEKAMSDVVE QGGKPFPIPA GCSEHPYGGL GFVGFAEEVR QQEKELGFKF DYIVVCSVTG STQAGMVVGF AADGRSKNVI GIDASAKPEQ TKAQILRIAR HTAELVELGR EITEEDVVLD TRFAYPEYGL PNEGTLEAIR LCGSLEGVLT DPVYEGKSMH GMIEMVRRGE FPEGSKVLYA HLGGAPALNA YSFLFRNG // ID 1A1D_PSESP STANDARD; PRT; 338 AA. AC Q00740; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) (ACC DE deaminase). OS Pseudomonas sp. (strain ACP). OC Bacteria; Proteobacteria. OX NCBI_TaxID=306; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE. RX MEDLINE=91358299; PubMed=1885510; RA Sheehy R.E., Honma M., Yamada M., Sasaki T., Martineau B., RA Hiatt W.R.; RT "Isolation, sequence, and expression in Escherichia coli of the RT Pseudomonas sp. strain ACP gene encoding 1-aminocyclopropane-1- RT carboxylate deaminase."; RL J. Bacteriol. 173:5260-5265(1991). CC -!- FUNCTION: CATALYSES THE CONVERSION OF 1-AMINOCYCLOPROPANE-1- CC CARBOXYLATE (ACC), THE PRECURSOR TO THE PHYTOHORMONE ETHYLENE, TO CC AMMONIA AND ALPHA-KETOBUTYRATE. ALLOWS GROWTH ON ACC AS A NITROGEN CC SOURCE. CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE. CC -!- SUBUNIT: HOMOTRIMER. CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M73488; AAA25689.1; -. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Lyase; Pyridoxal phosphate. FT BINDING 51 51 PYRIDOXAL PHOSPHATE. SQ SEQUENCE 338 AA; 36672 MW; 01FC286177012FDF CRC64; MNLQRFPRYP LTFGPTPIQP LARLSKHLGG KVHLYAKRED CNSGLAFGGN KTRKLEYLIP EALAQGCDTL VSIGGIQSNQ TRQVAAVAAH LGMKCVLVQE NWVNYSDAVY DRVGNIQMSR ILGADVRLVP DGFDIGFRRS WEDALESVRA AGGKPYAIPA GCSDHPLGGL GFVGFAEEVR AQEAELGFKF DYVVVCSVTG STQAGMVVGF AADGRADRVI GVDASAKPAQ TREQITRIAR QTAEKVGLER DIMRADVVLD ERFAGPEYGL PNEGTLEAIR LCARTEGMLT DPVYEGKSMH GMIEMVRNGE FPEGSRVLYA HLGGVPALNG YSFIFRDG // ID 1A1D_PYRAB STANDARD; PRT; 330 AA. AC Q9V2L2; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) DE (ACC deaminase). GN PAB2303. OS Pyrococcus abyssi. OC Archaea; Euryarchaeota; Thermococcales; Thermococcaceae; Pyrococcus. OX NCBI_TaxID=29292; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ORSAY; RA Heilig R.; RT "Pyrococcus abyssi genome sequence: insights into archaeal chromosome RT structure and evolution."; RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AJ248283; CAB48986.1; -. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Hypothetical protein; Lyase; Pyridoxal phosphate; Complete proteome. FT BINDING 54 54 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 330 AA; 35754 MW; CC8699923C0B11CD CRC64; MHPKVDALLS RFPRITLIPW ETPIQYLPRI SRELGVDVYV KRDDLTGLGI GGNKIRKLEF LLGDALSRGC DTVITIGAVH SNHAFVTALA AKKLGLGAVL ILRGEEVLKG NYLLDKLMGI ETRIYEADNS WELMKVAEEV AEELKGEGKK PYIIPPGGAS PVGTLGYIRG VGELYTQVKK LGLRIDTVVD AVGSGGTYAG LLLGSAIVNA EWSVVGIDVS SATEKAKERV KNLVEKTKEL LGINVKVQEP RIYDYGFGAY GKIVKEVAKL IKSVGTMEGL LLDPVYTGKA FYGLMDLAKK GDLGESVLFI HTGGLPGIFH YGEEMLELLV // ID 1A1D_PYRHO STANDARD; PRT; 325 AA. AC O57809; DT 15-DEC-1998 (Rel. 37, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) DE (ACC deaminase). GN PH0054 OR PHBE027. OS Pyrococcus horikoshii. OC Archaea; Euryarchaeota; Thermococcales; Thermococcaceae; Pyrococcus. OX NCBI_TaxID=53953; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=OT3; RX MEDLINE=98344137; PubMed=9679194; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., RA Yamamoto S., Sekine M., Baba S.-I., Kosugi H., Hosoyama A., Nagai Y., RA Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., RA Aoki K.-I., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., RA Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AP000001; BAA29122.1; ALT_INIT. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Hypothetical protein; Lyase; Pyridoxal phosphate; Complete proteome. FT BINDING 54 54 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 325 AA; 35188 MW; 60AE1B7A37CDF231 CRC64; MHPKIFALLA KFPRVELIPW ETPIQYLPNI SREIGADVYI KRDDLTGLGI GGNKIRKLEY LLGDALSKGA DVVITVGAVH SNHAFVTGLA AKKLGLDAIL VLRGKEELKG NYLLDKIMGI ETRVYDAKDS FELMKYAEEI AEELKREGRK PYVIPPGGAS PIGTLGYVRA VGEIATQSEV KFDSIVVAAG SGGTLAGLSL GLSILNEDIR PVGIAVGRFG EVMTSKLDNL IKEAAELLGV KVEVRPELYD YSFGEYGKIT GEVAQIIRKV GTREGIILDP VYTGKAFYGL VDLARKGELG EKILFIHTGG ISGTFHYGDK LLSLL // ID 1A1D_THEMA STANDARD; PRT; 312 AA. AC Q9WY68; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Putative 1-aminocyclopropane-1-carboxylate deaminase (EC 4.1.99.4) DE (ACC deaminase). GN TM0225. OS Thermotoga maritima. OC Bacteria; Thermotogales; Thermotoga. OX NCBI_TaxID=2336; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=MSB8 / DSM 3109; RX MEDLINE=99287316; PubMed=10360571; RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., RA Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., RA McDonald L., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., RA Stewart A.M., Cotton M.D., Pratt M.S., Phillips C.A., Richardson D., RA Heidelberg J., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., RA Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.; RT "Evidence for lateral gene transfer between Archaea and Bacteria from RT genome sequence of Thermotoga maritima."; RL Nature 399:323-329(1999). CC -!- CATALYTIC ACTIVITY: 1-AMINOCYCLOPROPANE-1-CARBOXYLATE + H(2)O = CC 2-OXOBUTANOATE + NH(3). CC -!- COFACTOR: PYRIDOXAL PHOSPHATE (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE ACC DEAMINASE FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AE001707; AAD35317.1; -. DR TIGR; TM0225; -. DR InterPro; IPR001926; PALP. DR Pfam; PF00291; PALP; 1. KW Hypothetical protein; Lyase; Pyridoxal phosphate; Complete proteome. FT BINDING 42 42 PYRIDOXAL PHOSPHATE (BY SIMILARITY). SQ SEQUENCE 312 AA; 34756 MW; 6BE2A4A0BFC1E15F CRC64; MRIDLSLKPT PVQFLKRLSE KYGFNIYVKR DDLTELVGSG NKIRKLEYLL WEALKKGATT VFTCGGLQSN HARATAYVSR RYGLKPVLFL RKGEKVLNGN LLLDILLGAE IVEVSPEEYE RIDEIFDVHK KMREKKGEKV YVIPEGGSNS LGAFGYFNAV LEMKDQLNLE SFDAIVCAVG SGGTIAGLSA GISFLEYHVP VVGVNVTTKN SDYFVGKVKR IISGMEEYGL RVNETVFEVV DDYRGPGYAI PSSEDVEILK EVASIEGIIL DPVYTAKAFR GMIEMFRNSE KNVLFIHTGG IFGLFAQSRR LV // ID 1A23_HUMAN STANDARD; PRT; 365 AA. AC P30447; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-23(A-9) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*2301). RX MEDLINE=92104637; PubMed=1729171; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE ONLY ALLELE OF A-23 KNOWN IS A*2301 WHICH IS CC SHOWN HERE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64742; AAA03662.1; -. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-23(A-9) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 365 AA; 40732 MW; C372DE503BF393D0 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTVHIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A24_HUMAN STANDARD; PRT; 365 AA. AC P05534; P30448; P30449; Q95355; DT 01-NOV-1988 (Rel. 09, Created) DT 01-NOV-1988 (Rel. 09, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-24(A-9) alpha chain DE precursor (AW-24). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*2401). RX MEDLINE=85206128; PubMed=2987115; RA N'Guyen C., Sodoyer R., Trucy J., Strachan T., Jordan B.R.; RT "The HLA-AW24 gene: sequence, surroundings and comparison with the RT HLA-A2 and HLA-A3 genes."; RL Immunogenetics 21:479-489(1985). RN [2] RP REVISIONS (A*2401). RA Jordan B.R.; RL Submitted (XXX-1988) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (A*2402/A*2403). RX MEDLINE=92104637; PubMed=1729171; RA Little A.-M., Madrigal J.A., Parham P.; RT "Molecular definition of an elusive third HLA-A9 molecule: HLA-A9.3."; RL Immunogenetics 35:41-45(1992). RN [4] RP SEQUENCE FROM N.A. (A*2402). RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [5] RP SEQUENCE FROM N.A. (A*2402). RX MEDLINE=98007772; PubMed=9349616; RA Laforet M., Froelich N., Parissiadis A., Bausinger H., Pfeiffer B., RA Tongio M.M.; RT "An intronic mutation responsible for a low level of expression of an RT HLA-A*24 allele."; RL Tissue Antigens 50:340-346(1997). RN [6] RP SEQUENCE OF 26-206 FROM N.A. RA Gao X., McCluskey J.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE FROM N.A. (A*2408). RC TISSUE=Blood; RA Kashiwase K., Tokunaga K., Ishikawa Y., Qiu L., Furuya M., RA Sawanaka K., Akaza T., Tadokoro K., Juji T.; RT "A new A9 sequence HLA-A9HH from Japanese."; RL MHC 3:9-14(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-24 ARE KNOWN: A*2401, CC A*2401, A*2403 AND A*2408 (A9HH). THE SEQUENCE SHOWN IS THAT OF CC A*2401. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15497; AAA59611.1; -. DR EMBL; M64740; AAA59600.1; -. DR EMBL; M64741; AAA59601.1; -. DR EMBL; U19733; AAB60651.1; -. DR EMBL; U18987; AAB60651.1; JOINED. DR EMBL; Z72422; CAA96532.1; -. DR EMBL; D83516; BAA11936.1; -. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-24(A-9) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 5 5 G -> A (IN A*2402, A*2403 AND A*2408). FT /FTId=VAR_004354. FT VARIANT 27 27 H -> Q (IN A*2408). FT /FTId=VAR_004355. FT VARIANT 86 86 E -> G (IN A*2408). FT /FTId=VAR_004356. FT VARIANT 89 89 G -> R (IN A*2408). FT /FTId=VAR_004357. FT VARIANT 180 180 Q -> W (IN REF. 6). FT /FTId=VAR_004358. FT VARIANT 190 191 DG -> EW (IN A*2403). FT /FTId=VAR_004359. FT VARIANT 206 206 A -> T (IN A*2402, A*2403, A*2408 AND FT REF. 6). FT /FTId=VAR_004360. SQ SEQUENCE 365 AA; 40644 MW; 7BDD98A4EDEFEA3E CRC64; MAVMGPRTLV LLLSGALALT QTWAGSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDEETGK VKAHSQTDRE NLRIALRYYN QSEAGSHTLQ MMFGCDVGSD GRFLRGYHQY AYDGKDYIAL KEDLRSWTAA DMAAQITKRK WEAAHVAEQQ RAYLEGTCVD GLRRYLENGK ETLQRADPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTVPIVG IIAGLVLLGA VITGAVVAAV MWRRNSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A25_HUMAN STANDARD; PRT; 365 AA. AC P18462; Q95362; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-25(A-10) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*2501). RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP SEQUENCE FROM N.A. (A*2502). RC TISSUE=Hematopoietic; RX MEDLINE=97045042; PubMed=8881046; RA Krausa P., Young D.M., Gotch F.; RT "Identification of a new HLA-A allele (A*2502) by PCR-SSP."; RL Immunogenetics 45:84-85(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-25 ARE KNOWN: A*2501 CC AND A*2502. THE SEQUENCE SHOWN IS THAT OF A*2501. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32321; AAA36234.1; -. DR EMBL; X97802; CAA66389.1; -. DR PIR; A35997; A35997. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-25(A-10) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 94 94 H -> Q (IN A*2502). FT /FTId=VAR_004361. SQ SEQUENCE 365 AA; 41218 MW; 00F71BD2F97C3620 CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRE SLRIALRYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A26_HUMAN STANDARD; PRT; 365 AA. AC P30450; Q31623; Q30208; DT 01-APR-1993 (Rel. 25, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-26(A-10) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*2601/A*2602). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). RN [2] RP SEQUENCE FROM N.A. (A*2601). RX MEDLINE=90256559; PubMed=1692821; RA Zinzsner H., Masset M., Bourge J.-F., Colombani J., Cohen D., RA Degos L., Paul P.; RT "Nucleotide sequence of the HLA-A26 class I gene: identification of RT specific residues and molecular mapping of public HLA class I RT epitopes."; RL Hum. Immunol. 27:155-166(1990). RN [3] RP SEQUENCE FROM N.A. (A*2601; A*2602; A*2603 AND A*2604). RC TISSUE=Blood; RX MEDLINE=94299439; PubMed=8026990; RA Ishikawa Y., Tokunaga K., Lin L., Imanishi T., Saitou S., RA Kashiwase K., Akaza T., Tadokoro K., Juji T.; RT "Sequences of four splits of HLA-A10 group. Implications for RT serologic cross-reactivities and their evolution."; RL Hum. Immunol. 39:220-224(1994). RN [4] RP SEQUENCE FROM N.A. (A*2601). RC TISSUE=Lymphocytes; RA Miyashita H., Fujiyoshi T., Yashiki S., Kuwayama M., Fujiyama C., RA Sonoda S.; RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 27-365 FROM N.A. (A*2601). RX MEDLINE=89122144; PubMed=2914713; RA Cianetti L., Testa U., Scotto L., la Valle R., Simeone A., RA Boccoli G., Giannella G., Peschle C., Boncinelli E.; RT "Three new class I HLA alleles: structure of mRNAs and alternative RT mechanisms of processing."; RL Immunogenetics 29:80-91(1989). RN [6] RP SEQUENCE FROM N.A. (A*2603). RC TISSUE=Lymphocytes; RX MEDLINE=96435465; PubMed=8838351; RA Miyashita H., Fujiyoshi T., Yashiki S., Kuwayama M., Fujiyama C., RA Sonoda S.; RT "Cloning of HLA-A26 cDNA from Japanese donors possessing 'ATL- RT associated HLA haplotypes'."; RL Tissue Antigens 46:398-400(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-26 ARE KNOWN: A*2601, CC A*2602, A*2603 AND A*2604 (A-10SA). THE SEQUENCE SHOWN IS THAT OF CC A*2601. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03697; AAA03720.1; -. DR EMBL; M98453; AAA35991.1; -. DR EMBL; D14350; BAA03279.1; -. DR EMBL; D14351; BAA03280.1; -. DR EMBL; D14354; BAA03282.1; -. DR EMBL; D16843; BAA04119.1; -. DR EMBL; D32130; BAA06856.1; -. DR EMBL; D32131; BAA06857.1; -. DR EMBL; M24095; AAA59655.1; -. DR EMBL; D32129; BAA06855.1; -. DR PIR; A37028; A37028. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-26(A-10) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 98 101 DRAN -> HRVD (IN A*2603). FT /FTId=VAR_004362. FT VARIANT 140 140 D -> N (IN A*2602). FT /FTId=VAR_004364. FT VARIANT 187 187 R -> L (IN A*2604). FT /FTId=VAR_004363. FT CONFLICT 153 153 D -> H (IN REF. 5). FT CONFLICT 160 160 A -> G (IN REF. 5). SQ SEQUENCE 365 AA; 41062 MW; 44B54DD363B46EDA CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A29_HUMAN STANDARD; PRT; 365 AA. AC P30512; P30451; O02955; O19687; DT 01-APR-1993 (Rel. 25, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-29 alpha chain precursor DE (AW-19). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*2901). RX MEDLINE=89065816; PubMed=2461903; RA Trapani J.A., Mizuno S., Kang S.H., Yang S.Y., Dupont B.; RT "Molecular mapping of a new public HLA class I epitope shared by all RT HLA-B and HLA-C antigens and defined by a monoclonal antibody."; RL Immunogenetics 29:25-32(1989). RN [2] RP REVISION TO 345. RA Yang S.Y.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (A*2901). RA Szmania S., Baxter-Lowe L.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (A*2902). RX MEDLINE=92145462; PubMed=1782566; RA Tabary T., Prochnicka-Chalufour A., Cornillet P., Lehoang P., RA Betuel H., Cohen H.M.; RT "HLA-A29 sub-types and 'Birdshot' choroido-retinopathy RT susceptibility: a possible 'resistance motif' in the HLA-A29.1 RT molecule."; RL C. R. Acad. Sci., III, Sci. Vie 313:599-605(1991). RN [5] RP SEQUENCE FROM N.A. (A*2903). RX MEDLINE=98119601; PubMed=9459513; RA Prokupek B., Dunn P., Ross J., Jordan F., Holman R., Madrigal J.A., RA Little A.M.; RT "HLA-A*2903 expresses an epitope shared with HLA-A*8001."; RL Tissue Antigens 51:115-118(1998). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-29 ARE KNOWN: A*2901 CC A*2902 (A29.2), A*2903. THE SEQUENCE SHOWN IS THAT OF A*2901. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23739; AAB47873.1; -. DR EMBL; U83415; AAB53373.1; -. DR EMBL; X60108; CAA42702.1; -. DR EMBL; AJ000661; CAA04209.1; -. DR PIR; A45847; A45847. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-29 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 126 126 H -> D (IN A*2902 AND A*2903). FT /FTId=VAR_004365. FT VARIANT 190 191 EW -> DG (IN A*2903). FT /FTId=VAR_010372. SQ SEQUENCE 365 AA; 40862 MW; 56E4B9039B3C783C CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDLQTRN VKAQSQTDRA NLGTLRGYYN QSEAGSHTIQ MMYGCHVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A30_HUMAN STANDARD; PRT; 365 AA. AC P16188; P30452; Q9UIP7; DT 01-APR-1990 (Rel. 14, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-30(AW-19) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3001). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP SEQUENCE FROM N.A. (A*3002). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [3] RP SEQUENCE OF 25-279 FROM N.A. (A*3003). RX MEDLINE=93209813; PubMed=8458735; RA Choo S.Y., Starling G.C., Anasetti C., Hansen J.A.; RT "Selection of an unrelated donor for marrow transplantation RT facilitated by the molecular characterization of a novel HLA-A RT allele."; RL Hum. Immunol. 36:20-26(1993). RN [4] RP SEQUENCE FROM N.A. (A*3001). RX MEDLINE=95176329; PubMed=7871528; RA Olerup O., Daniels T.J., Baxter-Lowe L.; RT "Correct sequence of the A*3001 allele obtained by PCR-SSP typing and RT automated nucleotide sequencing."; RL Tissue Antigens 44:265-267(1994). RN [5] RP SEQUENCE FROM N.A. (A*3004). RA Krausa P., Carcassi C., Orru S., Bodmer J.G., Browning M.J., RA Contu L.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE FROM N.A. (A*300X). RA Cox S.T., Mcwhinnie A.J., Madrigal A.J., Little A.M.; RT "New A*30 HLA allele found in an Afro-Caribbean bone marrow donor."; RL Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE OF 26-206 FROM N.A. (A*3004). RA Lienert K., Gao X., McCluskey J.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 28-205 FROM N.A. (A*3004). RX MEDLINE=96124443; PubMed=8560452; RA Blasczyk R., Wehling J., Paessler M., Hahn U., Huhn D., Salama A.; RT "A novel HLA-A30 allele (A*3004) identified by single-strand RT conformation polymorphism analysis and confirmed by solid-phase RT sequencing."; RL Tissue Antigens 46:322-326(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-30 ARE KNOWN: A*3001 CC (A30.3), A*3002, A*3003 AND A*3004. THE SEQUENCE SHOWN IS THAT OF CC A*3001. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30576; AAA59612.1; -. DR EMBL; X61702; CAA43871.1; -. DR EMBL; M93657; AAA58650.1; -. DR EMBL; U07234; AAA70162.1; -. DR EMBL; Z34921; CAA84401.1; -. DR EMBL; U19734; AAB53658.1; -. DR EMBL; U18988; AAB53658.1; JOINED. DR EMBL; U24261; AAB50434.1; -. DR EMBL; AJ249308; CAB57306.1; -. DR EMBL; AJ249309; CAB57306.1; JOINED. DR EMBL; AJ249310; CAB57306.1; JOINED. DR EMBL; AJ249311; CAB57306.1; JOINED. DR EMBL; AJ249312; CAB57306.1; JOINED. DR EMBL; AJ249313; CAB57306.1; JOINED. DR EMBL; AJ249314; CAB57306.1; JOINED. DR EMBL; AJ249315; CAB57306.1; JOINED. DR EMBL; X83770; CAA58723.1; -. DR EMBL; X83771; CAA58724.1; -. DR PIR; S16766; S16766. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-30(AW-19) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 21 21 H -> Q (IN A*3002, A*3004 AND A*300X). FT /FTId=VAR_004366. FT VARIANT 33 33 S -> Y (IN A*300X). FT /FTId=VAR_010284. FT VARIANT 80 80 R -> G (IN A*3003). FT /FTId=VAR_004367. FT VARIANT 94 94 Q -> H (IN A*3002, A*3003 AND A*3004). FT /FTId=VAR_004368. FT VARIANT 100 101 VD -> EN (IN A*3002, A*3003 AND A*3004). FT /FTId=VAR_004369. FT VARIANT 175 176 RW -> HV (IN A*3004). FT /FTId=VAR_004370. FT VARIANT 176 176 W -> R (IN A*3002 AND A*3003). FT /FTId=VAR_004371. FT VARIANT 180 180 L -> W (IN A*3004). FT /FTId=VAR_004372. FT CONFLICT 33 33 S -> F (IN REF. 1). SQ SEQUENCE 365 AA; 40904 MW; 521166D95FB1DC28 CRC64; MAVMAPRTLL LLLSGALALT HTWAGSHSMR YFSTSVSRPG SGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQER PEYWDQETRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ IMYGCDVGSD GRFLRGYEQH AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A31_HUMAN STANDARD; PRT; 365 AA. AC P16189; O98137; Q9TQ24; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-31 alpha chain precursor DE (Aw-19). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3101). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP SEQUENCE FROM N.A. (A*3101). RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [3] RP SEQUENCE FROM N.A. (A*31012). RX MEDLINE=96387675; PubMed=8795145; RA Arnett K.L., Adams E.J., Parham P.; RT "On the sequence of A*3101."; RL Tissue Antigens 47:428-430(1996). RN [4] RP SEQUENCE OF 9-365 FROM N.A. (A*3101). RX MEDLINE=92269956; PubMed=1589035; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [5] RP SEQUENCE FROM N.A. (A*3104). RA Bettinotti M.P., Dhillon G., Hackett J., Simonis T.B., Marincola F.M.; RT "A New HLA-A*31 allele."; RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 26-206 FROM N.A. (A*3104). RA Mitsuishi Y.; RT "New HLA-A31 allele identified in African American population."; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-31 ARE KNOWN: A*3101 AND CC A*3104. THE SEQUENCE SHOWN IS THAT OF A*3101. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30578; AAA59613.1; -. DR EMBL; M84375; AAA59599.1; -. DR EMBL; L78918; AAB05976.1; -. DR EMBL; AF148863; AAD39981.1; -. DR EMBL; AF105028; AAC79721.1; -. DR EMBL; AF105027; AAC79721.1; JOINED. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-31 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 121 121 M -> I (IN A*3104). FT /FTId=VAR_010373. FT VARIANT 138 138 Q -> R (IN A*3104). FT /FTId=VAR_010374. SQ SEQUENCE 365 AA; 41004 MW; 4E760C821A3C553B CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQER PEYWDQETRN VKAHSQIDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A32_HUMAN STANDARD; PRT; 365 AA. AC P10314; Q29838; DT 01-MAR-1989 (Rel. 10, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-32(AW-19) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3201). RA Domena J.D.; RL Submitted (DEC-1993) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE OF 25-298 FROM N.A. (A*3201). RX MEDLINE=87058961; PubMed=2431040; RA Wan A.M., Ennis P., Parham P., Holmes N.; RT "The primary structure of HLA-A32 suggests a region involved in RT formation of the Bw4/Bw6 epitopes."; RL J. Immunol. 137:3671-3674(1986). RN [3] RP SEQUENCE FROM N.A. (A*3202). RC TISSUE=Blood; RX MEDLINE=97045038; PubMed=8881042; RA Zino E., Severini G.M., Mazzi B., Bordignon C., Benazzi E., RA Fleischhauer K.; RT "Sequencing of a new HLA-A*32 subtype (A*3202)."; RL Immunogenetics 45:76-77(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-32 ARE KNOWN: A*3201 AND CC A*3202. THE SEQUENCE SHOWN IS THAT OF A*3201. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03907; AAA03605.1; -. DR EMBL; X97120; CAA65786.1; -. DR PIR; A26088; HLHU32. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-32(AW-19) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 175 175 R -> H (IN A*3202). FT /FTId=VAR_004373. FT VARIANT 180 180 L -> Q (IN A*3202). FT /FTId=VAR_004374. SQ SEQUENCE 365 AA; 41048 MW; BF7AF225329E0319 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAHSQTDRE SLRIALRYYN QSEAGSHTIQ MMYGCDVGPD GRLLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA MFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A33_HUMAN STANDARD; PRT; 365 AA. AC P16190; O02954; O02939; DT 01-APR-1990 (Rel. 14, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-33(AW-19) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3301). RX MEDLINE=90038496; PubMed=2478623; RA Kato K., Trapani J.A., Allopenna J., Dupont B., Yang S.Y.; RT "Molecular analysis of the serologically defined HLA-Aw19 antigens. A RT genetically distinct family of HLA-A antigens comprising A29, A31, RT A32, and Aw33, but probably not A30."; RL J. Immunol. 143:3371-3378(1989). RN [2] RP REVISIONS TO 178-179; 210 AND 345 (A*3301). RA Yang S.Y.; RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (A*3301). RA Szmania S., Baxter-Lowe L.A.; RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases. RN [4] RP SEQUENCE FROM N.A. (A*3302). RX MEDLINE=93369838; PubMed=8362415; RA Kato N., Kikuchi A., Kano K., Egawa K., Takiguchi M.; RT "Molecular analysis of a novel HLA-A33 subtype associated with RT HLA-B44."; RL Tissue Antigens 41:211-213(1993). RN [5] RP SEQUENCE FROM N.A. (A*3303). RX MEDLINE=95242316; PubMed=7725315; RA Balas A., Garcia-Sanchez F., Vicario J.L.; RT "Molecular characterization of a novel HLA-A33 allele (A*3303)."; RL Tissue Antigens 45:73-76(1995). RN [6] RP SEQUENCE OF 35-99 AND 122-205 FROM N.A. (A*3301/A*3303). RA Blasczyk R., Wehling J., Salama A.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [7] RP SEQUENCE OF 26-206 FROM N.A. (A*3301/A*3303). RA Gao X., Jakobsen I., Serjeantson S.W.; RL Submitted (JAN-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF AW-33 ARE KNOWN: A*3301 CC (AW-33.1), A*3302 AND A*3303. THE SEQUENCE SHOWN IS THAT OF CC A*3301. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30580; AAB47870.1; -. DR EMBL; U83416; AAB53374.1; -. DR EMBL; L06440; AAA71914.1; -. DR EMBL; U09740; AAA79865.1; -. DR EMBL; X83004; CAA58125.1; -. DR EMBL; X83005; CAA58126.1; -. DR EMBL; X83002; CAA58123.1; -. DR EMBL; X83003; CAA58124.1; -. DR EMBL; U19735; AAB60652.1; -. DR EMBL; U19736; AAB60653.1; -. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT AW-33(AW-19) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 41 41 R -> S (IN A*3302). FT /FTId=VAR_004375. FT VARIANT 195 195 H -> Y (IN A*3302 AND A*3303). FT /FTId=VAR_004376. FT VARIANT 217 218 AV -> PI (IN A*3302). FT /FTId=VAR_004377. FT VARIANT 358 358 M -> V (IN A*3302). FT /FTId=VAR_004378. FT CONFLICT 210 210 K -> R (IN REF. 3). SQ SEQUENCE 365 AA; 40891 MW; 060AE508EADEB328 CRC64; MAVMAPRTLL LLLLGALALT QTWAGSHSMR YFTTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAHSQIDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRHLENGK ETLQRTDPPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A34_HUMAN STANDARD; PRT; 365 AA. AC P30453; P30454; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-34(A-10) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3401/A*3402). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP SEQUENCE FROM N.A. (A*3401/A*3402). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF AW-34 ARE KNOWN: A*3401 CC (AW-34.1) AND A*3402 (AW34.2). THE SEQUENCE SHOWN IS THAT OF CC A*3401. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61704; CAA43873.1; -. DR EMBL; X61705; CAA43874.1; -. DR PIR; S16767; S16767. DR PIR; S16771; S16771. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT AW-34(A-10) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 3 3 I -> V (IN A*3402). FT /FTId=VAR_004379. FT VARIANT 90 90 K -> N (IN A*3402). FT /FTId=VAR_004380. FT VARIANT 121 121 R -> I (IN A*3402). FT /FTId=VAR_004381. FT VARIANT 129 129 P -> S (IN A*3402). FT /FTId=VAR_004382. FT VARIANT 138 138 Q -> R (IN A*3402). FT /FTId=VAR_004383. FT VARIANT 180 180 W -> L (IN A*3402). FT /FTId=VAR_004384. FT VARIANT 312 312 L -> I (IN A*3402). FT /FTId=VAR_004385. SQ SEQUENCE 365 AA; 41055 MW; 063BF63E6E6E01F6 CRC64; MAIMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRK VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG ILAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A36_HUMAN STANDARD; PRT; 365 AA. AC P30455; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-36 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*3601). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE ONLY ALLELE OF AW-36 KNOWN IS A*3601 WHICH IS CC SHOWN HERE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61700; CAA43869.1; -. DR PIR; S16768; S16768. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT AW-36 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 365 AA; 40934 MW; BA00A0085989CD3E CRC64; MAVMAPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQKME PRAPWIEQEG PEYWDQETRN MKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGPD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAVHAAEQR RVYLEGTCVE WLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEL SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYTQAASS DSAQGSDVSL TACKV // ID 1A43_HUMAN STANDARD; PRT; 365 AA. AC P30456; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-43 alpha chain precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*4301). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP SEQUENCE FROM N.A. (A*4301). RX MEDLINE=93235211; PubMed=8475492; RA Madrigal J.A., Hildebrand W.H., Belich M.P., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA du Toit E.D., Parham P.; RT "Structural diversity in the HLA-A10 family of alleles: correlations RT with serology."; RL Tissue Antigens 41:72-80(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE ONLY ALLELE OF AW-43 KNOWN IS A*4301 WHICH IS CC SHOWN HERE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61703; CAA43872.1; -. DR PIR; S16769; S16769. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT AW-43 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 365 AA; 41033 MW; 213FC69745FB4B0B CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDLQTRN VKAHSQTDRA NLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A66_HUMAN STANDARD; PRT; 365 AA. AC P30457; P30458; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-66 alpha chain precursor DE (Aw-66) (A-10). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*6601/A*6602). RX MEDLINE=92044300; PubMed=1940790; RA Madrigal J., Belich M.P., Benjamin R.J., Little A.-M., RA Hildebrand W.H., Mann D.L., Parham P.; RT "Molecular definition of a polymorphic antigen (LA45) of free HLA-A RT and -B heavy chains found on the surfaces of activated B and T RT cells."; RL J. Exp. Med. 174:1085-1095(1991). RN [2] RP SEQUENCE FROM N.A. (A*6602). RX MEDLINE=90237739; PubMed=2139695; RA Schnabl E., Stockinger H., Majdic O., Gaugitsch H., Lindley I.J.D., RA Maurer D., Hajek-Rosenmayr A., Knapp W.; RT "Activated human T lymphocytes express MHC class I heavy chains not RT associated with beta 2-microglobulin."; RL J. Exp. Med. 171:1431-1442(1990). RN [3] RP SEQUENCE OF 1-322 FROM N.A. (A*6601). RA Hurley C., Bei M.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-66 ARE KNOWN: A*6601 CC AND A*6602 (AW67). THE SEQUENCE SHOWN IS THAT OF A*6601. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61711; CAA43880.1; -. DR EMBL; X61712; CAA43881.1; -. DR EMBL; X51745; CAA36034.1; -. DR EMBL; U17571; AAA56781.1; -. DR PIR; S21966; S21966. DR PIR; S21967; S21967. DR PIR; JL0135; JL0135. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-66 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 28 28 S -> W (IN A*6602). FT /FTId=VAR_004386. FT VARIANT 114 114 D -> A (IN A*6602). FT /FTId=VAR_004387. FT VARIANT 187 187 R -> E (IN A*6602). FT /FTId=VAR_004388. SQ SEQUENCE 365 AA; 41082 MW; A3272DBE4008328D CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEDGSHTIQ RMYGCDVGPD GRFLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WETAHEAEQW RAYLEGRCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VIAGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A68_HUMAN STANDARD; PRT; 365 AA. AC P01891; P10315; P79505; O43907; Q9TQG7; Q9TQN5; Q9MYA5; Q9MYC4; AC O19673; O19695; O19794; O19795; O77938; O98010; DT 21-JUL-1986 (Rel. 01, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-68 alpha chain precursor DE (Aw-68) (A-28). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*6802). RX MEDLINE=87252273; PubMed=3496393; RA Holmes N., Ennis P., Wan A.M., Denney D.W., Parham P.; RT "Multiple genetic mechanisms have contributed to the generation of RT the HLA-A2/A28 family of class I MHC molecules."; RL J. Immunol. 139:936-941(1987). RN [2] RP SEQUENCE FROM N.A. (A*6802). RA Domena J.D.; RL Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. (A*6803). RX MEDLINE=97045039; PubMed=8881043; RA Ellexson M., Lau M., Terasaki P., Hildebrand W.; RT "Molecular characterization of HLA-A*6803."; RL Immunogenetics 45:78-79(1996). RN [4] RP SEQUENCE FROM N.A. (A*6808). RX MEDLINE=99321037; PubMed=10395114; RA Cox S.T., Arguello J.R., Marsh S.G.E., Boham E., Lau M., Kwan P.L., RA Madrigal J.A., Little A.M.; RT "Sequence of HLA-A*6808."; RL Tissue Antigens 53:597-600(1999). RN [5] RP SEQUENCE OF 26-206 FROM N.A. (A*6806). RA Bei M., Hurley C.K.; RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP SEQUENCE OF 26-206 FROM N.A. (A*6803). RC TISSUE=Blood; RX MEDLINE=97419180; PubMed=9271640; RA Vargas-Alarcon G., Martinez-Laso J., Gomez-Casado E., Perez-Blas M., RA Granados J., Alegre R., Alvarez M., Zuniga J., Arnaiz-Villena A.; RT "Description of HLA-A*6803 and A*68N in Mazatecan Indians from RT Mexico."; RL Immunogenetics 46:446-447(1997). RN [7] RP SEQUENCE OF 26-206 FROM N.A. (A*6803). RC TISSUE=Blood; RA Blasczyk R.; RL Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases. RN [8] RP SEQUENCE OF 26-206 FROM N.A. (A*6807). RA Hickman H.D., Ellexson M.E., Sidebottom D.A., Turner S., RA Hildebrand W.H.; RT "Sequenced based typing of the HLA-A locus."; RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP SEQUENCE OF 26-206 FROM N.A. (A*6802). RA Edson S.M., Hurley C.K.; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [10] RP SEQUENCE OF 26-206 FROM N.A. (A*6809 AND A*6810). RA Steiner N.K., Hurley C.K., Koester R.P.; RL Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases. RN [11] RP SEQUENCE OF 3-206 FROM N.A. (A*6816). RX MEDLINE=20260982; PubMed=10803837; RA Gomez-Casado E., Martinez-Laso J., Gonzalez-Hevilla M., Longas J., RA Rubio I., Silvera-Redondo C., Garcia-Gomez A., Lowy E., RA Arnaiz-Villena A.; RT "A novel HLA-A*6816 allele possible generated by a point mutation in a RT Chilean from Punta Arenas (Magellan Strait)."; RL Immunogenetics 51:257-260(2000). RN [12] RP SEQUENCE OF 26-206 FROM N.A. (A*6817). RA Hildebrand W.H., Ellexson-Turner M.E.; RT "Robust DNA sequence-based-typing of the HLA-A locus."; RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases. RN [13] RP SEQUENCE OF 26-297 FROM N.A. (A*6801). RX MEDLINE=86055720; PubMed=3877632; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). RN [14] RP PARTIAL SEQUENCE OF 25-294 (A*6801). RX MEDLINE=82247941; PubMed=6179086; RA Lopez de Castro J.A., Strominger J.L., Strong D.M., Orr H.T.; RT "Structure of crossreactive human histocompatibility antigens HLA-A28 RT and HLA-A2: possible implications for the generation of HLA RT polymorphism."; RL Proc. Natl. Acad. Sci. U.S.A. 79:3813-3817(1982). RN [15] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*6801). RX MEDLINE=93078854; PubMed=1448153; RA Guo H.-C., Jardetzky T.S., Garrett T.P.J., Lane W.S., Strominger J.L., RA Wiley D.C.; RT "Different length peptides bind to HLA-Aw68 similarly at their ends RT but bulge out in the middle."; RL Nature 360:364-366(1992). RN [16] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-294 (A*6801). RX MEDLINE=93078855; PubMed=1448154; RA Silver M.L., Guo H.-C., Strominger J.L., Wiley D.C.; RT "Atomic structure of a human MHC molecule presenting an influenza RT virus peptide."; RL Nature 360:367-369(1992). RN [17] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-199 (A*6801). RX MEDLINE=95166800; PubMed=7862664; RA Collins E.J., Garboczi D.N., Karpusas M.N., Wiley D.C.; RT "The three-dimensional structure of a class I major RT histocompatibility complex molecule missing the alpha 3 domain of the RT heavy chain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:1218-1221(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A*68 ARE KNOWN: A*6801 CC (AW68.1), A*6802, A*6803. A*6804, A*6805, A*6806, A*6807, A*6808, CC A*6809, A*6810, A*6816 AND A*6817. THE SEQUENCE SHOWN IS THAT OF CC A*6801. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03861; AAA03602.1; -. DR EMBL; X03070; -; NOT_ANNOTATED_CDS. DR EMBL; X03071; CAB56606.1; -. DR EMBL; U41057; AAB41292.1; -. DR EMBL; AF144013; AAF74211.1; -. DR EMBL; U91628; AAB50567.1; -. DR EMBL; U91627; AAB50567.1; JOINED. DR EMBL; U89946; AAB82079.1; -. DR EMBL; U89947; AAB82080.1; -. DR EMBL; AJ001274; CAA04647.1; -. DR EMBL; AF041372; AAD02208.1; -. DR EMBL; AF041371; AAD02208.1; JOINED. DR EMBL; AF072770; AAC25782.1; -. DR EMBL; AF072769; AAC25782.1; JOINED. DR EMBL; AF135545; AAD22270.1; -. DR EMBL; AF135544; AAD22270.1; JOINED. DR EMBL; AF108431; AAD27539.1; -. DR EMBL; AF108430; AAD27539.1; JOINED. DR EMBL; AJ223972; CAA11708.1; -. DR EMBL; AF268398; AAF73477.1; -. DR EMBL; AF268397; AAF73477.1; JOINED. DR PIR; A24671; HLHUAW. DR PIR; A02187; HLHU28. DR PDB; 2HLA; 15-APR-90. DR PDB; 1HSB; 31-OCT-93. DR PDB; 1TMC; 31-MAR-95. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism; KW 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-68 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...). FT DISULFID 125 188 FT DISULFID 227 283 FT VARIANT 36 36 V -> M (IN A*6802). FT /FTId=VAR_004389. FT VARIANT 86 87 RN -> EE (IN A*6810). FT /FTId=VAR_010362. FT VARIANT 94 94 Q -> H (IN A*6803, A*6804 AND A*6805). FT /FTId=VAR_010363. FT VARIANT 97 97 T -> I (IN A*6804). FT /FTId=VAR_010364. FT VARIANT 98 98 D -> H (IN A*6805). FT /FTId=VAR_010365. FT VARIANT 121 121 M -> R (IN A*6802). FT /FTId=VAR_004390. FT VARIANT 129 129 S -> P (IN A*6802). FT /FTId=VAR_004391. FT VARIANT 138 138 R -> E (IN A*6806). FT /FTId=VAR_010366. FT VARIANT 138 138 R -> H (IN A*6802). FT /FTId=VAR_004392. FT VARIANT 140 140 D -> H (IN A*6806 AND A*6807). FT /FTId=VAR_010367. FT VARIANT 140 140 D -> V (IN A*6817). FT /FTId=VAR_010368. FT VARIANT 140 140 D -> Y (IN A*6802). FT /FTId=VAR_004393. FT VARIANT 175 175 H -> L (IN A*6816). FT /FTId=VAR_010369. FT VARIANT 180 180 W -> L (IN A*6808). FT /FTId=VAR_010370. FT VARIANT 180 180 W -> Q (IN A*6809). FT /FTId=VAR_010371. FT CONFLICT 206 206 T -> A (IN REF. 11). FT CONFLICT 231 231 S -> G (IN REF. 14). FT STRAND 27 36 FT TURN 39 40 FT STRAND 45 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 70 71 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 159 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 207 207 FT STRAND 210 217 FT STRAND 222 233 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 248 FT TURN 250 251 FT STRAND 252 254 FT STRAND 258 259 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 SQ SEQUENCE 365 AA; 40909 MW; 78539C59DB8B1DFC CRC64; MAVMAPRTLV LLLSGALALT QTWAGSHSMR YFYTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDRNTRN VKAQSQTDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGSD GRFLRGYRQD AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQW RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWVA VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1A69_HUMAN STANDARD; PRT; 273 AA. AC P10316; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-69(A-28) alpha chain DE (Fragment). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*6901). RX MEDLINE=86055720; PubMed=3877632; RA Holmes N., Parham P.; RT "Exon shuffling in vivo can generate novel HLA class I molecules."; RL EMBO J. 4:2849-2854(1985). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE ONLY ALLELE OF AW-69 KNOWN IS A*6901 WHICH IS CC SHOWN HERE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03158; CAB56607.1; -. DR EMBL; X03159; CAB56608.1; -. DR PIR; B24671; HLHU69. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein. FT NON_TER 1 1 FT DOMAIN <1 89 EXTRACELLULAR ALPHA-1. FT DOMAIN 90 180 EXTRACELLULAR ALPHA-2. FT DOMAIN 181 273 EXTRACELLULAR ALPHA-3. FT CARBOHYD 85 85 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 100 163 BY SIMILARITY. FT DISULFID 202 258 BY SIMILARITY. FT NON_TER 273 273 SQ SEQUENCE 273 AA; 31677 MW; 21C4996882864F9D CRC64; SHSMRYFYTS VSRPGRGEPR FIAVGYVDDT QFVRFDSDAA SQRMEPRAPW IEQEGPEYWD RNTRNVKAQS QTDRVDLGTL RGYYNQSEAG SHTVQRMYGC DVGSDWRFLR GYHQYAYDGK DYIALKEDLR SWTAADMAAQ TTKHKWEAAH VAEQLRAYLE GTCVEWLRRY LENGKETLQR TDAPKTHMTH HAVSDHEATL RCWALSFYPA EITLTWQRDG EDQTQDTELV ETRPAGDGTF QKWAAVVVPS GQEQRYTCHV QHEGLPKPLT LRW // ID 1A74_HUMAN STANDARD; PRT; 365 AA. AC P30459; O46874; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-74 alpha chain precursor DE (Aw-74) (Aw-19). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (A*7401). RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP SEQUENCE FROM N.A. (A*7401). RA Hurley C.; RL Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE OF 1-206 FROM N.A. (A*7402). RC TISSUE=Blood; RA Blasczyk R.; RL Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE FOLLOWING ALLELES OF A-74 ARE KNOWN: A*7401 CC AND A*7402. THE SEQUENCE SHOWN IS THAT OF A*7401. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61701; CAA43870.1; -. DR EMBL; U17569; AAA56779.1; -. DR EMBL; U17570; AAA56780.1; -. DR EMBL; AJ223060; CAA11063.1; -. DR PIR; S16770; S16770. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; Polymorphism. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT A-74 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT VARIANT 23 23 R -> W (IN A*7402). FT /FTId=VAR_010375. SQ SEQUENCE 365 AA; 40891 MW; C94BF2569A852371 CRC64; MAVMAPRTLL LLLLGALALT QTRAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASQRME PRAPWIEQEG PEYWDQETRN VKAHSQTDRV DLGTLRGYYN QSEAGSHTIQ MMYGCDVGPD GRLLRGYQQD AYDGKDYIAL NEDLRSWTAA DMAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAS VVVPSGQEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLFGA MFAGAVVAAV RWRRKSSDRK GGSYSQAASS DSAQGSDMSL TACKV // ID 1A80_HUMAN STANDARD; PRT; 365 AA. AC Q09160; DT 01-NOV-1995 (Rel. 32, Created) DT 01-NOV-1995 (Rel. 32, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, AW-80(A-1) alpha chain DE precursor. GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94245293; PubMed=8188325; RA Balas A., Garcia-Sanchez F., Gomez-Reino F., Vicario J.L.; RT "Characterization of a new and highly distinguishable HLA-A allele in RT a Spanish family."; RL Immunogenetics 39:452-452(1994). RN [2] RP SEQUENCE FROM N.A. RA Domena J.D.; RL Submitted (JUN-1993) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- POLYMORPHISM: THE ONLY ALLELE OF AW-80 KNOWN IS A*8001 WHICH IS CC SHOWN HERE. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U03754; AAC04322.1; -. DR EMBL; L18898; AAA17012.1; -. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 365 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT AW-80(A-1) ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 365 AA; 40791 MW; CE1BC1CD60CA8FA8 CRC64; MAVMPPRTLL LLLSGALALT QTWAGSHSMR YFFTSVSRPG RGEPRFIAVG YVDDSQFVQF DSDAASQRME PRAPWIEQEE PEYWDEETRN VKAHSQTNRA NLGTLRGYYN QSEDGSHTIQ IMYGCDVGSD GRFLRGYRQD AYDGKDYIAL NEDLRSWTAA DMAAQITKRK WEAARRAEQL RAYLEGECVD GLRRYLENGK ETLQRTDPPK THMTHHPISD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGKEKR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IIAGLVLLGA VIAGAVVAAV MWRKKSSVRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1AXX_HUMAN STANDARD; PRT; 275 AA. AC P10313; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, A-10 alpha chain (Fragment). GN HLA-A OR HLAA. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86033791; PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of RT locus-specific oligonucleotide probes specific for HLA-A, HLA-B, and RT HLA-C genes."; RL J. Biol. Chem. 260:13414-13423(1985). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11887; AAA52656.1; -. DR PIR; B24512; HLHU10. DR HSSP; Q95352; 1HHH. DR MIM; 142800; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein. FT NON_TER 1 1 FT DOMAIN <1 24 EXTRACELLULAR ALPHA-1. FT DOMAIN 25 116 EXTRACELLULAR ALPHA-2. FT DOMAIN 117 208 EXTRACELLULAR ALPHA-3. FT DOMAIN 209 218 CONNECTING PEPTIDE. FT TRANSMEM 219 242 FT DOMAIN 243 275 CYTOPLASMIC TAIL. FT CARBOHYD 20 20 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 35 98 BY SIMILARITY. FT DISULFID 137 193 BY SIMILARITY. SQ SEQUENCE 275 AA; 30548 MW; 77E9BD3CF359DDAB CRC64; VKAQSQTHRV DLGTLRGYYN QSEAVSHTVQ RMYGCDVGSD GRFLRGYHQV AYDGKDYIAL KEDLRSWTAA DMAAQTTKHK WEAAHVAEQL RAYLEGTCVE WLRRYLENGK ETLQRTDAPK THMTHHAVSD HEATLRCWAL SFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAV MWRRKSSDRK GGSYSQAASS DSAQGSDVSL TACKV // ID 1B01_GORGO STANDARD; PRT; 362 AA. AC P30379; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-B0101 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60255; CAA42807.1; -. DR PIR; JH0539; JH0539. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 362 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-B0101 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40170 MW; 419EEE29817165A4 CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTIQ RMFGCDVGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B01_PANTR STANDARD; PRT; 359 AA. AC P13750; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, B-1 alpha chain precursor DE (Fragment). OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., RA Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP REVISIONS. RA Mayer W.; RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13115; CAA31507.1; -. DR PIR; S03537; S03537. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT NON_TER 1 1 FT SIGNAL <1 20 FT CHAIN 21 359 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-1 ALPHA CHAIN. FT DOMAIN 21 110 EXTRACELLULAR ALPHA-1. FT DOMAIN 111 202 EXTRACELLULAR ALPHA-2. FT DOMAIN 203 294 EXTRACELLULAR ALPHA-3. FT DOMAIN 295 305 CONNECTING PEPTIDE. FT TRANSMEM 306 329 FT DOMAIN 330 359 CYTOPLASMIC TAIL. FT DISULFID 121 184 BY SIMILARITY. FT DISULFID 223 279 BY SIMILARITY. FT CARBOHYD 106 106 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 359 AA; 40173 MW; 858ACBAF74D6829D CRC64; APRTVLLLLS AALALTETWA GSHSMRYFYT SVSRPGRGEP RFITVGYVDD TQFVRFDSDA ASPRMEPRAP WIEQEGPEYW DRETRNMKAS AQTDRENLRI ALRYYNQSEA GSHTWQTMYG CDMGPDGRLL RGYGQYAYDG KDYIALNEDL SSWTAADTAA QITQRKWEAA REAEQRRAYL EGTCVEWLRR YLENGKETLQ RADPPKTHVT HHPISDHEAT LRCWALGFYP AEITLTWQRD GEDQTQDTEL VETRPEGDRT FQKWAAVVVP SGEEQRYTCH VQHEGLPKPL TLRWEPSSQS TIPIVGIVAG LAVLVVTVAV VAVVAAVMCR RKSSGGKGGS YSQAASSDSA QGSDVSLTA // ID 1B01_SAGOE STANDARD; PRT; 365 AA. AC P30516; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, B alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Platyrrhini; Callitrichidae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33476; AAA36952.1; ALT_INIT. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40999 MW; B79A9E1FE54C5634 CRC64; MTVMAPRTLL LLLSGALVLT ETWAGSHSMR YFSTAVSRPG REEPRYIEVG YVDDTQFVRF DSDAASPRME PRAQWVEKEG REYWEEETQR AKAFAQTFRV NLQTALGYYN QSEAGSHTIQ MMSGCDLGPD GRLLRGYDQH AYDGKDYISL NEDLRSWTAA DVAAQITQRK WEAANEAERT RAYLEGTCVE WLHRYLENGK ETLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DMELVETRPT GNGTFQKWAA VVVLSGEEHR YTCHVQHEGL PEPLTLRWEP PSQPTIPIMG IVAILAILGA VVTGAVVTAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1B02_GORGO STANDARD; PRT; 362 AA. AC P30380; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-B0102 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60693; CAA43101.1; -. DR PIR; JH0540; JH0540. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 362 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-B0102 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40204 MW; E19EEE2B7CC7BECD CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTFQ RMFGCDVGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B02_HUMAN STANDARD; PRT; 362 AA. AC P01889; DT 21-JUL-1986 (Rel. 01, Created) DT 01-FEB-1991 (Rel. 17, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-7 B*0702 alpha chain DE precursor (B7.2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90315860; PubMed=2700944; RA Parham P., Benjamin R.J., Chen B.P., Clayberger C., Ennis P.D., RA Krensky A.M., Lawlor D.A., Littman D.R., Norment A.M., Orr H.T., RA Salter R.D., Zemmour J.; RT "Diversity of class I HLA molecules: functional and evolutionary RT interactions with T cells."; RL Cold Spring Harb. Symp. Quant. Biol. 54:529-543(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=85287366; PubMed=2993161; RA Sood A.K., Pan J., Biro P.A., Pereira D., Srivastava R., Reddy V.B., RA Duceman B.W., Weissman S.M.; RT "Structure and polymorphism of class I MHC antigen mRNA."; RL Immunogenetics 22:101-121(1985). RN [4] RP SEQUENCE FROM N.A. RA Ellexson M.E., Zhang L., Hildebrand W.H.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [5] RP SEQUENCE OF 25-295. RX MEDLINE=80088278; PubMed=518865; RA Orr H.T., Lopez de Castro J.A., Lancet D., Strominger J.L.; RT "Complete amino acid sequence of a papain-solubilized human RT histocompatibility antigen, HLA-B7. 2. Sequence determination and RT search for homologies."; RL Biochemistry 18:5711-5720(1979). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32317; AAA36230.1; -. DR EMBL; M16102; AAA59622.1; ALT_SEQ. DR EMBL; U29057; AAA91229.1; -. DR PIR; A02185; HLHUB7. DR PIR; B35997; B35997. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-7 B*0702 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...). FT DISULFID 125 188 FT DISULFID 227 283 FT CONFLICT 15 18 AALA -> GPW (IN REF. 3). FT CONFLICT 266 266 Q -> E (IN REF. 5). FT CONFLICT 268 268 W -> S (IN REF. 3). FT CONFLICT 297 297 R -> G (IN REF. 3). FT CONFLICT 314 315 GL -> RP (IN REF. 3). SQ SEQUENCE 362 AA; 40460 MW; 5E5A7BDE031403D6 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B02_PANTR STANDARD; PRT; 362 AA. AC P13751; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, B-2 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89030641; PubMed=2460344; RA Mayer W.E., Jonker M., Klein D., Ivanyi P., van Seventer G., RA Klein J.; RT "Nucleotide sequences of chimpanzee MHC class I alleles: evidence for RT trans-species mode of evolution."; RL EMBO J. 7:2765-2774(1988). RN [2] RP REVISIONS. RA Mayer W.; RL Submitted (FEB-1989) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X13116; CAA31508.1; -. DR PIR; S03538; S03538. DR HSSP; P30685; 1A9E. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-2 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40488 MW; FFDB2991044DAA83 CRC64; MQVTAPRTVL LLLSAALALT ETWAGSHSMK YFYTAVSRPG RGEPRFISVG YVDDTQFVWF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNAQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDMGPD GRLLRGYEQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARWAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B03_GORGO STANDARD; PRT; 362 AA. AC P30381; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-B0103 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60254; CAA42806.1; -. DR PIR; JH0541; JH0541. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 362 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-B0103 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40248 MW; 3DEE82572BD81469 CRC64; MRVTAPRTLL LLLSAALALT ETWAGSHSMR YFDTAVSRPG RGEPRFITVG YVDDTQFVRF DSDAASPRME PRAPWIEQEG PEYWDRETQT SKAQAQTDRE NLRIALRYYN QSEAGSHTIQ WMYGCDMGPD GRLLRGYSQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGR ETLQRADTPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEER YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVTAV ICRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B04_GORGO STANDARD; PRT; 363 AA. AC P30382; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-B0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60253; CAA42805.1; -. DR PIR; JH0542; JH0542. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 363 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-B0201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 363 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 363 AA; 40439 MW; A8CA366ED9A2B264 CRC64; MQVTAPRTLL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTQFVWF DSDAASPRKE PRTPWIEQEG PEYWDRETQI SKTNTQTYRV GLGTLRGYYN QSEDGSHTIQ RMYGCDMGPD GRLLRGYSQL AYDGKDYLAL NEDLSSWTAA DTAAQITQRK WEAARAAEQE RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCRVQHEGL PEPLTLRWEP SSQSTIPIVG IVAGLAVLVV TVAVVAVVAA VMCRRKSSGG KGGSYSQAAS SDSAQGSDVS LTA // ID 1B04_HUMAN STANDARD; PRT; 362 AA. AC P30460; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-8 B*0801 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 25-300. RX MEDLINE=97130420; PubMed=8976183; RA Reid S.W., McAdam S., Smith K.J., Klenerman P., O'Callaghan C.A., RA Harlos K., Jakobsen B.K., McMichael A.J., Bell J.I., Stuart D.I., RA Jones E.Y.; RT "Antagonist HIV-1 Gag peptides induce structural changes in HLA B8."; RL J. Exp. Med. 184:2279-2286(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24036; AAA52662.1; -. DR PDB; 1AGB; 16-JUN-97. DR PDB; 1AGC; 16-JUN-97. DR PDB; 1AGD; 16-JUN-97. DR PDB; 1AGE; 16-JUN-97. DR PDB; 1AGF; 16-JUN-97. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-8 B*0801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40331 MW; 9B2A9760021680DF CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFDTAMSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI FKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B05_HUMAN STANDARD; PRT; 362 AA. AC P30461; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-13 B*1301 alpha chain DE precursor (B13.1). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88152906; PubMed=3257938; RA Zemmour J., Ennis P.D., Parham P., Dupont B.; RT "Comparison of the structure of HLA-Bw47 to HLA-B13 and its RT relationship to 21-hydroxylase deficiency."; RL Immunogenetics 27:281-287(1988). RN [3] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=96053518; PubMed=7558929; RA Lin L., Tokunaga K., Nakajima F., Ishikawa Y., Kashiwase K., RA Tanaka H., Kuwata S., Sideltseva E., Akaza T., Tadokoro K., RA Shibata Y., Chandanayingyong D., Juji T.; RT "Both HLA-B*1301 and B*1302 exist in Asian populations and are RT associated with different haplotypes."; RL Hum. Immunol. 43:51-56(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24041; AAA59660.1; -. DR EMBL; M19757; AAA52657.1; -. DR EMBL; D50291; BAA08822.1; -. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-13 B*1301 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40474 MW; 28FF66B20961C75C CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTQFVRF DSDATSPRMA PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRTALRYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQLK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B07_HUMAN STANDARD; PRT; 362 AA. AC P30462; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-14 B*1401 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24040; AAA59661.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-14 B*1401 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40358 MW; 9039122CC400337F CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ WMYGCDVGPD GRLLRGYNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B08_HUMAN STANDARD; PRT; 362 AA. AC P30463; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-65(B-14) B*1402 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24032; AAA59664.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-65(B-14) B*1402 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40342 MW; EC2225DADE09DBAA CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ WMYGCDVGPD GRLLRGYNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B10_HUMAN STANDARD; PRT; 362 AA. AC P30464; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-75(B-15) B*1502 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92196792; PubMed=1801311; RA Little A.-M., Parham P.; RT "The HLA-Bw75 subtype of B15: molecular characterization and RT comparison with crossreacting antigens."; RL Tissue Antigens 38:186-190(1991). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=96369309; PubMed=8773315; RA Lin L., Tokunaga K., Tanaka H., Nakajima F., Imanishi T., RA Kashiwase K., Bannai M., Mizuno S., Akaza T., Tadokoro K., RA Shibata Y., Juji T.; RT "Further molecular diversity in the HLA-B15 group."; RL Tissue Antigens 47:265-274(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M75138; AAA59630.1; -. DR EMBL; D50293; BAA08824.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-75(B-15) B*1502 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40338 MW; CE6367B4C1D3EAF1 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRNTQI SKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B11_HUMAN STANDARD; PRT; 362 AA. AC P30465; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-72(BW-70) B*1503 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61709; CAA43878.1; -. DR PIR; S16789; S16789. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-72(BW-70) B*1503 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40387 MW; E5F11231A3595D3F CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B12_HUMAN STANDARD; PRT; 362 AA. AC P30513; DT 01-APR-1993 (Rel. 25, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-62 B*1504 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269956; PubMed=1589035; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RA Ramos M., Barber D.F., Layrisse Z., de Castro J.A.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84382; AAA59632.1; -. DR EMBL; U70528; AAB16918.1; -. DR PIR; S24433; S24433. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-62 B*1504 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40406 MW; 76E80A4507E23086 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQW RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B13_HUMAN STANDARD; PRT; 362 AA. AC P30466; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-18 B*1801 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24039; AAA59662.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-18 B*1801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40275 MW; 106552F4A0F28E17 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFISVG YVDGTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRHLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B14_HUMAN STANDARD; PRT; 361 AA. AC P03989; DT 23-OCT-1986 (Rel. 02, Created) DT 13-AUG-1987 (Rel. 05, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 alpha chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86138405; PubMed=3912316; RA Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.; RT "Organization, sequence and expression of the HLA-B27 gene: a RT molecular approach to analyze HLA and disease associations."; RL Immunobiology 170:367-380(1985). RN [2] RP SEQUENCE OF 25-361 FROM N.A. RX MEDLINE=86149317; PubMed=3485286; RA Szoets H., Riethmueller G., Weiss E., Meo T.; RT "Complete sequence of HLA-B27 cDNA identified through the RT characterization of structural markers unique to the HLA-A, -B, and RT -C allelic series."; RL Proc. Natl. Acad. Sci. U.S.A. 83:1428-1432(1986). RN [3] RP SEQUENCE OF 25-295. RX MEDLINE=85226361; PubMed=2408663; RA Ezquerra A., Bragado R., Vega M.A., Strominger J.L., Woody J., RA Lopez de Castro J.A.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B27."; RL Biochemistry 24:1733-1741(1985). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-300. RX MEDLINE=92405152; PubMed=1525820; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The three-dimensional structure of HLA-B27 at 2.1-A resolution RT suggests a general mechanism for tight peptide binding to MHC."; RL Cell 70:1035-1048(1992). RN [5] RP X-RAY CRYSTALLOGRAPHY. RX MEDLINE=92018187; PubMed=1922337; RA Madden D.R., Gorga J.C., Strominger J.L., Wiley D.C.; RT "The structure of HLA-B27 reveals nonamer self-peptides bound in an RT extended conformation."; RL Nature 353:321-325(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -!- DISEASE: THIS PROTEIN CORRELATES WITH THE DEVELOPMENT OF CC ANKYLOSING SPONDYLITIS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03945; CAA27578.1; ALT_TERM. DR PIR; A25128; HLHUB2. DR PIR; S07441; S07441. DR PDB; 1HSA; 15-OCT-92. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 361 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-27 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 361 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...). FT DISULFID 125 188 FT DISULFID 227 283 FT CONFLICT 206 206 A -> V (IN REF. 2). FT CONFLICT 266 266 Q -> E (IN REF. 3). FT STRAND 27 38 FT TURN 39 41 FT STRAND 42 52 FT TURN 53 54 FT STRAND 55 61 FT TURN 62 63 FT STRAND 70 71 FT HELIX 74 76 FT TURN 77 78 FT HELIX 81 108 FT TURN 109 110 FT TURN 113 114 FT STRAND 118 127 FT TURN 129 130 FT STRAND 133 142 FT TURN 143 144 FT STRAND 145 150 FT TURN 152 153 FT STRAND 157 159 FT HELIX 162 173 FT TURN 174 175 FT HELIX 176 185 FT TURN 186 186 FT HELIX 187 198 FT TURN 199 199 FT HELIX 200 203 FT TURN 204 204 FT STRAND 207 207 FT STRAND 210 217 FT STRAND 222 233 FT STRAND 238 243 FT TURN 244 245 FT STRAND 246 247 FT HELIX 249 251 FT STRAND 253 254 FT STRAND 258 259 FT STRAND 265 274 FT TURN 275 276 FT HELIX 278 280 FT STRAND 281 286 FT TURN 288 289 FT STRAND 294 296 SQ SEQUENCE 361 AA; 40464 MW; 2F8293299B52A47F CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASA TVPRALMCLS Q // ID 1B15_HUMAN STANDARD; PRT; 362 AA. AC P10317; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 B*2702 alpha chain DE precursor (B-27K) (B27.2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86220133; PubMed=3011411; RA Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.; RT "Gene conversion-like mechanisms may generate polymorphism in human RT class I genes."; RL EMBO J. 5:547-552(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96086486; PubMed=7482496; RA Moses J.H., Marsh S.G., Arnett K.L., Adams E.J., Bodmer J.G., RA Parham P.; RT "On the nucleotide sequences of B*2702 and B*2705."; RL Tissue Antigens 46:50-53(1995). RN [3] RP SEQUENCE OF 86-107 AND 171-181. RX MEDLINE=86042671; PubMed=2414775; RA Vega M.A., Ezquerra A., Rojo S., Aparicio P., Bragado R., RA Lopez de Castro J.A.; RT "Structural analysis of an HLA-B27 functional variant: identification RT of residues that contribute to the specificity of recognition by RT cytolytic T lymphocytes."; RL Proc. Natl. Acad. Sci. U.S.A. 82:7394-7398(1985). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03664; CAA27301.1; -. DR EMBL; X03667; CAA27301.1; JOINED. DR EMBL; L38504; AAA69724.1; -. DR PIR; B25092; HLHUBK. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-27 B*2702 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40397 MW; C8D5A72ED32E2F88 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE NLRIALRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B16_HUMAN STANDARD; PRT; 362 AA. AC P19373; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 B*2703 alpha chain DE precursor (B-27D). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88227491; PubMed=3286582; RA Choo S.Y., St John T., Orr H.T., Hansen J.A.; RT "Molecular analysis of the variant alloantigen HLA-B27d (HLA-B*2703) RT identifies a unique single amino acid substitution."; RL Hum. Immunol. 21:209-219(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M54883; AAA59616.1; -. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-27 B*2703 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40402 MW; 8CC7B45FE8999036 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEHWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B18_HUMAN STANDARD; PRT; 362 AA. AC P10318; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 B*2705 alpha chain DE precursor (B-27W) (B27.1). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86220133; PubMed=3011411; RA Seemann G.H.A., Rein R.S., Brown C.S., Ploegh H.L.; RT "Gene conversion-like mechanisms may generate polymorphism in human RT class I genes."; RL EMBO J. 5:547-552(1986). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=86138405; PubMed=3912316; RA Weiss E.H., Kuon W., Doerner C., Lang M., Riethmueller G.; RT "Organization, sequence and expression of the HLA-B27 gene: a RT molecular approach to analyze HLA and disease associations."; RL Immunobiology 170:367-380(1985). RN [3] RP 3D-STRUCTURE MODELING OF 115-206. RX MEDLINE=95148615; PubMed=7846047; RA Rognan D., Scapozza L., Folkers G., Daser A.; RT "Rational design of nonnatural peptides as high-affinity ligands for RT the HLA-B*2705 human leukocyte antigen."; RL Proc. Natl. Acad. Sci. U.S.A. 92:753-757(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X03665; CAA27302.1; -. DR EMBL; X03666; CAA27302.1; JOINED. DR EMBL; M12967; AAA36221.1; -. DR PIR; A25092; HLHUBW. DR PDB; 1ROG; 30-SEP-94. DR PDB; 1ROH; 30-SEP-94. DR PDB; 1ROI; 30-SEP-94. DR PDB; 1ROJ; 30-SEP-94. DR PDB; 1ROK; 30-SEP-94. DR PDB; 1ROL; 30-SEP-94. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-27 B*2705 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40428 MW; C8D2F154E3292031 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE DLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B19_HUMAN STANDARD; PRT; 362 AA. AC Q08136; DT 01-NOV-1995 (Rel. 32, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 B*2706 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94102824; PubMed=8276469; RA Vilches C., de Pablo R., Kreisler M.; RT "Nucleotide sequence of HLA-B*2706."; RL Immunogenetics 39:219-219(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96134006; PubMed=8550101; RA Rudwaleit M., Bowness P., Wordsworth P.; RT "The nucleotide sequence of HLA-B*2704 reveals a new amino acid RT substitution in exon 4 which is also present in HLA-B*2706."; RL Immunogenetics 43:160-162(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X73578; CAA51980.1; -. DR EMBL; U35734; AAC50447.1; -. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-27 B*2706 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1 (BY SIMILARITY). FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2 (BY SIMILARITY). FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3 (BY SIMILARITY). FT DOMAIN 299 308 CONNECTING PEPTIDE (BY SIMILARITY). FT TRANSMEM 309 332 BY SIMILARITY. FT DOMAIN 333 362 CYTOPLASMIC TAIL (BY SIMILARITY). FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (POTENTIAL). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CONFLICT 235 235 A -> G (IN REF. 1). SQ SEQUENCE 362 AA; 40456 MW; B5F5CFE59000C487 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI CKAKAQTDRE SLRTLLRYYN QSEAGSHTLQ NMYGCDVGPD GRLLRGYDQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B20_HUMAN STANDARD; PRT; 338 AA. AC P30467; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-27 B*2707 alpha chain DE (B27-HS). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91268545; PubMed=1711072; RA Choo Y.S., Fan L.A., Hansen J.A.; RT "A novel HLA-B27 allele maps B27 allospecificity to the region around RT position 70 in the alpha 1 domain."; RL J. Immunol. 147:174-180(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M62852; AAA59647.1; -. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein. FT DOMAIN 1 90 EXTRACELLULAR ALPHA-1. FT DOMAIN 91 182 EXTRACELLULAR ALPHA-2. FT DOMAIN 183 274 EXTRACELLULAR ALPHA-3. FT DOMAIN 275 284 CONNECTING PEPTIDE. FT TRANSMEM 285 308 FT DOMAIN 309 338 CYTOPLASMIC TAIL. FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 101 164 BY SIMILARITY. FT DISULFID 203 259 BY SIMILARITY. SQ SEQUENCE 338 AA; 37804 MW; B6529066C87317C7 CRC64; GSHSMRYFHT SVSRPGRGEP RFITVGYVDD TLFVRFDSDA ASPREEPRAP WIEQEGPEYW DRETQICKAK AQTDREDLRT LLRYYNQSEA GSHTLQSMYG CDVGPDGRLL RGHNQYAYDG KDYIALNEDL RSWTAADTAA QITQRKWEAA RVAEQLRAYL EGECVEWLRR YLENGKETLQ RADPPKTHVT HHPISDHEAT LRCWALGFYP AEITLTWQRD GEDQTQDTEL VETRPAGDRT FQKWAAVVVP SGEEQRYTCH VQHEGLPKPL TLRWEPSSQS TVPIVGIVAG LAVLAVVVIG AVVAAVMCRR KSSGGKGGSY SQAACSDSAQ GSDVSLTA // ID 1B21_HUMAN STANDARD; PRT; 362 AA. AC P30685; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3501 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89339610; PubMed=2788131; RA Ooba T., Hayashi H., Karaki S., Tanabe M., Kano K., Takiguchi M.; RT "The structure of HLA-B35 suggests that it is derived from HLA-Bw58 RT by two genetic mechanisms."; RL Immunogenetics 30:76-80(1989). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 25-300. RX MEDLINE=96209671; PubMed=8624811; RA Smith K.J., Reid S.W., Stuart D.I., McMichael A.J., Jones E.Y., RA Bell J.I.; RT "An altered position of the alpha 2 helix of MHC class I is revealed RT by the crystal structure of HLA-B*3501."; RL Immunity 4:203-214(1996). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). RX MEDLINE=99096952; PubMed=9878435; RA Menssen R., Orth P., Ziegler A., Saenger W.; RT "Decamer-like conformation of a nona-peptide bound to HLA-B*3501 due RT to non-standard positioning of the C terminus."; RL J. Mol. Biol. 285:645-653(1999). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28115; AAA59617.1; -. DR EMBL; M28109; AAA59617.1; JOINED. DR EMBL; M28110; AAA59617.1; JOINED. DR EMBL; M28111; AAA59617.1; JOINED. DR EMBL; M28112; AAA59617.1; JOINED. DR EMBL; M28113; AAA59617.1; JOINED. DR EMBL; M28114; AAA59617.1; JOINED. DR PIR; A45880; A45880. DR PDB; 1A1N; 08-APR-98. DR PDB; 1A9B; 18-NOV-98. DR PDB; 1A9E; 18-NOV-98. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3501 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 FT DISULFID 227 283 SQ SEQUENCE 362 AA; 40455 MW; 52906854FC43E7A6 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B22_HUMAN STANDARD; PRT; 362 AA. AC P30468; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3502 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91365651; PubMed=1890016; RA Chertkoff L.P., Herrera M., Fainboim L., Satz M.L.; RT "Complete nucleotide sequence of a genomic clone encoding HLA-B35 RT isolated from a Caucasian individual of Hispanic origin. RT Identification of a new variant of HLA-B35."; RL Hum. Immunol. 31:153-158(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M63454; AAA59682.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3502 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40564 MW; 3325E32C4DEB49A6 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRFLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B23_HUMAN STANDARD; PRT; 362 AA. AC P30469; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3503 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92176661; PubMed=1541831; RA Zemmour J., Little A.M., Schendel D.J., Parham P.; RT "The HLA-A,B 'negative' mutant cell line C1R expresses a novel RT HLA-B35 allele, which also has a point mutation in the translation RT initiation codon."; RL J. Immunol. 148:1941-1948(1992). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=95279930; PubMed=7759996; RA Beck Y., Satz L., Takamiya Y., Nakayama S., Ling L., Ishikawa Y., RA Nagao T., Uchida H., Tokunaga K., Mueller C., Juji T., Takiguchi M.; RT "Polymorphism of human minor histocompatibility antigens: T cell RT recognition of human minor histocompatibility peptides presented by RT HLA-B35 subtype molecules."; RL J. Exp. Med. 181:2037-2048(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M81798; AAA59684.1; -. DR EMBL; D50299; BAA08828.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3503 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40515 MW; A28DCF9E80E4288E CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B24_HUMAN STANDARD; PRT; 354 AA. AC P30470; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3504 alpha chain DE precursor (Fragment). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269956; PubMed=1589035; RA Watkins D.I., McAdam S.N., Liu X., Stang C.R., Milford E.L., RA Levine C.G., Garber T.L., Dogon A.L., Lord C.I., Ghim S.H., RA Troup G.M., Hughes A.L., Letvin N.L.; RT "New recombinant HLA-B alleles in a tribe of South American RT Amerindians indicate rapid evolution of MHC class I loci."; RL Nature 357:329-333(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86403; -; NOT_ANNOTATED_CDS. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT NON_TER 1 1 FT SIGNAL <1 16 FT CHAIN 17 354 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3504 ALPHA CHAIN. FT DOMAIN 17 106 EXTRACELLULAR ALPHA-1. FT DOMAIN 107 198 EXTRACELLULAR ALPHA-2. FT DOMAIN 199 290 EXTRACELLULAR ALPHA-3. FT DOMAIN 291 300 CONNECTING PEPTIDE. FT TRANSMEM 301 324 FT DOMAIN 325 354 CYTOPLASMIC TAIL. FT CARBOHYD 102 102 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 117 180 BY SIMILARITY. FT DISULFID 219 275 BY SIMILARITY. SQ SEQUENCE 354 AA; 39617 MW; 5FDF7C299D5EC93B CRC64; VLLLLWGAVA LTETWAGSHS MRYFYTAMSR PGRGEPRFIA VGYVDDTQFV RFDSDAASPR TEPRAPWIEQ EGPEYWDRNT QIFKTNTQTY RESLRNLRGY YNQSEAGSHI IQRMYGCDLG PDGRLLRGHN QYAYDGKDYI ALNEDLSSWT AADTAAQITQ RKWEAARVAE QLRAYLEGLC VEWLRRYLEN GKETLQRADP PKTHVTHHPV SDHEATLRCW ALGFYPAEIT LTWQRDGEDQ TQDTELVETR PAGDRTFQKW AAVVVPSGEE QRYTCHVQHE GLPKPLTLRW EPSSQSTIPI VGIVAGLAVL AVVVIGAVVA TVMCRRKSSG GKGGSYSQAA SSDSAQGSDV SLTA // ID 1B25_HUMAN STANDARD; PRT; 362 AA. AC P30471; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3505 alpha chain DE precursor (B35-G). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84385; AAA59635.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3505 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40374 MW; 9E601F49238BC337 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B26_HUMAN STANDARD; PRT; 362 AA. AC P30472; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3506 alpha chain DE precursor (B35-K). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84381; AAA59631.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3506 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40514 MW; 2E0707320C0CE602 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B27_HUMAN STANDARD; PRT; 362 AA. AC P30473; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3507 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93303752; PubMed=8316945; RA Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.; RT "Isolation and characterization of two new functional subtypes of RT HLA-B35."; RL Tissue Antigens 41:143-147(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04695; AAA59694.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3507 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40497 MW; FAE91E87203532A0 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPV RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B28_HUMAN STANDARD; PRT; 362 AA. AC P30474; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-35 B*3508 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93303752; PubMed=8316945; RA Theiler G., Pando M., Delfino J.M., Takiguchi M., Satz M.L.; RT "Isolation and characterization of two new functional subtypes of RT HLA-B35."; RL Tissue Antigens 41:143-147(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94186367; PubMed=8138421; RA Steinle A., Reinhardt C., Noessner E., Uchanska-Ziegler B., RA Ziegler A., Schendel D.J.; RT "Microheterogeneity in HLA-B35 alleles influences peptide-dependent RT allorecognition by cytotoxic T cells but not binding of a peptide- RT restricted monoclonal antibody."; RL Hum. Immunol. 38:261-269(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L04696; AAA52674.1; -. DR EMBL; Z22651; CAA80366.1; -. DR PIR; S32754; S32754. DR PIR; S32755; S32755. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-35 B*3508 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40498 MW; AFA3456AFC5DEF6B CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQR RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B29_HUMAN STANDARD; PRT; 362 AA. AC P18463; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-37 B*3701 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32320; AAA36233.1; -. DR PIR; C35997; C35997. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-37 B*3701 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40456 MW; FAB4375F05474725 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE DLRTLLRYYN QSEAGSHTIQ RMSGCDVGPD GRLLRGYNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B31_HUMAN STANDARD; PRT; 362 AA. AC P30475; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-39 B*3901 alpha chain DE precursor (B39.1). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93131294; PubMed=8420828; RA Kato N., Karaki S., Kashiwase K., Mueller C., Akaza T., Juji T., RA Kano K., Takiguchi M.; RT "Molecular analysis of HLA-B39 subtypes."; RL Immunogenetics 37:212-216(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94052; AAA52658.1; -. DR EMBL; M94051; AAA52660.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-39 B*3901 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40328 MW; 422698063DEAB039 CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI CKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B32_HUMAN STANDARD; PRT; 362 AA. AC P30476; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-39 B*3902 alpha chain DE precursor (B39.2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93131294; PubMed=8420828; RA Kato N., Karaki S., Kashiwase K., Mueller C., Akaza T., Juji T., RA Kano K., Takiguchi M.; RT "Molecular analysis of HLA-B39 subtypes."; RL Immunogenetics 37:212-216(1993). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=95242308; PubMed=7725307; RA Adams E.J., Martinez-Naves E., Arnett K.L., Little A.M., RA Tyan D.B., Parham P.; RT "HLA-B16 antigens: sequence of the ST-16 antigen, further definition RT of two B38 subtypes and evidence for convergent evolution of RT B*3902."; RL Tissue Antigens 45:18-26(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M94053; AAA52659.1; -. DR EMBL; U04243; AAA87396.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-39 B*3902 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40327 MW; 31CCC8099810E03B CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNTQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHNQF AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RTYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B33_HUMAN STANDARD; PRT; 270 AA. AC P01890; DT 21-JUL-1986 (Rel. 01, Created) DT 21-JUL-1986 (Rel. 01, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-60(B-40) B*4001 alpha chain DE (Fragment). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE. RX MEDLINE=84000412; PubMed=6193808; RA Lopez de Castro J.A., Bragado R., Strong D.M., Strominger J.L.; RT "Primary structure of papain-solubilized human histocompatibility RT antigen HLA-B40 (-Bw60). An outline of alloantigenic determinants."; RL Biochemistry 22:3961-3969(1983). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). DR PIR; A02186; HLHU40. DR HSSP; P30685; 1A9B. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Glycoprotein. FT DOMAIN 1 90 EXTRACELLULAR ALPHA-1. FT DOMAIN 91 181 EXTRACELLULAR ALPHA-2. FT DOMAIN 182 >270 EXTRACELLULAR ALPHA-3. FT CARBOHYD 86 86 N-LINKED (GLCNAC...). FT DISULFID 101 163 FT DISULFID 202 258 FT NON_TER 270 270 SQ SEQUENCE 270 AA; 31205 MW; 5E7C5057E4EEC68B CRC64; GSHSMRYFHT AMSRPGRGEP RFITVGYVDD TLFVRFDSDA TSPRKEPRAP WIEQEGPEYW DRETQISKTN TQTYRESLRN LRGYYNQSEA GSHTLQRMYG CDVGPDGRLL RGHNQYAYDG KDYIALNEDL RSWTAADTAA QIQRKLEAAR VAEQLRAYLE GECVEWLRRY LENGKDKLER ADPPKTHVTH HPISDHEATL RCWALGFYPA EITLTWQRDG EDQTQDTELV ETRPAGDRTF QKWAAVVVPS GEEQRYTCHV QHEGLPKPLT // ID 1B34_HUMAN STANDARD; PRT; 362 AA. AC Q04826; DT 01-OCT-1993 (Rel. 27, Created) DT 01-OCT-1993 (Rel. 27, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-40 B*4002 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93127148; PubMed=1362296; RA Domena J.D., Johnston-Dow L., Parham P.; RT "The B*4002 allele encodes the B61 antigen: B40* is identical to RT B61."; RL Tissue Antigens 40:254-256(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L09736; AAA36224.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-40 B*4002 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40505 MW; 7D66503ACD865152 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B35_HUMAN STANDARD; PRT; 362 AA. AC P30477; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-40 B*4003 alpha chain DE precursor (B40-G1). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84384; AAA59634.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-40 B*4003 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40600 MW; 6AFB91FB5E2AB383 CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B36_HUMAN STANDARD; PRT; 362 AA. AC P30478; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-40 B*4004 alpha chain DE precursor (B40-G2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84383; AAA59633.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-40 B*4004 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40430 MW; F940147E8FE2759A CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFHTSVSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B38_HUMAN STANDARD; PRT; 362 AA. AC P30479; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-41 B*4101 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24035; AAA59666.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-41 B*4101 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40539 MW; 7443DC40CF7A38F5 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B39_HUMAN STANDARD; PRT; 362 AA. AC P30480; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-42 B*4201 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24034; AAA59667.1; -. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-42 B*4201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40333 MW; C9155AB015DEA1BE CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARVAEQD RAYLEGTCVE WLRRYLENGK DTLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B40_HUMAN STANDARD; PRT; 359 AA. AC P10320; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-44(B-12) B*4401 alpha chain DE precursor (B44.1) (Fragment). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86249389; PubMed=3459708; RA Kottmann A.H., Seemann G.H.A., Guessow H.D., Roos M.H.; RT "DNA sequence of the coding region of the HLA-B44 gene."; RL Immunogenetics 23:396-400(1986). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M15470; AAA59619.1; -. DR PIR; A25295; HLHUB4. DR HSSP; P30685; 1A9B. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT NON_TER 1 1 FT SIGNAL <1 21 FT CHAIN 22 359 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-44(B-12) B*4401 ALPHA CHAIN. FT DOMAIN 22 111 EXTRACELLULAR ALPHA-1. FT DOMAIN 112 203 EXTRACELLULAR ALPHA-2. FT DOMAIN 204 295 EXTRACELLULAR ALPHA-3. FT DOMAIN 296 305 CONNECTING PEPTIDE. FT TRANSMEM 306 329 FT DOMAIN 330 359 CYTOPLASMIC. FT CARBOHYD 107 107 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 122 185 BY SIMILARITY. FT DISULFID 224 280 BY SIMILARITY. SQ SEQUENCE 359 AA; 40040 MW; 82ABD981B9E5F868 CRC64; TAPRTLLLLL WGAVALTETW AGSHSMRYFY TAMSRPGRGE PRFITVGYVD DTLFVRFDSD ATSPRKEPRA PWIEQEGPEY WDRETQISKT NTQTYRENLR TAARYYNQSE AGSHIIQRMY GCDVGPDGRL LRGYDQDAYD GKDYIALNED LSSWTAADTA AQITQRKWEA ARVAEQDRAY LEGLCVESLR RYLENGKETL QRADPPKTHV THHPISDHEA TLRCWSLGFY PAEITLTWQR DGEDQTQDTE LVETRPAGDR TFQKWAAVVV PSGEEQRYTC HVQHEGLPKP LTLRWEPSSQ STVPIVGIVA GLAVLAVVVI GAVVAAVMCR RKSSGGKGGS YSQAACSDSA QGSDVSLTA // ID 1B41_HUMAN STANDARD; PRT; 362 AA. AC P30481; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-44(B-12) B*4402 alpha chain DE precursor (B44.2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24038; AAA59663.1; -. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-44(B-12) B*4402 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40481 MW; E45C71FDEFC628AD CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRTALRYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEVTLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B42_HUMAN STANDARD; PRT; 362 AA. AC P30482; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-44(B-12) B*4403 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91335451; PubMed=1871765; RA Fleischhauer K., Kernan N.A., Dupont B., Yang S.Y.; RT "The two major subtypes of HLA-B44 differ for a single amino acid in RT codon 156."; RL Tissue Antigens 37:133-137(1991). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96435470; PubMed=8838356; RA Adams E.J., Little A.M., Arnett K.L., McAuley J.E., Williams R.C., RA Parham P.; RT "Three new HLA-B alleles found in Mexican-Americans."; RL Tissue Antigens 46:414-416(1995). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X64366; CAA45718.1; -. DR EMBL; L42282; AAB51454.1; -. DR EMBL; L42283; AAB51455.1; -. DR PIR; S25415; S25415. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-44(B-12) B*4403 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40479 MW; 41D1F475EFCE2E9B CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRTALRYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEVTLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B43_HUMAN STANDARD; PRT; 362 AA. AC P30483; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-45(B-12) B*4501 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61710; CAA43879.1; -. DR PIR; S16772; S16772. DR HSSP; P30685; 1A9B. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-45(B-12) B*4501 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40414 MW; A6C843121D613695 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQD RAYLEGLCVE SLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B44_HUMAN STANDARD; PRT; 362 AA. AC P30484; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-46 B*4601 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24033; AAA59665.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-46 B*4601 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40440 MW; 481B4C6876CB0E85 CRC64; MRVTAPRTVL LLLSGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQW RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B45_HUMAN STANDARD; PRT; 362 AA. AC P30485; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-47 B*4701 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88152906; PubMed=3257938; RA Zemmour J., Ennis P.D., Parham P., Dupont B.; RT "Comparison of the structure of HLA-Bw47 to HLA-B13 and its RT relationship to 21-hydroxylase deficiency."; RL Immunogenetics 27:281-287(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M19756; AAA52664.1; -. DR HSSP; P03989; 1HSA. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-47 B*4701 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40571 MW; E3D3E4CBF8C15EAE CRC64; MRVTAPRTLL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE DLRTLLRYYN QSEAGSHTLQ RMFGCDVGPD GRLLRGYHQD AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGECVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV VCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B46_HUMAN STANDARD; PRT; 362 AA. AC P30486; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-48 B*4801 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84380; AAA59629.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-48 B*4801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40362 MW; 8FADC7B64EBD5C8D CRC64; MLVMAPRTVL LLLSAALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTLQ SMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLRSWTAA DTAAQISQRK LEAARVAEQL RAYLEGECVE WLRRYLENGK DKLERADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWTA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B47_HUMAN STANDARD; PRT; 362 AA. AC P30487; DT 01-APR-1993 (Rel. 25, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-49(B-21) B*4901 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). RN [2] RP REVISION TO 78. RX MEDLINE=93056529; PubMed=1385528; RA Hildebrand W.H., Madrigal J.A., Belich M.P., Zemmour J., Ward F.E., RA Williams R.C., Parham P.; RT "Serologic cross-reactivities poorly reflect allelic relationships in RT the HLA-B12 and HLA-B21 groups. Dominant epitopes of the alpha 2 RT helix."; RL J. Immunol. 149:3563-3568(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24037; AAA02950.1; -. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-49(B-21) B*4901 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40581 MW; 77B1C82AD3DAEB4A CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRIALRYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B48_HUMAN STANDARD; PRT; 362 AA. AC P30488; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-50(B-21) B*5001 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61706; CAA43875.1; -. DR PIR; S16773; S16773. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-50(B-21) B*5001 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 309 CONNECTING PEPTIDE. FT TRANSMEM 310 333 FT DOMAIN 334 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40541 MW; 729B0736F81C4AB4 CRC64; MRVTAPRTVL LLLSAALALT ETWAGSHSMR YFHTAMSRPG RGEPRFITVG YVDDTLFVRF DSDATSPRKE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE SLRNLRGYYN QSEAGSHTWQ RMYGCDLGPD GRLLRGYNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B49_HUMAN STANDARD; PRT; 362 AA. AC P18464; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-51(B-5) B*5101 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=89080265; PubMed=2909619; RA Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K., RA Takiguchi M.; RT "HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the RT helical region of the alpha 1 domain."; RL J. Immunol. 142:306-311(1989). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=89233295; PubMed=2714852; RA Pohla H., Kuon W., Tabaczewski P., Doerner C., Weiss E.H.; RT "Allelic variation in HLA-B and HLA-C sequences and the evolution of RT the HLA-B alleles."; RL Immunogenetics 29:297-307(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32319; AAA36232.1; -. DR EMBL; M22792; AAA59620.1; ALT_SEQ. DR EMBL; M22786; AAA59620.1; JOINED. DR EMBL; M22787; AAA59620.1; JOINED. DR EMBL; M22788; AAA59620.1; JOINED. DR EMBL; M22789; AAA59620.1; JOINED. DR EMBL; M22790; AAA59620.1; JOINED. DR EMBL; M22791; AAA59620.1; JOINED. DR EMBL; L41087; AAA64513.1; -. DR EMBL; L41086; AAA64513.1; JOINED. DR PIR; A30345; A30345. DR PIR; A30548; A30548. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-51(B-5) B*5101 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40566 MW; D104163B4CC71F92 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B52_HUMAN STANDARD; PRT; 362 AA. AC P30489; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-51(B-5) B*5104 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z15143; CAA78849.1; -. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-51(B-5) B*5104 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40560 MW; 1DF5247796583B08 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B53_HUMAN STANDARD; PRT; 362 AA. AC P30490; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-52(B-5) B*5201 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89080265; PubMed=2909619; RA Hayashi H., Ennis P.D., Ariga H., Salter R.D., Parham P., Kano K., RA Takiguchi M.; RT "HLA-B51 and HLA-Bw52 differ by only two amino acids which are in the RT helical region of the alpha 1 domain."; RL J. Immunol. 142:306-311(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M22799; AAA59645.1; ALT_SEQ. DR EMBL; M22793; AAA59645.1; JOINED. DR EMBL; M22794; AAA59645.1; JOINED. DR EMBL; M22795; AAA59645.1; JOINED. DR EMBL; M22796; AAA59645.1; JOINED. DR EMBL; M22797; AAA59645.1; JOINED. DR EMBL; M22798; AAA59645.1; JOINED. DR PIR; B30345; B30345. DR PIR; B30548; B30548. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-52(B-5) B*5201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40521 MW; A32E36370FD84F91 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRETQI SKTNTQTYRE NLRIALRYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B54_HUMAN STANDARD; PRT; 362 AA. AC P30491; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-53 B*5301 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=91033941; PubMed=1699887; RA Hayashi H., Ooba T., Nakayama S., Sekimata M., Kano K., RA Takiguchi M.; RT "Allospecificities between HLA-Bw53 and HLA-B35 are generated by RT substitution of the residues associated with HLA-Bw4/Bw6 public RT epitopes."; RL Immunogenetics 32:195-199(1990). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 25-302. RX MEDLINE=96209672; PubMed=8624812; RA Smith K.J., Reid S.W., Harlos K., McMichael A.J., Stuart D.I., RA Bell J.I., Jones E.Y.; RT "Bound water structure and polymorphic amino acids act together to RT allow the binding of different peptides to MHC class I HLA-B53."; RL Immunity 4:215-228(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58636; AAA36228.1; -. DR PIR; A45834; A45834. DR PDB; 1A1M; 08-APR-98. DR PDB; 1A1O; 08-APR-98. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal; 3D-structure. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-53 B*5301 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 FT DISULFID 227 283 SQ SEQUENCE 362 AA; 40495 MW; 57BAA748D7854658 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTYRE NLRIALRYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B55_HUMAN STANDARD; PRT; 362 AA. AC P30492; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-54(BW-22) B*5401 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77774; AAA03686.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-54(BW-22) B*5401 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40380 MW; 111730024578515D CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B56_HUMAN STANDARD; PRT; 362 AA. AC P30493; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-55(BW-22) B*5501 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77778; AAA03687.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-55(BW-22) B*5501 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40496 MW; 8F3C1F6D245257C4 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B57_HUMAN STANDARD; PRT; 362 AA. AC P30494; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-55(BW-22) B*5502 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77777; AAA03688.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-55(BW-22) B*5502 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40466 MW; 8F25C5AE2E9B8D07 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGTCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B58_HUMAN STANDARD; PRT; 362 AA. AC P30495; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-56(BW-22) B*5601 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77776; AAA03689.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-56(BW-22) B*5601 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40478 MW; D442225B8A09D667 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B59_HUMAN STANDARD; PRT; 362 AA. AC P30496; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-56(BW-22) B*5602 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92148136; PubMed=1737933; RA Hildebrand W.H., Madrigal J.A., Little A.-M., Parham P.; RT "HLA-Bw22: a family of molecules with identity to HLA-B7 in the alpha RT 1-helix."; RL J. Immunol. 148:1155-1162(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M77775; AAA03690.1; -. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-56(BW-22) B*5602 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40460 MW; 24431016FE990D01 CRC64; MRVTAPRTLL LLLWGALALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPREE PRAPWIEQEG PEYWDRNTQI YKAQAQTDRE SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGHNQL AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B60_HUMAN STANDARD; PRT; 362 AA. AC P18465; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-57(B-17) B*5701 alpha DE chain precursor (BW57.1). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90207291; PubMed=2320591; RA Ennis P.D., Zemmour J., Salter R.D., Parham P.; RT "Rapid cloning of HLA-A,B cDNA by using the polymerase chain RT reaction: frequency and nature of errors produced in amplification."; RL Proc. Natl. Acad. Sci. U.S.A. 87:2833-2837(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91067476; PubMed=2251138; RA Isamat M., Girdlestone J., Milstein C.; RT "Nucleotide sequence of an HLA-Bw57 gene."; RL Nucleic Acids Res. 18:6702-6702(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M32318; AAA36231.1; -. DR EMBL; X55711; CAA39244.1; -. DR PIR; S12622; S12622. DR PIR; D35997; D35997. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-57(B-17) B*5701 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40224 MW; C1EFCF089096AFF9 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ VMYGCDVGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B61_HUMAN STANDARD; PRT; 362 AA. AC P30497; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, B-57(B-17) B*5702 alpha chain DE precursor (BW57.2). GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61707; CAA43876.1; -. DR PIR; S16774; S16774. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT B-57(B-17) B*5702 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40342 MW; B8FAA672D2EC83FC CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRMA PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ VMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQR RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTVPIVG IVAGLAVLAV VVIGAVVAAV MCRRKSSGGK GGSYSQAACS DSAQGSDVSL TA // ID 1B62_HUMAN STANDARD; PRT; 362 AA. AC P10319; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-58(B-17) B*5801 alpha DE chain precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86008247; PubMed=2995352; RA Ways J.P., Coppin H.L., Parham P.; RT "The complete primary structure of HLA-Bw58."; RL J. Biol. Chem. 260:11924-11933(1985). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RA Inoue T., Ogawa A.; RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11799; AAA59628.1; -. DR EMBL; AB008102; BAA22916.1; -. DR PIR; A23895; HLHUB8. DR HSSP; P30491; 1A1O. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-58(B-17) B*5801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40337 MW; 2056116240BB9AC0 CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDGETRN MKASAQTYRE NLRIALRYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQS AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAARVAEQL RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1B63_HUMAN STANDARD; PRT; 362 AA. AC P30498; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, BW-78 B*7801 alpha chain DE precursor. GN HLA-B OR HLAB. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93056508; PubMed=1431115; RA Madrigal J.A., Belich M.P., Hildebrand W.H., Benjamin R.J., RA Little A.-M., Zemmour J., Ennis P.D., Ward F.E., Petzl-Erler M.L., RA Martell R.W., du Toit E.D., Parham P.; RT "Distinctive HLA-A,B antigens of black populations formed by RT interallelic conversion."; RL J. Immunol. 149:3411-3415(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=90217537; PubMed=1691230; RA Sekimata M., Hiraiwa M., Andrien M., Dupont E., Karaki S., RA Yamamoto J., Kano K., Takiguchi M.; RT "Allodeterminants and evolution of a novel HLA-B5 CREG antigen, HLA-B RT SNA."; RL J. Immunol. 144:3228-3233(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X61708; CAA43877.1; -. DR EMBL; M33573; AAA59644.1; -. DR PIR; S16775; S16775. DR HSSP; P30685; 1A9E. DR MIM; 142830; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 362 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT BW-78 B*7801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. SQ SEQUENCE 362 AA; 40478 MW; D2D6142768F28E6C CRC64; MRVTAPRTVL LLLWGAVALT ETWAGSHSMR YFYTAMSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRTE PRAPWIEQEG PEYWDRNTQI FKTNTQTDRE SLRNLRGYYN QSEAGSHTWQ TMYGCDVGPD GRLLRGHNQY AYDGKDYIAL NEDLSSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRHLENGK ETLQRADPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDRTFQKWAA VVVPSGEEQR YTCHVQHEGL PKPLTLRWEP SSQSTIPIVG IVAGLAVLAV VVIGAVVATV MCRRKSSGGK GGSYSQAASS DSAQGSDVSL TA // ID 1C01_GORGO STANDARD; PRT; 365 AA. AC P30383; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-C0101/C0102 alpha chain DE precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60252; CAA42804.1; -. DR EMBL; X60250; CAA42802.1; -. DR PIR; JH0543; JH0543. DR PIR; JH0544; JH0544. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-C0101/C0102 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40938 MW; 0DAC1859620B778F CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFFTAVAPPG RGEPRFIAVG YVDDTQFVRF DSDAANTRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRKLRGYYN QSEDGSHTFQ RMYGCDVGPD GRLQRGYDQL AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARWAERQ RAYLEGLCVE WLRRYLENGK ETLQRADPPK THVTHHPISD HEATLRCWAL GFYPAEITLT WQRDGEEQTQ DIELVETRPA GDGTFQKWAA MVVPSGEEQR YTCHVQHKGL LEPLTLRWEP SSQPTIPIVG IVAGLAVLAV VFTGTVVAAV MCRRKSSGGK GGSCSQAACS NSAQGSDESL IACKA // ID 1C01_HUMAN STANDARD; PRT; 366 AA. AC P30499; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-1 CW*0101 alpha chain DE precursor (CW1.1). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89215297; PubMed=2708822; RA Ellis S.A., Strachan T., Palmer M.S., McMichael A.J.; RT "Complete nucleotide sequence of a unique HLA class I C locus product RT expressed on the human choriocarcinoma cell line BeWo."; RL J. Immunol. 142:3281-3285(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26429; AAA59701.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-1 CW*0101 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40964 MW; 285CCFCB92788744 CRC64; MRVMEPRTLI LLLSGALALT ETWACSHSMK YFFTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YNRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMCGCDLGPD GRLLRGYDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEER RAYLEGTCVE WLRRYLENGK ESLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VMVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIASKA // ID 1C01_PANTR STANDARD; PRT; 366 AA. AC P30686; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-JUL-1993 (Rel. 26, Last annotation update) DE CHLA class I histocompatibility antigen, C alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92391104; PubMed=1381540; RA Kato T., Esumi M., Yamashita S., Abe K., Shikata T.; RT "Interferon-inducible gene expression in chimpanzee liver infected RT with hepatitis C virus."; RL Virology 190:856-860(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D11383; BAA01979.1; ALT_INIT. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 366 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT C ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 366 CYTOPLASMIC TAIL. FT DISULFID 125 192 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40842 MW; 58B25703B3D82C4D CRC64; MRVTAPRTLL LLLSGGLALT ETWAGSHSLR YFDTAVSRPG RREPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTLQ WMYGCDLGPD GRLLRGYGQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGKRVE SCRRYLENGK ETLQRTECPK THMTHHPVSD HEATLRCWAL AFYPAEITLT WQRDGEDQIQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHVQHEGL PEPLTLRWKP TSQPTIPIVG IVAGLAVLAV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LIACKA // ID 1C01_SAGOE STANDARD; PRT; 365 AA. AC P30517; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, C alpha chain precursor. OS Saguinus oedipus (Cotton-top tamarin). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Platyrrhini; Callitrichidae; Saguinus. OX NCBI_TaxID=9490; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90111120; PubMed=2104912; RA Watkins D.I., Letvin N.L., Hughes A.L., Tedder T.F.; RT "Molecular cloning of cDNA that encode MHC class I molecules from a RT New World primate (Saguinus oedipus). Natural selection acts at RT positions that may affect peptide presentation to T cells."; RL J. Immunol. 144:1136-1143(1990). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M33477; AAA36953.1; -. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 365 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT C ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 365 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 365 AA; 40829 MW; D6A0F974104BA1EE CRC64; MTIMAPRTLL LLLSGALSVT ETWAGSHSMR YFSTTVSRPG RGEPRYIEVG YVDDTQFVRF DSDAASPRME PRAPWVEQEG PEYWVLQTRN SKASAQTFRV NLQTLLGYYN QSEAGFHTIQ WMYGCDLGPD GRLLRGYHQY AYDGKDYIAL NEDLRSWTAA DAAAQITQRK WAEANAAEGM RAYLEGTCVE WLRRHLENGK EMLQRAEPPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQAQ DMELVETRPT GNGTFQKWAA VVVLSGEEHK YTCHVQHEGL PEPFTLRWEP PSQPTIPIMG IVAILAILGA VVTGAVVAAV MWRKKSSDKK GGSYSQAARS DSAQGSDVSL TACKV // ID 1C02_GORGO STANDARD; PRT; 366 AA. AC P30385; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Class I histocompatibility antigen, GOGO-C0201 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60251; CAA42803.1; -. DR PIR; JH0545; JH0545. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 366 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-C0201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40954 MW; 05E159364C769FC5 CRC64; MRVMAPRTLI LPLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQVTQRK WEAARVAEQE RAYLEGLCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C02_HUMAN STANDARD; PRT; 366 AA. AC P30500; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-1 CW*0102 alpha chain DE precursor (CW1.2). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84171; AAA59685.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-1 CW*0102 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40950 MW; D52DF8886B5FCE22 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMK YFFTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMCGCDLGPD GRLLRGYDQY AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VMVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C03_GORGO STANDARD; PRT; 366 AA. AC P30386; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-C0202 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60249; CAA42801.1; -. DR PIR; JH0546; JH0546. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 366 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-C0202 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40782 MW; 11CCAD1F6091831B CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQQ RAYLEGLCVE SLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C03_HUMAN STANDARD; PRT; 366 AA. AC P30501; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-2 CW*0201 alpha chain DE precursor (CW2.1). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89215297; PubMed=2708822; RA Ellis S.A., Strachan T., Palmer M.S., McMichael A.J.; RT "Complete nucleotide sequence of a unique HLA class I C locus product RT expressed on the human choriocarcinoma cell line BeWo."; RL J. Immunol. 142:3281-3285(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M26430; AAA59703.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-2 CW*0201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 41095 MW; AD8025DEB7DA8CE6 CRC64; MRVMEPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPS RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRGRWVEQEG PEYWDRETQK YNRQAQTDRV NLRKLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEEW RAYLEGECVE WLRRYLENGK EKLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPTEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIASKA // ID 1C04_GORGO STANDARD; PRT; 366 AA. AC P30387; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-C0203 alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60248; CAA42800.1; -. DR PIR; JH0547; JH0547. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 366 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-C0203 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40970 MW; EE962C8189CAC001 CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTSVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEDGSHTLQ SMYGCDLGPD GRLLRGYSQF AYDGKDYIAL NEDLRSWTAA DTAAQVTQRK WEAARVAEQE RAYLEGLCVE WLRRYLENGK ETLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL PEPLTLRWEP SSQPTIPIVG IVVGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C04_HUMAN STANDARD; PRT; 366 AA. AC P30502; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-2 CW*0202 alpha chain DE precursor (CW2.2). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89235215; PubMed=2715640; RA Parham P., Lawlor D.A., Lomen C.E., Ennis P.D.; RT "Diversity and diversification of HLA-A,B,C alleles."; RL J. Immunol. 142:3937-3950(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M24030; AAA59671.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-2 CW*0202 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40994 MW; 64AD7B8C2BCD5D6B CRC64; MRVMAPRTLL LLLSGALALT ETWACSHSMR YFYTAVSRPS RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV NLRKLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW RAYLEGECVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPTEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C05_HUMAN STANDARD; PRT; 366 AA. AC P04222; DT 20-MAR-1987 (Rel. 04, Created) DT 20-MAR-1987 (Rel. 04, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-3 CW*0301 alpha chain DE precursor (CW3.1). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=84207947; PubMed=6609813; RA Sodoyer R., Damotte M., Delovitch T.L., Trucy J., Jordan B.R., RA Strachan T.; RT "Complete nucleotide sequence of a gene encoding a functional human RT class I histocompatibility antigen (HLA-CW3)."; RL EMBO J. 3:879-885(1984). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X00495; CAA25190.1; -. DR PIR; A02190; HLHUW3. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-3 CW*0301 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40744 MW; BB73490AA9FA65F0 CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFCTAVSRPG RGEPHFIAVG YVDDTQFVRF DSDDESPRGE PRAPWVERKG PEYWDRETQK YKPQAQTDRV SLRNLRGYYN QSEAGSHIIQ RMYGCDVGPD GRLLRGYDQH AYDGKDYIAL NEDLRSWTAA NTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLKNGK ETLQGAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C06_HUMAN STANDARD; PRT; 366 AA. AC P30503; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-3 CW*0302 alpha chain DE precursor (CW3.2). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84172; AAA59686.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-3 CW*0302 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40784 MW; 1A169A0852B3E17E CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTAVSRPG RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHILQ RMYGCDVGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGLCVE WLRRYLKNGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C07_HUMAN STANDARD; PRT; 366 AA. AC P30504; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-4 CW*0401 alpha chain DE precursor (PL208). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=91277627; PubMed=1711567; RA Grassi F., Meneveri R., Gullberg M., Lopalco L., Rossi G.B., RA Lanza P., de Santis C., Brattsand G., Butto S., Ginelli E., RA Beretta A., Siccardi A.G.; RT "Human immunodeficiency virus type 1 gp120 mimics a hidden RT monomorphic epitope borne by class I major histocompatibility complex RT heavy chains."; RL J. Exp. Med. 174:53-62(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84386; AAA59705.1; -. DR EMBL; X58536; CAA41427.1; -. DR PIR; S21855; S21855. DR PIR; JH0526; JH0526. DR HSSP; P03989; 1HSA. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-4 CW*0401 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40995 MW; E883EB3968658DCB CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFSTSVSWPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PREPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ RMFGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWKP SSQPTIPIVG IVAGLAVLAV LAVLGAMVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C11_HUMAN STANDARD; PRT; 366 AA. AC Q29631; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-7 CW*0704 alpha chain DE precursor. GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=96086482; PubMed=7482492; RA Vilches C., Bunce M., de Pablo R., Herrero M.J., Kreisler M.; RT "Anchored PCR cloning of the novel HLA-Cw*0704 allele detected by RT PCR-SSP."; RL Tissue Antigens 46:19-23(1995). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Blood; RX MEDLINE=96232973; PubMed=8655361; RA Wang H., Tokunaga K., Ishikawa Y., Asahina A., Kuwata S., RA Akaza T., Tadokoro K., Shibata Y., Takiguchi M., Juji T.; RT "Identification and DNA typing of two Cw7 alleles (Cw*0702 and RT Cw*0704) in Japanese, with the corrected sequence of Cw*0702."; RL Hum. Immunol. 45:52-58(1996). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X83394; CAA58313.1; -. DR EMBL; D49552; BAA08500.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-7 CW*0704 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40819 MW; 4073C3BC53E55D0C CRC64; MRVMAPRALL LLLSGGLALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEDGSHTFQ RMYGCDLGPD GRLLRGYDQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK LEAARAAEQD RAYLEGTCVE WLRRYLENGK KTLQRAEPPK THVTHHPLSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGQEQR YTCHMQHEGL QEPLTLSWEP SSQPTIPIMG IVAGLAVLVV LAVLGAVVTA MMCRRKSSGG KGGSCSQAAC SNSAQGSDES LITCKA // ID 1C12_HUMAN STANDARD; PRT; 366 AA. AC P30505; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-8 CW*0801 alpha chain DE precursor (CW8.1). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84174; AAA59688.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-8 CW*0801 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40772 MW; 2A84D41389A0486A CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARTAEQL RAYLEGTCVE WLRRYLENGK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C13_HUMAN STANDARD; PRT; 366 AA. AC P30506; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-8 CW*0802 alpha chain DE precursor (CW8.2). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=93031775; PubMed=1384166; RA Zemmour J., Gumperz J.E., Hildebrand W.H., Ward F.E., Marsh S.G., RA Williams R.C., Parham P.; RT "The molecular basis for reactivity of anti-Cw1 and anti-Cw3 RT alloantisera with HLA-B46 haplotypes."; RL Tissue Antigens 39:249-257(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M84173; AAA59687.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-8 CW*0802 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40871 MW; D343B054568EA32C CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DKAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C14_HUMAN STANDARD; PRT; 366 AA. AC P30507; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-8 CW*0803 alpha chain DE precursor. GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92269955; PubMed=1317015; RA Belich M.P., Madrigal J.A., Hildebrand W.H., Zemmour J., RA Williams R.C., Luz R., Petzl-Erler M.L., Parham P.; RT "Unusual HLA-B alleles in two tribes of Brazilian Indians."; RL Nature 357:326-329(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z15144; CAA78850.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-8 CW*0803 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40872 MW; C025DFA398B14866 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVQF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYNQF AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAARTAEQL RAYLEGTCVE WLRRYLENRK KTLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWGP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C15_HUMAN STANDARD; PRT; 366 AA. AC P30508; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW*1201 alpha chain precursor DE (HLA-CX52). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=88330144; PubMed=2843461; RA Takata H., Inoko H., Ando A., Haranaka M., Watanabe B., Tsuji K., RA Iri H.; RT "Cloning and analysis of HLA class I cDNA encoding a new HLA-C RT specificity Cx52."; RL Immunogenetics 28:265-270(1988). RN [2] RP SEQUENCE FROM N.A. RA Takata H., Sonoda A., Beck S., Heyes J.M., Bodmer J.G., Inoko H.; RL Submitted (JUN-1992) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M21963; AAA59847.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW*1201 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40851 MW; E6A7DA16117A7B46 CRC64; MRVMAPRTLI LLLSGALALT ETWAGSHSMR YFYTAVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV SLRNLRGYYN QSEAGSHTLQ RMYGCDLGPD GRLLRGYDQV AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C16_HUMAN STANDARD; PRT; 366 AA. AC P30509; DT 01-APR-1993 (Rel. 25, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW*1202 alpha chain precursor DE (HLA-CB-2) (CW*0602) (CW6). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89309827; PubMed=2787363; RA Takiguchi M., Nishimura I., Hayashi H., Karaki S., Kariyone A., RA Kano K.; RT "The structure and expression of genes encoding serologically RT undetected HLA-C locus antigens."; RL J. Immunol. 143:1372-1378(1989). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=94131818; PubMed=7905471; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Molecular cloning and polymerase chain reaction-sequence-specific RT oligonucleotide detection of the allele encoding the novel RT allospecificity HLA-Cw6.2 (Cw*1502) in Spanish gypsies."; RL Hum. Immunol. 37:259-263(1993). RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=92285886; PubMed=1598685; RA Steinle A., Noessner E., Schendel D.J.; RT "Isolation and characterization of a genomic HLA-Cw6 clone."; RL Tissue Antigens 39:134-137(1992). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28172; AAA59670.1; -. DR EMBL; X70856; CAA50209.1; -. DR EMBL; X70857; CAA50210.1; -. DR EMBL; Z22752; CAA80437.1; -. DR EMBL; Z22753; CAA80437.1; JOINED. DR EMBL; Z22754; CAA80437.1; JOINED. DR PIR; S31958; S31958. DR PIR; S32757; S32757. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW*1202 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). FT CONFLICT 33 33 D -> Y (IN REF. 1). FT CONFLICT 48 48 S -> A (IN REF. 1). FT CONFLICT 101 101 N -> S (IN REF. 1). FT CONFLICT 104 104 K -> N (IN REF. 1). FT CONFLICT 114 114 D -> A (IN REF. 1). FT CONFLICT 121 121 W -> R (IN REF. 1). SQ SEQUENCE 366 AA; 40968 MW; 45876CB22256DE80 CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFDTAVSRPG RGEPRFISVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQADRV NLRKLRGYYN QSEDGSHTLQ WMYGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQW RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C17_HUMAN STANDARD; PRT; 366 AA. AC P30510; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW*1401 alpha chain precursor DE (HLA-CB-1). GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89309827; PubMed=2787363; RA Takiguchi M., Nishimura I., Hayashi H., Karaki S., Kariyone A., RA Kano K.; RT "The structure and expression of genes encoding serologically RT undetected HLA-C locus antigens."; RL J. Immunol. 143:1372-1378(1989). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M28171; AAA59669.1; -. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW*1401 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 366 AA; 40855 MW; 075264AECA0AD4FF CRC64; MRVMAPRTLI LLLSGALALT ETWACSHSMR YFSTSVSRPG RGEPRFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQK YKRQAQTDRV SLRNLRGYYN QSEAGSHTLQ WMFGCDLGPD GRLLRGYDQS AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQR RAYLEGTCVE WLRRYLENGK ESLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQWDGEDQTQ DTELVETRPA GDGTFQKWAA VMVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVVAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C18_HUMAN STANDARD; PRT; 366 AA. AC Q07000; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, CW-2 CW*1502 alpha chain DE precursor. GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=94131818; PubMed=7905471; RA Vilches C., de Pablo R., Herrero M.J., Moreno M.E., Kreisler M.; RT "Molecular cloning and polymerase chain reaction-sequence-specific RT oligonucleotide detection of the allele encoding the novel RT allospecificity HLA-Cw6.2 (Cw*1502) in Spanish gypsies."; RL Hum. Immunol. 37:259-263(1993). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X67818; CAA48029.1; -. DR PIR; S32756; S32756. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 FT CHAIN 25 366 HLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CW-2 CW*1502 ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 333 FT DOMAIN 334 366 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (POTENTIAL). SQ SEQUENCE 366 AA; 40862 MW; FDF703B7AFB05FDD CRC64; MRVMAPRTLL LLLSGALALT ETWACSHSMR YFYTAVSRPG RGEPHFIAVG YVDDTQFVRF DSDAASPRGE PRAPWVEQEG PEYWDRETQN YKRQAQTDRV NLRKLRGYYN QSEAGSHIIQ RMYGCDLGPD GRLLRGHDQL AYDGKDYIAL NEDLRSWTAA DTAAQITQRK WEAAREAEQL RAYLEGTCVE WLRRYLENGK ETLQRAEHPK THVTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPA GDGTFQKWAA VVVPSGEEQR YTCHVQHEGL PEPLTLRWEP SSQPTIPIVG IVAGLAVLAV LAVLGAVMAV VMCRRKSSGG KGGSCSQAAS SNSAQGSDES LIACKA // ID 1C28_PANTR STANDARD; PRT; 346 AA. AC P16215; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE CHLA class I histocompatibility antigen, CH28 alpha chain precursor. OS Pan troglodytes (Chimpanzee). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Pan. OX NCBI_TaxID=9598; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90201944; PubMed=1690682; RA Lawlor D.A., Warren E., Ward F.E., Parham P.; RT "Comparison of class I MHC alleles in humans and apes."; RL Immunol. Rev. 113:147-185(1990). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=88319000; PubMed=3412487; RA Lawlor D.A., Ward F.E., Ennis P.D., Jackson A.P., Parham P.; RT "HLA-A and B polymorphisms predate the divergence of humans and RT chimpanzees."; RL Nature 335:268-271(1988). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M30685; AAA87973.1; -. DR HSSP; P03989; 1HSA. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 21 FT CHAIN 22 346 CHLA CLASS I HISTOCOMPATIBILITY ANTIGEN, FT CH28 ALPHA CHAIN. FT DOMAIN 22 111 EXTRACELLULAR ALPHA-1. FT DOMAIN 112 203 EXTRACELLULAR ALPHA-2. FT DOMAIN 204 295 EXTRACELLULAR ALPHA-3. FT DOMAIN 296 305 CONNECTING PEPTIDE. FT TRANSMEM 306 329 FT DOMAIN 330 346 CYTOPLASMIC TAIL. FT DISULFID 122 185 BY SIMILARITY. FT DISULFID 224 280 BY SIMILARITY. FT CARBOHYD 107 107 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 346 AA; 39084 MW; F83E882D5C2E0971 CRC64; MAPRSLLLLF SGALALTETW AGSHSLRYFS TAVSRPGRGE PRYIAVEYVD DTQFLRFDSD AAIPRMEPRE PWVEQEGPQY WERTTGYAKA NAQTDRVALR NLLRRYNQSE AGSHTLQGMN GCDMGPDGRL LRGYHQHAYD GKDYISLNED LRSWTAADTV AQITQRFYEA EEYAEEFRTY LEGECLELLR RYLENGKETL QRADPPKAHI AHHPISDHEA TLRCWALGFY PAEITLTWQR DGEEQTQDTE LVETRPAGDG NFQKWAAVVV PSGEEQRYTC HVQHEGLPQP LTLRWEQSPQ PTIPIVGIVA GLVVLGAVVT GAVVAAVMWR KKSSDRNRGS YSQAAV // ID 1CPX_DIRIM STANDARD; PRT; 235 AA. AC O17433; DT 16-OCT-2001 (Rel. 40, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 1-Cys peroxidoxin (EC 1.11.1.7) (1-CysPxn). OS Dirofilaria immitis. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Spirurida; Filarioidea; OC Onchocercidae; Dirofilaria. OX NCBI_TaxID=6287; RN [1] RP SEQUENCE FROM N.A. RA McGonigle S., James E.R.; RT "1-Cys peroxidoxin from Dirofilaria immitis."; RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THIOL SPECIFIC ANTIOXIDANT. CC -!- CATALYTIC ACTIVITY: DONOR + H(2)O(2) = OXIDIZED DONOR + 2 H(2)O. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- PTM: CYS-49 IS THE SITE OF OXIDATION BY H(2)O(2). THE OXIDIZED CC INTERMEDIATE MIGHT BE CYS-SOH (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE AHPC/TSA FAMILY. REHYDRIN SUBFAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF027387; AAB83998.1; -. DR HSSP; P30041; 1PRX. DR InterPro; IPR000866; AhpC-TSA. DR Pfam; PF00578; AhpC-TSA; 1. KW Oxidoreductase; Peroxidase; Antioxidant. FT ACT_SITE 49 49 BY SIMILARITY. SQ SEQUENCE 235 AA; 26342 MW; BCC198C87D88FD97 CRC64; MTKGILLGDK FPDFRAETNE GFIPSFYDWI GKDSWAILFS HPRDFTPVCT TELARLVQLA PEFNKRNVKL IGLSCDSAES HRKWVDDIMA VCKMKCNDGD TCCSGNKLPF PIIADENRFL ATELGMMDPD ERDENGNALT ARCVFIIGPE KTLKLSILYP ATTGRNFDEI LRVVDSLQLT AVKLVATPVD WKDGDDCVVL PTIDDTEAKK LFGEKINTIE LPSGKHYLRM VAHPK // ID 1CXX_HUMAN STANDARD; PRT; 342 AA. AC P10321; DT 01-MAR-1989 (Rel. 10, Created) DT 01-MAR-1989 (Rel. 10, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE HLA class I histocompatibility antigen, C-4 alpha chain. GN HLA-C OR HLAC. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=86033791; PubMed=3863816; RA Davidson W.F., Kress M., Khoury G., Jay G.; RT "Comparison of HLA class I gene sequences. Derivation of RT locus-specific oligonucleotide probes specific for HLA-A, HLA-B, and RT HLA-C genes."; RL J. Biol. Chem. 260:13414-13423(1985). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M11886; AAA52665.1; -. DR PIR; A24512; HLHUC4. DR HSSP; P30685; 1A9B. DR MIM; 142840; -. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; FALSE_NEG. KW MHC I; Transmembrane; Glycoprotein. FT DOMAIN 25 90 EXTRACELLULAR ALPHA-1. FT DOMAIN 91 182 EXTRACELLULAR ALPHA-2. FT DOMAIN 183 274 EXTRACELLULAR ALPHA-3. FT DOMAIN 275 284 CONNECTING PEPTIDE. FT TRANSMEM 285 309 FT DOMAIN 310 342 CYTOPLASMIC TAIL. FT CARBOHYD 86 86 N-LINKED (GLCNAC...) (BY SIMILARITY). FT DISULFID 164 203 BY SIMILARITY. SQ SEQUENCE 342 AA; 38082 MW; 22C39A6D84C05D09 CRC64; CSHSMRYFDT AVSRPGAGEP RFISVGYVDD TQFVRFDSDA ASPRGEPRAP WVEQEGPEYW DRETQKYKRQ AQADRVSLRN LRGYYNQSED GSHTLQRMSG CDLGPDGRLL RGYDQSAYDG KDYIALNEDL RSWTAADTAA QITQRKWEAA RAAEQLRAYL EGLCVEWLRR YLENGKETLQ RAEPPKTHVT HHPLSDHEAT LRCWALGFYP AEITLTWQRD GEDQTQDTEL VETRPAGDGT FQKWAAVVVP SGQEQRYTCH MQHEGLQEPL TLSWEPSSQP TIPIMGIVAG LAVLVVLAVL GAVVTAMMCR RKSSGGKGGS CSQAACSNSA QGSDESLITC KA // ID 1OKO_GORGO STANDARD; PRT; 362 AA. AC P30388; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 01-APR-1993 (Rel. 25, Last annotation update) DE Class I histocompatibility antigen, GOGO-OKO alpha chain precursor. OS Gorilla gorilla gorilla (Lowland gorilla). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Gorilla. OX NCBI_TaxID=9595; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92078860; PubMed=1744581; RA Lawlor D.A., Warren E., Taylor P., Parham P.; RT "Gorilla class I major histocompatibility complex alleles: comparison RT to human and chimpanzee class I."; RL J. Exp. Med. 174:1491-1509(1991). CC -!- FUNCTION: INVOLVED IN THE PRESENTATION OF FOREIGN ANTIGENS TO CC THE IMMUNE SYSTEM. CC -!- SUBUNIT: DIMER OF ALPHA CHAIN AND A BETA CHAIN (BETA-2- CC MICROGLOBULIN). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X60692; CAA43100.1; -. DR PIR; JH0538; JH0538. DR HSSP; P30685; 1A9B. DR InterPro; IPR003006; Ig_MHC. DR InterPro; IPR003597; Ig_c1. DR InterPro; IPR001039; MHC_I. DR Pfam; PF00047; ig; 1. DR Pfam; PF00129; MHC_I; 1. DR ProDom; PD000050; MHC_I; 1. DR SMART; SM00407; IGc1; 1. DR PROSITE; PS00290; IG_MHC; 1. KW MHC I; Transmembrane; Glycoprotein; Signal. FT SIGNAL 1 24 BY SIMILARITY. FT CHAIN 25 362 CLASS I HISTOCOMPATIBILITY ANTIGEN, FT GOGO-OKO ALPHA CHAIN. FT DOMAIN 25 114 EXTRACELLULAR ALPHA-1. FT DOMAIN 115 206 EXTRACELLULAR ALPHA-2. FT DOMAIN 207 298 EXTRACELLULAR ALPHA-3. FT DOMAIN 299 308 CONNECTING PEPTIDE. FT TRANSMEM 309 332 FT DOMAIN 333 362 CYTOPLASMIC TAIL. FT DISULFID 125 188 BY SIMILARITY. FT DISULFID 227 283 BY SIMILARITY. FT CARBOHYD 110 110 N-LINKED (GLCNAC...) (BY SIMILARITY). SQ SEQUENCE 362 AA; 40755 MW; BFE4D9A72C55649D CRC64; MAVVAPRTLL LLLSGTLALT RTWAGSHSMR YFYTTMSRPG RGEPRFISVG YVDDTQFVRF DSDDASPREE PRAPWMEREG PEYWDRNTQI YKAQAQTDRV DLETLRGYYN QSEGGSHTIQ RMYGCEVGPD GRFLRGYLQD AYDGKDYITL NEDLRSWTAA DMAAQITQRK WEAAREAERL RAYMEGTCVE WLRRHLENGK ETLQRTDPPK THMTHHPVSD HEATLRCWAL GFYPAEITLT WQRDGEDQTQ DTELVETRPG GDGTFQKWAA VVVPSGKEQR YTCHVQHEGL PKPLTLRWEP SSQPTIPIVG IIAGLVLLGA VITGAVVAAM MWRKKSSGRK GGSYSQAASS DSAQGSDVSL TA // ID 219_HUMAN STANDARD; PRT; 230 AA. AC P98173; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 2-19 protein precursor. GN 2-19 OR 2.19. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Fetal brain; RX MEDLINE=94068527; PubMed=8248200; RA Bione S., Tamanini F., Maestrini E., Tribioli C., Poustka A., RA Torri G., Rivella S., Toniolo D.; RT "Transcriptional organization of a 450-kb region of the human X RT chromosome in Xq28."; RL Proc. Natl. Acad. Sci. U.S.A. 90:10977-10981(1993). RN [2] RP SEQUENCE FROM N.A. RA Zollo M., Mazzarella R., Bione S., Toniolo D., Schlessinger D., RA D'Urso M., Chen E.Y.; RL Submitted (MAY-1991) to the EMBL/GenBank/DDBJ databases. RN [3] RP SEQUENCE FROM N.A. RX MEDLINE=96311563; PubMed=8733135; RA Chen E.Y., Zollo M., Mazzarella R.A., Ciccodicola A., Chen C.-N., RA Zuo L., Heiner C., Burough F.W., Ripetto M., Schlessinger D., RA D'Urso M.; RT "Long-range sequence analysis in Xq28: thirteen known and six RT candidate genes in 219.4 kb of high GC DNA between the RCP/GCP and RT G6PD loci."; RL Hum. Mol. Genet. 5:659-668(1996). CC -!- TISSUE SPECIFICITY: IN SIMILAR AMOUNTS IN TESTIS, PANCREAS, CC ADRENAL, PLACENTA, BRAIN, FETAL BRAIN, LIVER, KIDNEY, SKELETAL CC MUSCLE, HEART. CC -!- SIMILARITY: BELONGS TO THE 2-19 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X55448; CAA39090.1; -. DR EMBL; X87193; CAA60645.1; -. DR EMBL; L44140; AAA92652.1; -. KW Signal; Polymorphism. FT SIGNAL 1 33 POTENTIAL. FT CHAIN 34 230 2-19 PROTEIN. FT VARIANT 213 213 C -> W (IN DBSNP:1050788). FT /FTId=VAR_011923. SQ SEQUENCE 230 AA; 25069 MW; FE3934D91F98CAAD CRC64; MRLAGPLRIV VLVVSVGVTW IVVSILLGGP GSGFPRIQQL FTSPESSVTA APRARKYKCG LPQPCPEEHL AFRVVSGAAN VIGPKICLED KMLMSSVKDN VGRGLNIALV NGVSGELIEA RAFDMWAGDV NDLLKFIRPL HEGTLVFVAS YDDPATKMNE ETRKLFSELG SRNAKELAFR DSWVFVGAKG VQNKSPFEQH VKNSKHSNKY EGCPEALEME GCIPRRSTAS // ID 21KD_DAUCA STANDARD; PRT; 193 AA. AC P17407; DT 01-AUG-1990 (Rel. 15, Created) DT 01-AUG-1990 (Rel. 15, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 21 kDa protein precursor (1.2 protein). OS Daucus carota (Carrot). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Asteridae; euasterids II; Apiales; Apiaceae; Daucus. OX NCBI_TaxID=4039; RN [1] RP SEQUENCE FROM N.A. RA Aleith F.; RL Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X52395; CAA36642.1; -. DR PIR; S10911; S10911. KW Signal. FT SIGNAL 1 22 POTENTIAL. FT CHAIN 23 193 21 KDA PROTEIN. SQ SEQUENCE 193 AA; 21041 MW; 75940F09ACAB9796 CRC64; MKLSKSTLVF SALLVILAAA SAAPANQFIK TSCTLTTYPA VCEQSLSAYA KTIQNNPQEL ASTALQVSLT RTQQAQTFMK RLNKFKGLKA RQYAAIHDCL EEVEDSLDRV SRSCDEMKNL SHAKGNDFTF RMSNVETWVS AALTDETTCM DGFAGKGMDG KIKESVRAQV VAVARVTSNA LALVNNFAAK HKH // ID 21KD_ZYMMO STANDARD; PRT; 184 AA. AC P15256; DT 01-APR-1990 (Rel. 14, Created) DT 01-APR-1990 (Rel. 14, Last sequence update) DT 15-DEC-1998 (Rel. 37, Last annotation update) DE 20.9 kDa protein (ORF 2). OS Zymomonas mobilis. OG Plasmid pZM2. OC Bacteria; Proteobacteria; alpha subdivision; Sphingomonadaceae; OC Zymomonas. OX NCBI_TaxID=542; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=ATCC 10988 / ZM1; RA Misawa N., Nakamura K.; RT "The nucleotide sequence of the 2.7 kilobase pair plasmid of Zymomonas RT mobilis ATCC 10988."; RL J. Biotechnol. 12:63-70(1989). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X14438; CAA32610.1; -. DR PIR; S06695; S06695. KW Plasmid. SQ SEQUENCE 184 AA; 20962 MW; 83D50576B6F2802B CRC64; MATKLRKQPI RYDENPFIEG MVVPVKSQRV QLSRLGRDDN ILVNQATGEM QGTHVTTYRR VDSEEFVKLF STNIALTFEL GAAGIKAFSV LVWILQDKGI SKDLVPLDKF VLEDFLNAQE KKLALSQATF ARGLAELEKA KIIAKHVRQG WYFINPNFVF NGDRVAFTTV IERKKTLQKQ DESE // ID 22A3_MOUSE STANDARD; PRT; 154 AA. AC P70122; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE Protein 22A3 (Fragment). GN 22A3. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BALB/C; TISSUE=Cochlea; RA Crozet F.; RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: BELONGS TO THE UPF0023 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X99668; CAA67982.1; -. DR InterPro; IPR002140; UPF0023. DR Pfam; PF01172; UPF0023; 1. DR ProDom; PD009796; UPF0023; 1. DR PROSITE; PS01267; UPF0023; 1. FT NON_TER 1 1 FT NON_TER 154 154 SQ SEQUENCE 154 AA; 17453 MW; 4EA8EC0B59A000B8 CRC64; RACGSFFPGR FRKSRALLGS YGFARRRVVS AEHLASPRAR DLRTATMSIF TPTNQIRLTN VAVVRMKRGG KRFEIACYKN KVVGWRSGVE KDLDEVLQTH TVFGNVSKGQ GCQRREDLIN AFGERRTRLK ILQSRILGLK GVKFQVVKIK GTRN // ID 22P1_RAT STANDARD; PRT; 176 AA. AC P22282; Q63674; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Cystatin related protein 1 precursor (CRP-1) (Prostatic 22 kDa DE glycoprotein P22K16/P22K20) (Androgen regulated 20 kDa protein). GN CRP1. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Prostate; RX MEDLINE=91125374; PubMed=2280780; RA Winderickx J., Hemschoote K., de Clercq N., van Dijck P., RA Peeters B., Rombauts W., Verhoeven G., Heyns W.; RT "Tissue-specific expression and androgen regulation of different RT genes encoding rat prostatic 22-kilodalton glycoproteins homologous RT to human and rat cystatin."; RL Mol. Endocrinol. 4:657-667(1990). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 32-81. RX MEDLINE=90001187; PubMed=2477055; RA Ho K.-C., Snoek R., Quarmby V., Viskochil D.H., Rennie P.S., RA Wilson E.M., French F.S., Bruchovsky N.; RT "Primary structure and androgen regulation of a 20-kilodalton protein RT specific to rat ventral prostate."; RL Biochemistry 28:6367-6373(1989). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RT "An effect of androgens on the length of the poly(A)-tail and RT alternative splicing cause size heterogeneity of the messenger RT ribonucleic acids encoding cystatin-related protein."; RL Endocrinology 131:2496-2502(1992). RN [4] RP ERRATUM. RX MEDLINE=93178358; PubMed=7679983; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RL Endocrinology 132:2496-2502(1993). RN [5] RP SEQUENCE FROM N.A. RX MEDLINE=93216117; PubMed=8462870; RA Devos A., de Clercq N., Vercaeren I., Heyns W., Rombauts W., RA Peeters B.; RT "Structure of rat genes encoding androgen-regulated cystatin-related RT proteins (CRPs): a new member of the cystatin superfamily."; RL Gene 125:159-167(1993). RN [6] RP SEQUENCE FROM N.A. RX MEDLINE=94086539; PubMed=8262963; RA Ho K.-C., Marschke K.B., Tan J.A., Power S.G.A., Wilson E.M., RA French F.S.; RT "A complex response element in intron 1 of the androgen-regulated RT 20-kDa protein gene displays cell type-dependent androgen receptor RT specificity."; RL J. Biol. Chem. 268:27226-27235(1993). CC -!- TISSUE SPECIFICITY: PROSTATE AND LACRIMAL GLAND. CC -!- INDUCTION: BY ANDROGENS. CC -!- SIMILARITY: TO THE C-TERMINAL OF TYPE 2 CYSTATIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58167; AAA63498.1; -. DR EMBL; Z13993; CAA78384.1; -. DR EMBL; S48988; AAA12401.1; -. DR EMBL; S57980; AAB26027.1; -. DR EMBL; L12454; AAA40732.1; -. DR EMBL; M27901; AAA42345.1; -. DR PIR; JT0615; JT0615. DR PIR; A32819; A32819. DR InterPro; IPR000010; Cystatin. DR SMART; SM00043; CY; 1. KW Thiol protease inhibitor; Glycoprotein; Signal; Multigene family. FT SIGNAL 1 26 POTENTIAL. FT PROPEP 27 31 POTENTIAL. FT CHAIN 32 176 CYSTATIN RELATED PROTEIN 1. FT DISULFID 129 139 BY SIMILARITY. FT DISULFID 153 173 BY SIMILARITY. FT CARBOHYD 71 71 N-LINKED (GLCNAC...). FT SIMILAR 125 176 TO TYPE 2 CYSTATINS C-TERMINAL. FT CONFLICT 1 22 MISSING (IN REF. 2). FT CONFLICT 23 24 HA -> MQ (IN REF. 2). FT CONFLICT 157 157 V -> L (IN REF. 2, 3 AND 6). SQ SEQUENCE 176 AA; 21060 MW; 3D5355EC56E3CBA0 CRC64; MCKTLHGTLL LLAIFVLFLN FSHATAKRTR RGMEIFEKNF IDKNKLKDVY DVFKYLYNTH SADTYLSNIK NESFTMNIWG FGEIEMVKTK CRKIDSDFYK CSFQREFYNL KRTPGETMYY ISLPGSVRCR KLLSKLDNCP FEEQTEQLKR EICYFVVYPD YIEQNIHAVR FDCYTK // ID 22P2_RAT STANDARD; PRT; 176 AA. AC P22283; DT 01-AUG-1991 (Rel. 19, Created) DT 01-AUG-1991 (Rel. 19, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Cystatin related protein 2 precursor (Prostatic 22 kDa glycoprotein DE P22K15). GN CRP2. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; TISSUE=Prostate; RX MEDLINE=91125374; PubMed=2280780; RA Winderickx J., Hemschoote K., de Clercq N., van Dijck P., RA Peeters B., Rombauts W., Verhoeven G., Heyns W.; RT "Tissue-specific expression and androgen regulation of different RT genes encoding rat prostatic 22-kilodalton glycoproteins homologous RT to human and rat cystatin."; RL Mol. Endocrinol. 4:657-667(1990). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=WISTAR; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RT "An effect of androgens on the length of the poly(A)-tail and RT alternative splicing cause size heterogeneity of the messenger RT ribonucleic acids encoding cystatin-related protein."; RL Endocrinology 131:2496-2502(1992). RN [3] RP ERRATUM. RX MEDLINE=93178358; PubMed=7679983; RA Vercaeren I., Winderickx J., Devos A., Peeters B., Heyns W.; RL Endocrinology 132:2496-2502(1993). RN [4] RP SEQUENCE FROM N.A. RX MEDLINE=93216117; PubMed=8462870; RA Devos A., de Clercq N., Vercaeren I., Heyns W., Rombauts W., RA Peeters B.; RT "Structure of rat genes encoding androgen-regulated cystatin-related RT proteins (CRPs): a new member of the cystatin superfamily."; RL Gene 125:159-167(1993). CC -!- TISSUE SPECIFICITY: PROSTATE. CC -!- INDUCTION: BY ANDROGENS. CC -!- SIMILARITY: TO THE C-TERMINAL OF TYPE 2 CYSTATIN FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M58169; AAA63499.1; -. DR EMBL; Z13994; CAA78385.1; -. DR PIR; JT0616; JT0616. DR InterPro; IPR000010; Cystatin. DR SMART; SM00043; CY; 1. KW Thiol protease inhibitor; Glycoprotein; Signal; Multigene family. FT SIGNAL 1 26 POTENTIAL. FT PROPEP 27 30 POTENTIAL. FT CHAIN 31 176 CYSTATIN RELATED PROTEIN 2. FT DISULFID 129 139 BY SIMILARITY. FT DISULFID 153 173 BY SIMILARITY. FT CARBOHYD 71 71 N-LINKED (GLCNAC...) (PROBABLE). FT SIMILAR 125 176 TO TYPE 2 CYSTATINS C-TERMINAL. FT CONFLICT 149 176 KREICYFQLYPDYIEQNIRSVRFNCYTK -> FT IERNMLLSTVS (IN REF. 2). SQ SEQUENCE 176 AA; 21013 MW; 1B8F4FAEBA06B461 CRC64; MYKTLCGTQL LLAIFVLFLN FSHATAKGTR GPMEIFKKNF MEKNKLNDVY DIFKFLYNKF SHDTYLSNIK NQSFTMNTWG FGEIEVVKTK CRKIDSDFYK CSFQWEFCNI KRTPGVTIYY ITLPGSVRCR KLLSKLVNCP FEEQTEQLKR EICYFQLYPD YIEQNIRSVR FNCYTK // ID 239A_HUMAN STANDARD; PRT; 302 AA. AC O15442; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Adult brain protein 239 (239AB). GN C22ORF1. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Brain; RX MEDLINE=97409957; PubMed=9266672; RA Schwartz F., Ota T.; RT "The 239AB gene on chromosome 22: a novel member of an ancient gene RT family."; RL Gene 194:57-62(1997). CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN ADULT BRAIN. CC -!- SIMILARITY: BELONGS TO THE UPF0046 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U84894; AAC51673.2; -. DR MIM; 602112; -. DR InterPro; IPR000934; Ser_thr_phosphtse. SQ SEQUENCE 302 AA; 34581 MW; FB7B2B423B691417 CRC64; MAFSQSHVMA ARRHQHSRLI IEVDEYSSNP TQAFTFYNIN QGRFQPPHVQ MVDPVPHDAP KPPGYTRFVC VSDTHSRTDP IQMPYGDVLI HAGDFTELGL PSEVKKFNEW LGSLPYEYKI VIAGNHELTF DQEFMADLIK QDFYYFPSVS KLKPENYENV QSLLTNCIYL QDSEVTVRGF RIYGSPWQPW FYGWGFNLPR GQALLEKWNL IPEGVDILIT HGPPLGFLDW VPKKMQRVGC VELLNTVQRR VQPRLHVFGH IHEGYGVMAD GTTTYVNASV CTVNYQPVNP PIVIDLPTPR NS // ID 239F_HUMAN STANDARD; PRT; 294 AA. AC Q15777; DT 15-JUL-1998 (Rel. 36, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Fetal brain protein 239 (239FB). GN C11ORF8. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=95080775; PubMed=7527372; RA Schwartz F., Neve R., Eisenman R., Gessler M., Bruns G.; RT "A WAGR region gene between PAX-6 and FSHB expressed in fetal brain."; RL Hum. Genet. 94:658-664(1994). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=96115606; PubMed=8666403; RA Schwartz F., Eisenman R., Knoll J., Gessler M., Bruns G.; RT "cDNA sequence, genomic organization, and evolutionary conservation RT of a novel gene from the WAGR region."; RL Genomics 29:526-532(1995). CC -!- TISSUE SPECIFICITY: EXPRESSED PREDOMINANTLY IN FETAL BRAIN. CC -!- SIMILARITY: BELONGS TO THE UPF0046 FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U57911; AAC50564.1; -. DR MIM; 600911; -. DR InterPro; IPR000934; Ser_thr_phosphtse. SQ SEQUENCE 294 AA; 33360 MW; 43B2BC0DA1BFD1F0 CRC64; MAHGIPSQGK VTITVDEYSS NPTQAFTHYN INQSRFQPPH VHMVDPIPYD TPKPAGHTRF VCISDTHSRT DGIQMPYGDI LLHTGDFTEL GLPSEVKKFN DWLGNLPYEY KIVIAGNHEL TFDKEFMADL VKQDYYRFPS VSKLKPEDFD NVQSLLTNSI YLQDSEVTVK GFRIYGAPWT PWFNGWGFNL PRGQSLLDKW NLIPEGIDIL MTHGPPLGFR DWVPKELQRV GCVELLNTVQ RRVRPKLHVF GGIHEGYGIM TDGYTTYINA STCTVSFQPT NPPIIFDLPN PQGS // ID 23KD_BACST STANDARD; PRT; 22 AA. AC P80166; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 01-FEB-1994 (Rel. 28, Last annotation update) DE 23 kDa basic protein (Fragment). OS Bacillus stearothermophilus. OC Bacteria; Firmicutes; Bacillus/Clostridium group; OC Bacillus/Staphylococcus group; Geobacillus. OX NCBI_TaxID=1422; RN [1] RP SEQUENCE. RA Vorgias C.E.; RL Submitted (OCT-1992) to the SWISS-PROT data bank. FT NON_TER 22 22 SQ SEQUENCE 22 AA; 2376 MW; 96C604E42CE0BFFC CRC64; XKESSFDIVS KVDLSEVANA IN // ID 24KD_PLACH STANDARD; PRT; 37 AA. AC P14592; DT 01-JAN-1990 (Rel. 13, Created) DT 01-JAN-1990 (Rel. 13, Last sequence update) DT 01-MAY-1991 (Rel. 18, Last annotation update) DE 24 kDa antigen (Fragment). OS Plasmodium chabaudi. OC Eukaryota; Alveolata; Apicomplexa; Haemosporida; Plasmodium. OX NCBI_TaxID=5825; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=87174746; PubMed=3550696; RA Langsley G., Sibilli L., Mattei D., Falanga P., Mercereau-Puijalon O.; RT "Karyotype comparison between P. chabaudi and P. falciparum: analysis RT of a P. chabaudi cDNA containing sequences highly repetitive in P. RT falciparum."; RL Nucleic Acids Res. 15:2203-2211(1987). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X04892; CAA28580.1; -. KW Malaria. FT NON_TER 1 1 SQ SEQUENCE 37 AA; 4757 MW; E6F0EB6A45CFEBD5 CRC64; NYCYYMVDYL TFYNIKNYKI YTYAQRLLEI YFSYLSI // ID 25KD_SARPE STANDARD; PRT; 258 AA. AC P23170; DT 01-NOV-1991 (Rel. 20, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Development-specific 25 kDa protein. OS Sarcophaga peregrina (Flesh fly) (Boettcherisca peregrina). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Oestroidea; Sarcophagidae; Sarcophaga. OX NCBI_TaxID=7386; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=85289142; PubMed=2993269; RA Matsumoto N., Sekimizu K., Soma G.I., Ohmura Y., Andoh T., RA Nakanishi Y., Obinata M., Natori S.; RT "Structural analysis of a developmentally regulated 25-kDa protein RT gene of Sarcophaga peregrina."; RL J. Biochem. 97:1501-1508(1985). RN [2] RP REVISIONS. RX MEDLINE=96235235; PubMed=8647115; RA Horio T., Kubo T., Natori S.; RT "Purification and cDNA cloning of the alcohol dehydrogenase of the RT flesh fly Sarcophaga peregrina. A structural relationship between RT alcohol dehydrogenase and a 25-kDa protein."; RL Eur. J. Biochem. 237:698-703(1996). CC -!- DEVELOPMENTAL STAGE: EXPRESSED IN THE FAT BODY OF MIDDLE THIRD- CC INSTAR LARVAE. CC -!- SIMILARITY: BELONGS TO THE SHORT-CHAIN DEHYDROGENASES/REDUCTASES CC (SDR) FAMILY. STRONG, TO DROSOPHILA P6 (FBP2). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X02570; CAA26412.1; -. DR PIR; A24181; A24181. DR HSSP; P10807; 1B16. DR InterPro; IPR002198; ADH_short. DR Pfam; PF00106; adh_short; 1. DR PRINTS; PR00080; SDRFAMILY. DR PROSITE; PS00061; ADH_SHORT; 1. KW Oxidoreductase. FT NP_BIND 10 34 NAD OR NADP (BY SIMILARITY). FT ACT_SITE 151 151 BY SIMILARITY. SQ SEQUENCE 258 AA; 28633 MW; 651CB188A5D1547A CRC64; MMDWNNKNVV YVGGFSGFGY QVCQMMMKKP MKHLIVCSRM ENVEMLKKLQ AINTSVKVMF VQMNIADYAS IVKGVKQVIG HVGHVDVLIN GVGGLADKDV ETTVAVNLTG LINTTLMFMP YMDKTQSGHG GMVVSISSVY GLEPGPAFSV YSAAKHGGIG FTRSMADEHL YHKTGVAFMC ICPAMTSTEL MMNKRDMNWM KWVPHSEEMW KMVMDAKMQT PEECAVNMMT AMEQAKNGAI YICSTSGMKE ITPTVYMH // ID 28KD_MYCLE STANDARD; PRT; 236 AA. AC P19361; DT 01-NOV-1990 (Rel. 16, Created) DT 01-NOV-1990 (Rel. 16, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE 28 kDa antigen precursor. GN ML0091. OS Mycobacterium leprae. OC Bacteria; Firmicutes; Actinobacteria; Actinobacteridae; OC Actinomycetales; Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1769; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89067516; PubMed=3058804; RA Cherayil B.J., Young R.A.; RT "A 28-kDa protein from Mycobacterium leprae is a target of the human RT antibody response in lepromatous leprosy."; RL J. Immunol. 141:4370-4375(1988). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=TN; RX MEDLINE=21128732; PubMed=11234002; RA Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R., RA Wheeler P.R., Honore N., Garnier T., Churcher C., Harris D., RA Mungall K., Basham D., Brown D., Chillingworth T., Connor R., RA Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N., RA Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S., RA Murphy L., Oliver K., Quail M.A., Rajandream M.-A., Rutherford K.M., RA Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R., RA Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R., RA Barrell B.G.; RT "Massive gene decay in the leprosy bacillus."; RL Nature 409:1007-1011(2001). CC -!- SIMILARITY: TO M.TUBERCULOSIS ERP. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M23232; AAA25345.1; -. DR EMBL; AL583917; CAC29599.1; -. DR PIR; A30557; A30557. DR Leproma; ML0091; -. KW Antigen; Signal; Complete proteome. FT SIGNAL 1 22 FT CHAIN 23 236 28 KDA ANTIGEN. SQ SEQUENCE 236 AA; 23784 MW; 5A9760D06ADACDFB CRC64; MPNRRRCKLS TAISTVATLA IASPCAYFLV YEPTASAKPA AKHYEFKQAA SIADLPGEVL DAISQGLSQF GINLPPVPSL TGTDDPGNGL RTPGLTSPDL TNQELGTPVL TAPGTGLTPP VTGSPICTAP DLNLGGTCPS EVPITTPISL DPGTDGTYPI LGDPSTLGGT SPISTSSGEL VNDLLKVANQ LGASQVMDLI KGVVMPAVMQ GVQNGNVAGD LSGSVTPAAI SLIPVT // ID 28KD_TRIFO STANDARD; PRT; 29 AA. AC P33405; DT 01-FEB-1994 (Rel. 28, Created) DT 01-FEB-1994 (Rel. 28, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE 28 kDa protein (Fragment). OS Tritrichomonas foetus (Trichomonas foetus). OC Eukaryota; Parabasalidea; Trichomonadida; Tritrichomonas. OX NCBI_TaxID=5724; RN [1] RP SEQUENCE. RX MEDLINE=93307628; PubMed=8319888; RA Irvine J.W., Coombs G.H., North M.J.; RT "Purification of cysteine proteinases from trichomonads using RT bacitracin-Sepharose."; RL FEMS Microbiol. Lett. 110:113-120(1993). CC -!- MISCELLANEOUS: BINDS TO BACITRACIN. FT UNSURE 12 12 OR Y. FT UNSURE 13 13 OR W. FT NON_TER 29 29 SQ SEQUENCE 29 AA; 3279 MW; 155FEDA75B7496E0 CRC64; ARYAILFAGS NVVYNAXXQA DIYTIYTFL // ID 2A5A_HUMAN STANDARD; PRT; 486 AA. AC Q15172; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE alpha isoform (PP2A, B subunit, B' alpha isoform) (PP2A, B subunit, DE B56 alpha isoform) (PP2A, B subunit, PR61 alpha isoform) (PP2A, B DE subunit, R5 alpha isoform). GN PPP2R5A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Breast cancer; RX MEDLINE=96064678; PubMed=7592815; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [2] RP SEQUENCE OF 47-56; 129-132; 347-354; 448-462 AND 471-480. RC TISSUE=Brain; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED WITH THE HIGHEST EXPRESSION CC IN HEART AND SKELETAL MUSCLE. CC -!- PTM: PHOSPHORYLATED ON SERINE RESIDUES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42373; AAC37601.1; -. DR MIM; 601643; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Phosphorylation; Multigene family. FT DOMAIN 2 5 POLY-SER. FT CONFLICT 52 52 E -> F (IN REF. 2; AA SEQUENCE). FT CONFLICT 54 54 H -> S (IN REF. 2; AA SEQUENCE). FT CONFLICT 451 451 R -> E (IN REF. 2; AA SEQUENCE). SQ SEQUENCE 486 AA; 56193 MW; D31407F7032A6D44 CRC64; MSSSSPPAGA ASAAISASEK VDGFTRKSVR KAQRQKRSQG SSQFRSQGSQ AELHPLPQLK DATSNEQQEL FCQKLQQCCI LFDFMDSVSD LKSKEIKRAT LNELVEYVST NRGVIVESAY SDIVKMISAN IFRTLPPSDN PDFDPEEDEP TLEASWPHIQ LVYEFFLRFL ESPDFQPSIA KRYIDQKFVQ QLLELFDSED PRERDFLKTV LHRIYGKFLG LRAFIRKQIN NIFLRFIYET EHFNGVAELL EILGSIINGF ALPLKAEHKQ FLMKVLIPMH TAKGLALFHA QLAYCVVQFL EKDTTLTEPV IRGLLKFWPK TCSQKEVMFL GEIEEILDVI EPTQFKKIEE PLFKQISKCV SSSHFQVAER ALYFWNNEYI LSLIEENIDK ILPIMFASLY KISKEHWNPT IVALVYNVLK TLMEMNGKLF DDLTSSYKAE RQREKKKELE REELWKKLEE LKLKKALEKQ NSAYNMHSIL SNTSAE // ID 2A5B_HUMAN STANDARD; PRT; 497 AA. AC Q15173; Q13853; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE beta isoform (PP2A, B subunit, B' beta isoform) (PP2A, B subunit, DE B56 beta isoform) (PP2A, B subunit, PR61 beta isoform) (PP2A, B DE subunit, R5 beta isoform). GN PPP2R5B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM BETA-1). RC TISSUE=Fetal brain; RX MEDLINE=96064678; PubMed=7592815; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [2] RP SEQUENCE FROM N.A. (ISOFORM BETA-2), AND PARTIAL SEQUENCE. RC TISSUE=Brain; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; BETA-1 (SHOWN HERE) AND BETA-2; CC ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: HIGHEST EXPRESSION IN BRAIN. CC -!- INDUCTION: ACTIVATED BY RETINOIC ACID IN NEUROBLASTOMA CELL LINES. CC -!- PTM: AT LEAST ISOFORM BETA-1 IS PHOSPHORYLATED ON SERINE RESIDUES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L42374; AAC37602.1; -. DR EMBL; Z69028; CAA93152.1; -. DR MIM; 601644; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Phosphorylation; Alternative splicing; Multigene family. FT VARSPLIC 1 19 METKLPPASTPTSPSSPGL -> MITVNPPLPQDTVNLF FT (IN ISOFORM BETA-2). FT CONFLICT 57 58 QE -> IF (IN REF. 2; AA SEQUENCE). FT CONFLICT 177 178 ES -> GA (IN REF. 2; AA SEQUENCE). FT CONFLICT 181 181 F -> M (IN REF. 2; AA SEQUENCE). FT CONFLICT 184 184 S -> M (IN REF. 2; AA SEQUENCE). FT CONFLICT 461 461 W -> E (IN REF. 2; AA SEQUENCE). SQ SEQUENCE 497 AA; 57393 MW; 8BEF84F20A77982D CRC64; METKLPPAST PTSPSSPGLS PVPPPDKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT PLPLLKDVPA SELHELLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEME EILDVIEPSQ FVKIQEPLFK QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKAQERQEL WQGLEELRLR RLQGTQGAKE APLQRLTPQV AASGGQS // ID 2A5B_RABIT STANDARD; PRT; 500 AA. AC Q28647; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE beta isoform (PP2A, B subunit, B' beta isoform) (PP2A, B subunit, DE B56 beta isoform) (PP2A, B subunit, PR61 beta isoform) (PP2A, B DE subunit, R5 beta isoform) (PP2A, B subunit, B'-alpha). GN PPP2R5B. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND; RX MEDLINE=96161994; PubMed=8576224; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: NOMENCLATURE USED IN REF.1 REFERS TO PP2A B SUBUNIT CC B' ALPHA ISOFORM, WHICH IS CITED AS PP2A B SUBUNIT BETA-PR61 CC ISOFORM IN LATER PUBLICATIONS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37769; AAC48527.1; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Multigene family; Nuclear protein. SQ SEQUENCE 500 AA; 57709 MW; 001CA9360E4C04B0 CRC64; METKLPPAST PTSPSSPGLS PVPPADKVDG FSRRSLRRAR PRRSHSSSQF RYQSNQQELT PLPLLKDVPA SELHDLLSRK LAQCGVMFDF LDCVADLKGK EVKRAALNEL VECVGSTRGV LIEPVYPDII RMISVNIFRT LPPSENPEFD PEEDEPNLEP SWPHLQLVYE FFLRFLESPD FQPSVAKRYV DQKFVLMLLE LFDSEDPRER EYLKTILHRV YGKFLGLRAY IRKQCNHIFL RFIYEFEHFN GVAELLEILG SIINGFALPL KTEHKQFLVR VLIPLHSVKS LSVFHAQLAY CVVQFLEKDA TLTEHVIRGL LKYWPKTCTQ KEVMFLGEVE EILDVIEPSQ FVKIQEPLFK QVARCVSSPH FQVAERALYF WNNEYILSLI EDNCHTVLPA VFGTLYQVSK EHWNQTIVSL IYNVLKTFME MNGKLFDELT ASYKLEKQQE QQKARERQEL WQGLEELRLR RLQGTQGTQG AREAPLQRFV PQVAATGGQS // ID 2A5D_HUMAN STANDARD; PRT; 602 AA. AC Q14738; O00696; O00494; Q15171; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE delta isoform (PP2A, B subunit, B' delta isoform) (PP2A, B subunit, DE B56 delta isoform) (PP2A, B subunit, PR61 delta isoform) (PP2A, B DE subunit, R5 delta isoform). GN PPP2R5D. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM DELTA-1). RC TISSUE=Fetal brain; RX MEDLINE=96355607; PubMed=8703017; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORMS DELTA-1 AND DELTA-3). RC TISSUE=Brain cortex; RX MEDLINE=97324098; PubMed=9180267; RA Tanabe O., Gomez G.A., Nishito Y., Usui H., Takeda M.; RT "Molecular heterogeneity of the cDNA encoding a 74-kDa regulatory RT subunit (B'' or delta) of human protein phosphatase 2A."; RL FEBS Lett. 408:52-56(1997). RN [3] RP SEQUENCE FROM N.A. (ISOFORM DELTA-2), AND PARTIAL SEQUENCE (DELTA-1). RC TISSUE=Brain cortex, and Bone marrow; RX MEDLINE=96159032; PubMed=8566219; RA Tanabe O., Nagase T., Murakami T., Nozaki H., Usui H., Nishito Y., RA Hayashi H., Kagamiyama H., Takeda M.; RT "Molecular cloning of a 74-kDa regulatory subunit (B'' or delta) of RT human protein phosphatase 2A."; RL FEBS Lett. 379:107-111(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC AND NUCLEAR IN INTERPHASE, CC NUCLEAR DURING MITOSIS. CC -!- ALTERNATIVE PRODUCTS: 3 ISOFORMS; DELTA-1 (SHOWN HERE), DELTA-2 CC AND DELTA-3; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: ISOFORM DELTA-2 IS WIDELY EXPRESSED. ISOFORM CC DELTA-1 IS HIGHLY EXPRESSED IN BRAIN. CC -!- INDUCTION: ACTIVATED BY RETINOIC ACID IN NEUROBLASTOMA CELL LINES. CC -!- PTM: AT LEAST ISOFORM DELTA-1 IS PHOSPHORYLATED ON SERINE CC RESIDUES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L76702; AAB69751.1; -. DR EMBL; AB000634; BAA20381.1; -. DR EMBL; AB000635; BAA20382.1; -. DR EMBL; D78360; BAA11372.1; -. DR MIM; 601646; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Nuclear protein; Phosphorylation; Alternative splicing; Repeat; KW Multigene family. FT DOMAIN 37 52 8 X 2 AA APPROXIMATE TANDEM REPEATS OF Q- FT P. FT DOMAIN 523 530 SH3 BINDING, CLASS I (POTENTIAL). FT DOMAIN 548 565 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT VARSPLIC 11 116 MISSING (IN ISOFORM DELTA-3). FT VARSPLIC 85 116 MISSING (IN ISOFORM DELTA-2). SQ SEQUENCE 602 AA; 69991 MW; F15F71AF4E565387 CRC64; MPYKLKKEKE PPKVAKCTAK PSSSGKDGGG ENTEEAQPQP QPQPQPQAQS QPPSSNKRPS NSTPPPTQLS KIKYSGGPQI VKKERRQSSS RFNLSKNREL QKLPALKDSP TQEREELFIQ KLRQCCVLFD FVSDPLSDLK FKEVKRAGLN EMVEYITHSR DVVTEAIYPE AVTMFSVNLF RTLPPSSNPT GAEFDPEEDE PTLEAAWPHL QLVYEFFLRF LESPDFQPNI AKKYIDQKFV LALLDLFDSE DPRERDFLKT ILHRIYGKFL GLRAYIRRQI NHIFYRFIYE TEHHNGIAEL LEILGSIING FALPLKEEHK MFLIRVLLPL HKVKSLSVYH PQLAYCVVQF LEKESSLTEP VIVGLLKFWP KTHSPKEVMF LNELEEILDV IEPSEFSKVM EPLFRQLAKC VSSPHFQVAE RALYYWNNEY IMSLISDNAA RVLPIMFPAL YRNSKSHWNK TIHGLIYNAL KLFMEMNQKL FDDCTQQYKA EKQKGRFRMK EREEMWQKIE ELARLNPQYP MFRAPPPLPP VYSMETETPT AEDIQLLKRT VETEAVQMLK DIKKEKVLLR RKSELPQDVY TIKALEAHKR AEEFLTASQE AL // ID 2A5D_RABIT STANDARD; PRT; 586 AA. AC Q28653; Q28655; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE delta isoform (PP2A, B subunit, B' delta isoform) (PP2A, B subunit, DE B56 delta isoform) (PP2A, B subunit, PR61 delta isoform) (PP2A, B DE subunit, R5 delta isoform) (PP2A, B subunit, B'-gamma). GN PPP2R5D. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND; TISSUE=Brain, and Skeletal muscle; RX MEDLINE=96161994; PubMed=8576224; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: NOMENCLATURE USED IN REF.1 REFERS TO PP2A B SUBUNIT CC B' GAMMA ISOFORM, WHICH IS CITED AS PP2A B SUBUNIT DELTA-PR61 CC ISOFORM IN LATER PUBLICATIONS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38193; AAC48532.1; -. DR EMBL; U38195; AAC48534.1; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Multigene family; Nuclear protein; Repeat. FT DOMAIN 21 36 8 X 2 AA APPROXIMATE TANDEM REPEATS OF Q- FT P. FT DOMAIN 507 514 SH3 BINDING, CLASS I (POTENTIAL). FT DOMAIN 532 549 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). SQ SEQUENCE 586 AA; 68090 MW; E149A309CDDA7495 CRC64; MSPSPSSSGK DGGGENAEEA QPQPQPQPQP QPQSQPPSSN KRPSNSTPPP TQLSKIKYSG GPQIVKKERR QSSSRFNLSK NRELQKLPAL KDSPTQEREE LFIQKLRQCC VLFDFVSDPL SDLKFKEVKR AGLNEMVEYI THSRDVVTEA IYPEAVTMFS VNLFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLALLDL FDSEDPRERD FLKTILHRIY GKFLGLRAYI RRQINHIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKMFLIRV LLPLHKVKSL SVYHPQLAYC VVQFLEKESS LTEPVIVGLL KFWPKTHSPK EVMFLNELEE ILDVIEPSEF SKVMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAARVLPIM FPALYRNSKS HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QYKAEKQKGR FRMKEREEMW QKIEELARLN PQYPMFRAPP PLPPVYSMET ETPTAEDIQL LKRTVETEAV QMLKDIKKEK VLLRRKSELP QDVYTIKALE AHKRAEEFLT ASQEAL // ID 2A5E_HUMAN STANDARD; PRT; 467 AA. AC Q16537; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform). GN PPP2R5E. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., AND SEQUENCE OF 449-455. RC TISSUE=Fetal retina; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [2] RP SEQUENCE FROM N.A. RC TISSUE=Fetal brain; RX MEDLINE=96355607; PubMed=8703017; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- PTM: PHOSPHORYLATED ON SERINE RESIDUES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z69029; CAA93153.1; -. DR EMBL; L76703; AAB69752.1; -. DR MIM; 601647; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Phosphorylation; Multigene family. SQ SEQUENCE 467 AA; 54699 MW; DD9CE11433F499CF CRC64; MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMFSS LYRISKEHWN PAIVALVYNV LKAFMEMNST MFDELTATYK SDRQREKKKE KEREELWKKL EDLELKRGLR RDGIIPT // ID 2A5E_MOUSE STANDARD; PRT; 387 AA. AC Q61151; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform) (Fragment). GN PPP2R5E. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Embryonic fibroblast; RX MEDLINE=97042488; PubMed=8887688; RA Okamoto K., Kamibayashi C., Serrano M., Prives C., Mumby M.C., RA Beach D.; RT "p53-dependent association between cyclin G and the B' subunit of RT protein phosphatase 2A."; RL Mol. Cell. Biol. 16:6593-6602(1996). RN [2] RP IDENTIFICATION OF PROBABLE FRAMESHIFT. RA Hulo C.; RL Unpublished observations (JAN-2000). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. INTERACTS WITH CYCLIN G (IN VITRO). CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: THIS IS A CONCEPTUAL TRANSLATION; A FRAMESHIFT WAS CC INTRODUCED FROM POSITION 112-135 TO EXTEND THE SIMILARITY WITH THE CC HUMAN HOMOLOG. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U49728; AAB37234.1; ALT_FRAME. DR MGD; MGI:1349473; Ppp2r5e. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Multigene family. FT NON_TER 1 1 FT NON_TER 387 387 SQ SEQUENCE 387 AA; 45497 MW; 780D5404848A548E CRC64; LKDVPTSEQP ELFLKKLQQC CVICDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FWESQEFQPS IAKKYIDQKF VLQLLELFDS EDPRERDYLK TVLHRIYGKF LGLRAFIRKQ INNIFLRFVY ETEHFNGVAE LLEILGSIIN GFALPLKAEH KQFLVKVLIP LHTVRSLSLF HAQLAYCIVQ FLEKDPSLTE PVIRGLMKFW PKTCSQKEVM FLGELEEILD VIEPSQFVKI QEPLFKQIAK CVSSPHFQVA ERALYYWNNE YIMSLIEENS NVILPIMSSS LYRISKEHWN PAIVALVYTV LKAFMEMNST MFDELTATYK SDRQREK // ID 2A5E_RABIT STANDARD; PRT; 165 AA. AC Q28654; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE epsilon isoform (PP2A, B subunit, B' epsilon isoform) (PP2A, B DE subunit, B56 epsilon isoform) (PP2A, B subunit, PR61 epsilon isoform) DE (PP2A, B subunit, R5 epsilon isoform) (PP2A, B subunit, B'-delta) DE (Fragment). GN PPP2R5E. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND; TISSUE=Brain; RX MEDLINE=96161994; PubMed=8576224; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN TESTIS, LUNG AND BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: NOMENCLATURE USED IN REF.1 REFERS TO PP2A B SUBUNIT CC B' DELTA ISOFORM, WHICH IS CITED AS PP2A B SUBUNIT EPSILON-PR61 CC ISOFORM IN LATER PUBLICATIONS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38194; AAC48533.1; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Multigene family. FT NON_TER 165 165 SQ SEQUENCE 165 AA; 19048 MW; 6F4A6E32D0D85B7D CRC64; MSSAPTTPPS VDKVDGFSRK SVRKARQKRS QSSSQFRSQG KPIELTPLPL LKDVPSSEQP ELFLKKLQQC CVIFDFMDTL SDLKMKEYKR STLNELVDYI TISRGCLTEQ TYPEVVRMVS CNIFRTLPPS DSNEFDPEED EPTLEASWPH LQLVYEFFIR FLESQ // ID 2A5G_HUMAN STANDARD; PRT; 524 AA. AC Q13362; Q14391; Q15174; Q15060; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform). GN PPP2R5C OR KIAA0044. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. (ISOFORM GAMMA-3). RC TISSUE=Umbilical vein; RX MEDLINE=96214950; PubMed=8617797; RA Tehrani M.A., Mumby M.C., Kamibayashi C.; RT "Identification of a novel protein phosphatase 2A regulatory subunit RT highly expressed in muscle."; RL J. Biol. Chem. 271:5164-5170(1996). RN [2] RP SEQUENCE FROM N.A. (ISOFORM GAMMA-1). RC TISSUE=Fetal retina; RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [3] RP SEQUENCE OF 2-524 FROM N.A. (ISOFORM GAMMA-2). RC TISSUE=Bone marrow; RX MEDLINE=96051398; PubMed=7584044; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K.-I., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [4] RP SEQUENCE OF 11-524 FROM N.A. (ISOFORM GAMMA-1). RX MEDLINE=96064678; PubMed=7592815; RA McCright B., Virshup D.M.; RT "Identification of a new family of protein phosphatase 2A regulatory RT subunits."; RL J. Biol. Chem. 270:26123-26128(1995). RN [5] RP PHOSPHORYLATION, AND SUBCELLULAR LOCATION. RX MEDLINE=96355607; PubMed=8703017; RA McCright B., Rivers A.M., Audlin S., Virshup D.M.; RT "The B56 family of protein phosphatase 2A (PP2A) regulatory subunits RT encodes differentiation-induced phosphoproteins that target PP2A to RT both nucleus and cytoplasm."; RL J. Biol. Chem. 271:22081-22089(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: AT LEAST ISOFORM GAMMA-1 AND ISOFORM GAMMA-3 CC ARE NUCLEAR. CC -!- ALTERNATIVE PRODUCTS: 3 ISOFORMS; GAMMA-1, GAMMA-2 AND GAMMA-3 CC (SHOWN HERE); ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: HIGHEST LEVELS IN HEART, SKELETAL MUSCLE AND CC BRAIN. LOWER LEVELS IN PANCREAS, KIDNEY, LUNG AND PLACENTA. VERY CC LOW LEVELS IN LIVER. CC -!- PTM: AT LEAST ISOFORM GAMMA-3 IS PHOSPHORYLATED ON SERINE RESIDUES CC WHILE ISOFORM GAMMA-1 IS NOT. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37352; AAC50387.1; ALT_INIT. DR EMBL; Z69030; CAA93154.1; -. DR EMBL; D26445; BAA05465.1; -. DR EMBL; L42375; AAC37603.1; -. DR MIM; 601645; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Nuclear protein; Phosphorylation; Alternative splicing; KW Multigene family. FT DOMAIN 416 422 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT VARSPLIC 443 524 YTVYSQASTMSIPVAMETDGPLFEDVQMLRKTVKDEAHQAQ FT KDPKKDRPLALRKSELPQDPHTKKALEAHCRADELASQDGR FT -> VLKKRIT (IN ISOFORM GAMMA-1). FT VARSPLIC 443 481 MISSING (IN ISOFORM GAMMA-2). FT CONFLICT 494 494 L -> R (IN REF. 3). SQ SEQUENCE 524 AA; 61017 MW; 28EBF54550D70C19 CRC64; MLTCNKAGSR MVVDAANSNG PFQPVVLLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYTVYSQAS TMSIPVAMET DGPLFEDVQM LRKTVKDEAH QAQKDPKKDR PLALRKSELP QDPHTKKALE AHCRADELAS QDGR // ID 2A5G_MOUSE STANDARD; PRT; 435 AA. AC Q60996; O35708; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform) (PP2A, B subunit, B'alpha3 isoform) DE (Fragment). GN PPP2R5C. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=T-cell; RX MEDLINE=96214950; PubMed=8617797; RA Tehrani M.A., Mumby M.C., Kamibayashi C.; RT "Identification of a novel protein phosphatase 2A regulatory subunit RT highly expressed in muscle."; RL J. Biol. Chem. 271:5164-5170(1996). RN [2] RP SEQUENCE OF 15-435 FROM N.A. RC STRAIN=C57BL/6; RX MEDLINE=96354596; PubMed=8752144; RA Francia G., Mitchell S.D., Moss S.E., Hanby A.M., Marshall J.F., RA Hart I.R.; RT "Identification by differential display of annexin-VI, a gene RT differentially expressed during melanoma progression."; RL Cancer Res. 56:3855-3858(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. INTERACTS WITH CYCLIN G IN VITRO. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC (BY SIMILARITY). CC -!- TISSUE SPECIFICITY: HIGHEST LEVELS IN HEART,LIVER AND BRAIN. LOWER CC LEVELS IN SKELETAL MUSCLE, SPLEEN, KIDNEY, AND LUNG. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U37353; AAC52435.1; -. DR EMBL; U59418; AAB70857.1; -. DR MGD; MGI:1349475; Ppp2r5c. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Multigene family. FT NON_TER 1 1 FT CONFLICT 15 15 D -> N (IN REF. 2). SQ SEQUENCE 435 AA; 51196 MW; E3C2DF4C57F729C2 CRC64; SNGPFQPVAL LHIRDVPPAD QEKLFIQKLR QCCVLFDFVS DPLSDLKWKE VKRASLSEMV EYITHNRNVI TEPIYPEAVH MFAVNMFRTL PPSSNPTGAE FDPEEDEPTL EAAWPHLQLV YEFFLRFLES PDFQPNIAKK YIDQKFVLQL LELFDSEDPR ERDFLKTTLH RIYGKFLGLR AYIRKQINNI FYRFIYETEH HNGIAELLEI LGSIINGFAL PLKEEHKIFL LKVLLPLHKV KSLSVYHPQL AYCVVQFLEK DSTLTEPVVM ALLKYWPKTH SPKEVMFLNE LEEILDVIEP SEFVKIMEPL FRQLAKCVSS PHFQVAERAL YYWNNEYIMS LISDNAAKIL PIMFPSLYRN SKTHWNKTIH GLIYNALKLF MEMNQKLFDD CTQQFKAEKL KEKLKMKERE EAWVKIENLA KANPQVLKKR VTREC // ID 2A5G_RABIT STANDARD; PRT; 524 AA. AC Q28651; Q28648; Q28650; Q28652; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 56 kDa regulatory subunit, DE gamma isoform (PP2A, B subunit, B' gamma isoform) (PP2A, B subunit, DE B56 gamma isoform) (PP2A, B subunit, PR61 gamma isoform) (PP2A, B DE subunit, R5 gamma isoform) (PP2A, B subunit, B' beta isoform). GN PPP2R5C. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND; TISSUE=Skeletal muscle; RX MEDLINE=96161994; PubMed=8576224; RA Csortos C., Zolnierowicz S., Bako E., Durbin S.D., Depaoli-Roach A.A.; RT "High complexity in the expression of the B' subunit of protein RT phosphatase 2A0. Evidence for the existence of at least seven novel RT isoforms."; RL J. Biol. Chem. 271:2578-2588(1996). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: NUCLEAR (BY SIMILARITY). CC -!- ALTERNATIVE PRODUCTS: 4 ISOFORMS; GAMMA-1/BETA-4, GAMMA-3/BETA- CC 3 (SHOWN HERE), GAMMA-4/BETA-1 AND GAMMA-5/BETA-2; ARE PRODUCED BY CC ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN TESTIS, HEART AND SPLEEN. CC ALSO FOUND IN BRAIN AND SKELETAL MUSCLE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U38191; AAC48530.1; -. DR EMBL; U37770; AAC48528.1; -. DR EMBL; U38190; AAC48529.1; -. DR EMBL; U38192; AAC48531.1; -. DR InterPro; IPR002554; B56. DR Pfam; PF01603; B56; 1. KW Alternative splicing; Multigene family; Nuclear protein. FT DOMAIN 472 489 NUCLEAR LOCALIZATION SIGNAL (POTENTIAL). FT VARSPLIC 482 524 AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQD FT GR -> QLVGRKAVSSTQVRKV (IN ISOFORM GAMMA- FT 4). FT VARSPLIC 482 524 AQKDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQD FT GR -> VKVPG (IN ISOFORM GAMMA-5). FT VARSPLIC 443 524 YSLCSHASTVSMPLAMETDGPLFEDVQMLRKTVSDEARQAQ FT KDPKKERPLARRKSELPQDPHTKKALEAHCRADELVPQDGR FT -> VLKKRAI (IN ISOFORM GAMMA-1). SQ SEQUENCE 524 AA; 60984 MW; DC4520D122DAF386 CRC64; MLTCNKAGSR MVVDAASSNG PFQPVALLHI RDVPPADQEK LFIQKLRQCC VLFDFVSDPL SDLKWKEVKR AALSEMVEYI THNRNVITEP IYPEVVHMFA VNMFRTLPPS SNPTGAEFDP EEDEPTLEAA WPHLQLVYEF FLRFLESPDF QPNIAKKYID QKFVLQLLEL FDSEDPRERD FLKTTLHRIY GKFLGLRAYI RKQINNIFYR FIYETEHHNG IAELLEILGS IINGFALPLK EEHKIFLLKV LLPLHKVKSL SVYHPQLAYC VVQFLEKDST LTEPVVMALL KYWPKTHSPK EVMFLNELEE ILDVIEPSEF VKIMEPLFRQ LAKCVSSPHF QVAERALYYW NNEYIMSLIS DNAAKILPIM FPSLYRNSKT HWNKTIHGLI YNALKLFMEM NQKLFDDCTQ QFKAEKLKEK LKMKEREEAW VKIENLAKAN PQYSLCSHAS TVSMPLAMET DGPLFEDVQM LRKTVSDEAR QAQKDPKKER PLARRKSELP QDPHTKKALE AHCRADELVP QDGR // ID 2A5R_MOUSE STANDARD; PRT; 491 AA. AC Q9Z176; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Protein phosphatase 2A, 59 kDa regulatory subunit B (PP2A PR59) (PP2A DE B''-PR59). GN PPP2R6. OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Teratocarcinoma; RX MEDLINE=99124398; PubMed=9927208; RA Voorhoeve P.M., Hijmans E.M., Bernards R.; RT "Functional interaction between a novel protein phosphatase 2A RT regulatory subunit, PR59, and the retinoblastoma-related p107 RT protein."; RL Oncogene 18:515-524(1999). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. INTERACTS WITH RETINOBLASTOMA-RELATED PROTEIN P107 CC (IN VIVO). MAY TARGET PP2A CORE DIMER TO P107 RESULTING IN CC DEPHOSPHORYLATION OF P107. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: EXPRESSED IN TESTIS, KIDNEY, LIVER, LUNG, CC SPLEEN, BRAIN AND HEART. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF050165; AAC98973.1; -. DR MGD; MGI:1335093; Ppp2r6. DR InterPro; IPR002048; EF-hand. DR Pfam; PF00036; efhand; 1. KW Multigene family. FT DOMAIN 464 469 POLY-ASP. SQ SEQUENCE 491 AA; 55705 MW; 4B4BAB5C864FB683 CRC64; MPERPPIRAL RRDPDDPAVA QALASLARGS DLVFPSRFQK WLRDFRQVHA HRKEEPPPQS PPPGHTVPAF YFPCGRPPPR PQDTEDAIAL VECAFEGLPR GRAGLGDMAV VAKACGCPLY WKAPLFYAAG GERTGSVSVH MFVAMWRKVL LTCHDDAARF VRLLGHPGCS GLIQEDFVPF LQDVVNSHPG LAFLRAAKDF HSRYITTVIQ RIFYTVNRSW SGMISREELR RSSFLQAVSQ LEVEPDINRM TSFFSYEHFY VIYCKFWELD LDRDLTIDRS DLARHGDGAI SSRMIDRIFS GAVTRARLPR KVGKLSYADF VWFLLSEEDK TTPTSTEYWF RCMDLDGDGA LSMFELEFFY EEQAQRMAAR GVEPLPFHDL ARQVLDLVAP RCPGRITLRD LKQCGLAGEF FDAFFNVDKY LAREQREQAG TPQDTDSDPA ASAWDRYAAE EYDFLVAEEA MAEDDDDHDE GSDPIDLYGL ADEDCDDLEP L // ID 2AAA_CAEEL STANDARD; PRT; 664 AA. AC Q09543; DT 01-NOV-1997 (Rel. 35, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Probable protein phosphatase PP2A regulatory subunit (Protein DE phosphatase PP2A regulatory subunit A). GN F48E8.5. OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea; OC Rhabditidae; Peloderinae; Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=BRISTOL N2; RA Kirsten J.; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME (BY SIMILARITY). CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U23514; AAC46541.1; -. DR HSSP; P30153; 1B3U. DR WormPep; F48E8.5; CE01957. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 14. DR PROSITE; PS50077; HEAT_REPEAT; 8. KW Hypothetical protein; Repeat. FT REPEAT 84 122 HEAT 1. FT REPEAT 123 160 HEAT 2. FT REPEAT 161 199 HEAT 3. FT REPEAT 200 237 HEAT 4. FT REPEAT 238 276 HEAT 5. FT REPEAT 277 315 HEAT 6. FT REPEAT 316 354 HEAT 7. FT REPEAT 355 397 HEAT 8. FT REPEAT 398 436 HEAT 9. FT REPEAT 437 475 HEAT 10. FT REPEAT 476 514 HEAT 11. FT REPEAT 515 553 HEAT 12. FT REPEAT 554 592 HEAT 13. FT REPEAT 593 631 HEAT 14. FT REPEAT 632 664 HEAT 15. FT DOMAIN 26 29 POLY-LEU. FT DOMAIN 260 263 POLY-ALA. SQ SEQUENCE 664 AA; 74930 MW; F3CA6F8189965F8F CRC64; MDCAIAVRER WPFSASLRIT VAAVSLLLLS PLFFCMFVRY SKMTIRRFCK FFQNTQFFYF LSNLFLQKPP ALFIMSVVEE ATDDALYPIA VLIDELRNED VTLRLNSIRK LSTIALALGV ERTRNELIQF LTDTIYDEDE VLLVLAEQLG NFTPLVGGPD HVHCLLLPLE NLATVEETVV RDKAVESLRK IADKHSSASL EEHFVPMLRR LATGDWFTSR TSACGLFSVV YPRVSPAIKS ELKSMFRTLC RDDTPMVRRA AAAKLGEFAK VFEKTAVIEG LHSSLTDLHV DEQDSVRLLT VESAIAFGTL LDKANKKKLI EPILIELFDD KSWRVRYMVA EKLIEIQNVL GEDMDTTHLV NMYTNLLKDP EGEVRCAATQ RLQEFALNLP EDKRQNIICN SLLNVAKELV TDGNQLVKSE LAGVIMGLAP LIGKEQTVSE LLPIYMQLLN DQTPEVRLNI ISSLDKVNEV IGAAQLSTSL LPAIVGLAED GKWRVRLAIV QFMPLLASQL GQEFFDEKLL PLCLNWLTDH VFSIREASTL IMKELTQKFG GQWASTNIVP KMQKLQKDTN YLQRMTCLFC LNTLSEAMTQ EQILKEIMPI VKDLVEDDVP NVRFNAAKSL KRIGKNLTPS TLTSEVKPLL EKLGKDSDFD VRYFSEEAKN SLGL // ID 2AAA_DROME STANDARD; PRT; 590 AA. AC P36179; Q9VLN3; DT 01-JUN-1994 (Rel. 29, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein phosphatase PP2A, 65 kDa regulatory subunit (Protein DE phosphatase PP2A regulatory subunit A) (PR65). GN PP2A-29B OR CG17291. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92329996; PubMed=1320961; RA Mayer-Jaekel R.E., Baumgartner S., Bilbe G., Ohkura H., Glover D.M., RA Hemmings B.A.; RT "Molecular cloning and developmental expression of the catalytic and RT 65-kDa regulatory subunits of protein phosphatase 2A in RT Drosophila."; RL Mol. Biol. Cell 3:287-298(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- TISSUE SPECIFICITY: EXPRESSION VARIES IN TISSUES THROUGHOUT CC DEVELOPMENT. IN LATE EMBRYONAL DEVELOPMENT IT IS FOUND AT HIGH CC LEVELS IN SNC AND GONADS; IN THIRD INSTAR LARVAE IT IS FOUND IN CC BRAIN, IMAGINAL DISKS AND SALIVARY GLANDS. CC -!- DEVELOPMENTAL STAGE: MOST ABUNDANT DURING EARLY EMBRYOGENESIS. CC EXPRESSED AT LOWER LEVELS IN LARVAE AND ADULT. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M86442; AAA28304.1; -. DR EMBL; AE003621; AAF52651.1; -. DR PIR; A43767; A43767. DR HSSP; P30153; 1B3U. DR FlyBase; FBgn0005776; Pp2A-29B. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 14. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Repeat; Acetylation. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT REPEAT 9 47 HEAT 1. FT REPEAT 48 85 HEAT 2. FT REPEAT 86 124 HEAT 3. FT REPEAT 125 162 HEAT 4. FT REPEAT 163 201 HEAT 5. FT REPEAT 202 240 HEAT 6. FT REPEAT 241 279 HEAT 7. FT REPEAT 280 322 HEAT 8. FT REPEAT 323 361 HEAT 9. FT REPEAT 362 400 HEAT 10. FT REPEAT 401 439 HEAT 11. FT REPEAT 440 478 HEAT 12. FT REPEAT 479 517 HEAT 13. FT REPEAT 518 556 HEAT 14. FT REPEAT 557 590 HEAT 15. FT CONFLICT 232 232 S -> T (IN REF. 1). SQ SEQUENCE 590 AA; 65280 MW; ABE4317F248FA37A CRC64; AASDKSVDDS LYPIAVLIDE LKNEDVQLRL NSIKKLSTIA LALGEERTRS ELIPFLTETI YDEDEVLLAL ADQLGNFTSL VGGPEFAMYL IPPLESLATV EETVVRDKAV ESLRTVAAEH SAQDLEIHVV PTLQRLVSGD WFTSRTSACG LFSVCYPRVT QPVKAELRAN FRKLCQDETP MVRRAAANKL GEFAKVVETE YLKSDLIPNF VQLAQDDQDS VRLLAVEACV TSAQLLPQDD VEHLVLPTLR QCASDSSWRV RYMVAEKFVD LQKAVGPEIT RVDLVPAFQY LLKDAEAEVR AAVATKVKDF CANLDKVNQV QIILSSILPY VRDLVSDPNP HVKSALASVI MGLSPMLGAY QTVEQLLPLF LIQLKDECPE VRLNIISNLD CVNDVIGIQQ LSQSLLPAIV ELAEDSKWRV RLAIIEYMPA LAGQLGQEFF DQKLRGLCMG WLNDHVYAIR EAATLNMKKL VEQFGAPWAE QAIIPMILVM SRNKNYLHRM TCLFCLNVLA EVCGTDITTK LLLPTVLLLA ADPVANVRFN VAKTLQKISP FLEASVIDAQ VKPTLDKLNT DTDVDVKHFA AQAIAGIAAA // ID 2AAA_HUMAN STANDARD; PRT; 588 AA. AC P30153; Q13773; DT 01-APR-1993 (Rel. 25, Created) DT 01-JUL-1993 (Rel. 26, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 65 KDA regulatory subunit A, DE alpha isoform (PP2A, subunit A, PR65-alpha isoform) (PP2A, subunit A, DE R1-alpha isoform) (Medium tumor antigen-associated 61 KDA protein). GN PPP2R1A. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=90241887; PubMed=2159327; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase RT 2A have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [2] RP SEQUENCE FROM N.A., AND SEQUENCE OF 241-254. RC TISSUE=Placenta; RX MEDLINE=90046854; PubMed=2554323; RA Walter G., Ferre F., Espiritu O., Carbone-Wiley A.; RT "Molecular cloning and sequence of cDNA encoding polyoma medium tumor RT antigen-associated 61-kDa protein."; RL Proc. Natl. Acad. Sci. U.S.A. 86:8669-8672(1989). RN [3] RP SEQUENCE OF 203-213; 260-271 AND 520-526. RX MEDLINE=96276417; PubMed=8694763; RA Zolnierowicz S., van Hoof C., Andjelkovic N., Cron P., Stevens I., RA Merlevede W., Goris J., Hemmings B.A.; RT "The variable subunit associated with protein phosphatase 2A0 defines RT a novel multimember family of regulatory subunits."; RL Biochem. J. 317:187-194(1996). RN [4] RP BINDING DOMAINS. RX MEDLINE=94076400; PubMed=8254721; RA Ruediger R., Hentz M., Fait J., Mumby M., Walter G.; RT "Molecular model of the A subunit of protein phosphatase 2A: RT interaction with other subunits and tumor antigens."; RL J. Virol. 68:123-129(1994). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX MEDLINE=99142607; PubMed=9989501; RA Groves M.R., Hanlon N., Turowski P., Hemmings B.A., Barford D.; RT "The structure of the protein phosphatase 2A PR65/A subunit reveals RT the conformation of its 15 tandemly repeated HEAT motifs."; RL Cell 96:99-110(1999). CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; J02902; AAA36399.1; -. DR EMBL; M31786; AAA35531.1; -. DR PIR; A34541; A34541. DR MIM; 605983; -. DR PDB; 1B3U; 09-FEB-99. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 14. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Multigene family; Acetylation; Repeat; Polymorphism; 3D-structure. FT INIT_MET 0 0 FT MOD_RES 1 1 ACETYLATION. FT REPEAT 7 45 HEAT 1. FT REPEAT 46 83 HEAT 2. FT REPEAT 84 122 HEAT 3. FT REPEAT 123 160 HEAT 4. FT REPEAT 161 199 HEAT 5. FT REPEAT 200 238 HEAT 6. FT REPEAT 239 277 HEAT 7. FT REPEAT 278 320 HEAT 8. FT REPEAT 321 359 HEAT 9. FT REPEAT 360 398 HEAT 10. FT REPEAT 399 437 HEAT 11. FT REPEAT 438 476 HEAT 12. FT REPEAT 477 515 HEAT 13. FT REPEAT 516 554 HEAT 14. FT REPEAT 555 588 HEAT 15. FT DOMAIN 7 398 PP2A SUBUNIT B BINDING. FT DOMAIN 46 320 POLYOMA SMALL AND MEDIUM T ANTIGEN FT BINDING. FT DOMAIN 84 238 SV40 SMALL T ANTIGEN BINDING. FT DOMAIN 399 588 PP2A SUBUNIT C BINDING. FT VARIANT 86 86 H -> R (IN LUNG). FT /FTId=VAR_006383. FT CONFLICT 129 129 P -> A (IN REF. 2). FT CONFLICT 257 257 A -> R (IN REF. 2). FT CONFLICT 271 271 K -> R (IN REF. 3). SQ SEQUENCE 588 AA; 65092 MW; 2D08A93195A885D2 CRC64; AAADGDDSLY PIAVLIDELR NEDVQLRLNS IKKLSTIALA LGVERTRSEL LPFLTDTIYD EDEVLLALAE QLGTFTTLVG GPEYVHCLLP PLESLATVEE TVVRDKAVES LRAISHEHSP SDLEAHFVPL VKRLAGGDWF TSRTSACGLF SVCYPRVSSA VKAELRQYFR NLCSDDTPMV RRAAASKLGE FAKVLELDNV KSEIIPMFSN LASDEQDSVR LLAVEACVNI AQLLPQEDLE ALVMPTLRQA AEDKSWAVRY MVADKFTELQ KAVGPEITKT DLVPAFQNLM KDCEAEVRAA ASHKVKEFCE NLSADCRENV IMSQILPCIK ELVSDANQHV KSALASVIMG LSPILGKDNT IEHLLPLFLA QLKDECPEVR LNIISNLDCV NEVIGIRQLS QSLLPAIVEL AEDAKWRVRL AIIEYMPLLA GQLGVEFFDE KLNSLCMAWL VDHVYAIREA ATSNLKKLVE KFGKEWAHAT IIPKVLAMSG DPNYLHRMTT LFCINVLSEV CGQDITTKHM LPTVLRMAGD PVANVRFNVA KSLQKIGPIL DNSTLQSEVK PILEKLTQDQ DVDVKYFAQE ALTVLSLA // ID 2AAA_PEA STANDARD; PRT; 395 AA. AC P36875; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Protein phosphatase PP2A regulatory subunit A (PR65) (Fragment). OS Pisum sativum (Garden pea). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; Rosidae; OC eurosids I; Fabales; Fabaceae; Papilionoideae; Vicieae; Pisum. OX NCBI_TaxID=3888; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=CV. JI 813; RX MEDLINE=94207195; PubMed=8155887; RA Evans I.M., Fawcett T., Boulter D., Fordham-Skelton A.P.; RT "A homologue of the 65 kDa regulatory subunit of protein phosphatase RT 2A in early pea (Pisum sativum L.) embryos."; RL Plant Mol. Biol. 24:689-695(1994). CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS AT LEAST 8 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z25888; CAA81107.1; -. DR PIR; S40171; S40171. DR PIR; S43776; S43776. DR HSSP; P30153; 1B3U. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 10. DR PROSITE; PS50077; HEAT_REPEAT; 8. KW Repeat. FT NON_TER 1 1 FT REPEAT 44 81 HEAT 1. FT REPEAT 83 120 HEAT 2. FT REPEAT 122 159 HEAT 3. FT REPEAT 161 198 HEAT 4. FT REPEAT 200 237 HEAT 5. FT REPEAT 239 276 HEAT 6. FT REPEAT 279 316 HEAT 7. FT REPEAT 318 355 HEAT 8. SQ SEQUENCE 395 AA; 43911 MW; F444DBDC935F8A04 CRC64; VEAAHLKTDI MSVFDDLTQD DQDSFRFLAV EGCAALGKLL EPQDCLAHIL PVIVNFSQDK SWRVRYMVAN QLYELCEAVG PDSTKTELVP AYVRLLRDNV AEVRIAAAGK VSKFSRILSP ELAIQHILPC VKELSTDSSQ HVRSALASVI MGMAPVLGKD ATIEQLLPIF LSLLKDEFPD VRLNIISKLD QVNQVIGIDL LSQSLLPAIV ELAEDRHWRV RLAIIEYIPL LASQLGVGFF DDKLGALIMQ WLKDKEYSIR NAAANNVKRL AAEEFGPEWA MQHIIPQVLD MINDPHYLYR MTILHAISLL APVLGSEITS TNLLPLVVNA SKDRVPNIKF NVAKVLQSLI PIVDESVVES TIRPCLVELS EDPDVDVRFF ASQALQSSDQ VKMSS // ID 2AAA_PIG STANDARD; PRT; 588 AA. AC P54612; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 65 kDa regulatory subunit A, DE alpha isoform (PP2A, subunit A, PR65-alpha isoform) (PP2A, subunit A, DE R1-alpha isoform). GN PPP2R1A. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34955; CAA84414.1; -. DR HSSP; P30153; 1B3U. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 14. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Multigene family; Acetylation; Repeat. FT INIT_MET 0 0 BY SIMILARITY. FT MOD_RES 1 1 ACETYLATION (BY SIMILARITY). FT REPEAT 7 45 HEAT 1. FT REPEAT 46 83 HEAT 2. FT REPEAT 84 122 HEAT 3. FT REPEAT 123 160 HEAT 4. FT REPEAT 161 199 HEAT 5. FT REPEAT 200 238 HEAT 6. FT REPEAT 239 277 HEAT 7. FT REPEAT 278 320 HEAT 8. FT REPEAT 321 359 HEAT 9. FT REPEAT 360 398 HEAT 10. FT REPEAT 399 437 HEAT 11. FT REPEAT 438 476 HEAT 12. FT REPEAT 477 515 HEAT 13. FT REPEAT 516 554 HEAT 14. FT REPEAT 555 588 HEAT 15. SQ SEQUENCE 588 AA; 65191 MW; 99956CA566957821 CRC64; AAADGDDSLY PIAVLIDELR NEDVQLRLNS IKKLSTIALA LGVERTRSEL LPFLTDTIYD EDEVLLALAE QLGTFTTLVG GPEYVHCLLP PLESLATVEE TVVRDKAVES LRAISHEHSP SDLEAHFVPL VKRLAGGDWF TSRTSACGLF SVCYPRVSSA VKAELRQYFR NLCSDDTPMV RRAAASKLGE FAKVLELDNV KSEIIPMFSN LASDEQDSVR LLAVEACVNI AQLLPQEDLE ALVMPTLRQA AEDKSWRVRY MVADKFTELQ KAVGPEITKT DLVPAFQNLM KDCEAEVRAA ASHKVKEFCE NLSADCRENV IMTQILPCIK ELVSDANQHV KSALASVIMG LSPILGKDNT IEHLLPLFLA QLKDECPEVR LNIISNLDCV NEVIGIRQLS QSLLPAIVEL AEDAKWRVRL AIIEYMPLLA GQLGVEFFDE KLNSLCMAWL VDHVYAIREA ATSNLKKLVE KFGKEWAHAT IIPKVLAMSG DPNYLHRMTT LFCINVLSEV CGQDITTKHM LPTVLRMAGD PVANVRFNVA KSLQKIGPIL DNSTLQSEVK PILEKLTQDQ DVDVKYFAQE ALTVLSLA // ID 2AAA_YEAST STANDARD; PRT; 635 AA. AC P31383; DT 01-JUL-1993 (Rel. 26, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein phosphatase PP2A regulatory subunit A (PR65). GN TPD3 OR YAL016W OR FUN32. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=S288C; RX MEDLINE=93024440; PubMed=1328868; RA van Zyl W., Huang W., Sneddon A.A., Stark M., Camier S., Werner M., RA Marck C., Sentenac A., Broach J.R.; RT "Inactivation of the protein phosphatase 2A regulatory subunit A RT results in morphological and transcriptional defects in Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 12:4946-4959(1992). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RX MEDLINE=93209532; PubMed=8458570; RA Ouellette B.F.F., Clark M.W., Keng T., Storms R.K., Zhong W.W., RA Zeng B., Fortin N., Delaney S., Barton A.B., Kaback D.B., Bussey H.; RT "Sequencing of chromosome I from Saccharomyces cerevisiae: analysis RT of a 32 kb region between the LTE1 and SPO7 genes."; RL Genome 36:32-42(1993). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=S288C / AB972; RX MEDLINE=94193531; PubMed=8144453; RA Barton A.B., Kaback D.B.; RT "Molecular cloning of chromosome I DNA from Saccharomyces cerevisiae: RT analysis of the genes in the FUN38-MAK16-SPO7 region."; RL J. Bacteriol. 176:1872-1880(1994). CC -!- FUNCTION: PHOSPHATASE 2A AFFECTS A VARIETY OF BIOLOGICAL PROCESSES CC IN THE CELL SUCH AS TRANSCRIPTION, CELL CYCLE PROGRESSION AND CC CELLULAR MORPHOGENESIS, AND PROVIDES AN INITIAL IDENTIFICATION OF CC CRITICAL SUBSTRATES FOR THIS PHOSPHATASE. THE REGULATORY SUBUNIT CC MAY DIRECT THE CATALYTIC SUBUNIT TO DISTINCT, ALBEIT OVERLAPPING, CC SUBSETS OF SUBSTRATES. CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L05146; AAC04941.1; -. DR EMBL; M98389; AAA35163.1; -. DR PIR; S31296; S31296. DR HSSP; P30153; 1B3U. DR SGD; S0000014; TPD3. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 15. DR PROSITE; PS50077; HEAT_REPEAT; 9. KW Multigene family; Repeat. FT REPEAT 34 72 HEAT 1. FT REPEAT 73 111 HEAT 2. FT REPEAT 112 150 HEAT 3. FT REPEAT 151 189 HEAT 4. FT REPEAT 190 228 HEAT 5. FT REPEAT 229 273 HEAT 6. FT REPEAT 274 316 HEAT 7. FT REPEAT 317 356 HEAT 8. FT REPEAT 357 395 HEAT 9. FT REPEAT 396 434 HEAT 10. FT REPEAT 435 473 HEAT 11. FT REPEAT 474 512 HEAT 12. FT REPEAT 513 553 HEAT 13. FT REPEAT 554 598 HEAT 14. FT REPEAT 599 632 HEAT 15. FT CONFLICT 611 611 F -> C (IN REF. 1). SQ SEQUENCE 635 AA; 70951 MW; 7B8305FB20633DC8 CRC64; MSGARSTTAG AVPSAATTST TSTTSNSKDS DSNESLYPLA LLMDELKHDD IANRVEAMKK LDTIALALGP ERTRNELIPF LTEVAQDDED EVFAVLAEQL GKFVPYIGGP QYATILLPVL EILASAEETL VREKAVDSLN NVAQELSQEQ LFSDFVPLIE HLATADWFSS KVSACGLFKS VIVRIKDDSL RKNILALYLQ LAQDDTPMVK RAVGKNLPIL IDLLTQNLGL STDEDWDYIS NIFQKIINDN QDSVKFLAVD CLISILKFFN AKGDESHTQD LLNSAVKLIG DEAWRVRYMA ADRFSDLASQ FSSNQAYIDE LVQPFLNLCE DNEGDVREAV AKQVSGFAKF LNDPSIILNK ILPAVQNLSM DESETVRSAL ASKITNIVLL LNKDQVINNF LPILLNMLRD EFPDVRLNII ASLKVVNDVI GIELLSDSLL PAITELAKDV NWRVRMAIIE YIPILAEQLG MQFFDQQLSD LCLSWLWDTV YSIREAAVNN LKRLTEIFGS DWCRDEIISR LLKFDLQLLE NFVSRFTILS ALTTLVPVVS LDVVTEQLLP FISHLADDGV PNIRFNVAKS YAVIVKVLIK DEAKYDALIK NTILPSLQTL FQDEDVDVKY FAKKSLAECQ ELLKN // ID 2AAB_HUMAN STANDARD; PRT; 601 AA. AC P30154; O75620; DT 01-APR-1993 (Rel. 25, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 65 kDa regulatory subunit A, DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform). GN PPP2R1B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=99014242; PubMed=9795170; RA Baysal B.E., Farr J.E., Goss J.R., Devlin B., Richard C.W. III; RT "Genomic organization and precise physical location of protein RT phosphatase 2A regulatory subunit A beta isoform gene on chromosome RT band 11q23."; RL Gene 217:107-116(1998). RN [2] RP SEQUENCE OF 27-601 FROM N.A. RX MEDLINE=90241887; PubMed=2159327; RA Hemmings B.A., Adams-Pearson C., Maurer F., Mueller P., Goris J., RA Merlevede W., Hofsteenge J., Stone S.R.; RT "Alpha- and beta-forms of the 65-kDa subunit of protein phosphatase RT 2A have a similar 39 amino acid repeating structure."; RL Biochemistry 29:3166-3173(1990). RN [3] RP SEQUENCE FROM N.A., AND VARIANT LUNG CANCER ASP-90. RX MEDLINE=98438696; PubMed=9765152; RA Wang S.S., Esplin E.D., Li J.L., Huang L., Gazdar A., Minna J., RA Evans G.A.; RT "Alterations of the PPP2R1B gene in human lung and colon cancer."; RL Science 282:284-287(1998). CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- DISEASE: DEFECTS IN PPP2R1B COULD BE THE CAUSE OF SOME LUNG AND CC COLON CANCERS. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF083439; AAC63525.1; -. DR EMBL; AF083425; AAC63525.1; JOINED. DR EMBL; AF083426; AAC63525.1; JOINED. DR EMBL; AF083427; AAC63525.1; JOINED. DR EMBL; AF083428; AAC63525.1; JOINED. DR EMBL; AF083429; AAC63525.1; JOINED. DR EMBL; AF083430; AAC63525.1; JOINED. DR EMBL; AF083431; AAC63525.1; JOINED. DR EMBL; AF083432; AAC63525.1; JOINED. DR EMBL; AF083433; AAC63525.1; JOINED. DR EMBL; AF083434; AAC63525.1; JOINED. DR EMBL; AF083435; AAC63525.1; JOINED. DR EMBL; AF083436; AAC63525.1; JOINED. DR EMBL; AF083437; AAC63525.1; JOINED. DR EMBL; AF083438; AAC63525.1; JOINED. DR EMBL; M65254; AAA59983.1; -. DR EMBL; AF087438; AAC69624.1; -. DR HSSP; P30153; 1B3U. DR MIM; 603113; -. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 14. DR PROSITE; PS50077; HEAT_REPEAT; 12. KW Multigene family; Repeat; Disease mutation. FT REPEAT 20 58 HEAT 1. FT REPEAT 59 96 HEAT 2. FT REPEAT 97 135 HEAT 3. FT REPEAT 136 173 HEAT 4. FT REPEAT 174 212 HEAT 5. FT REPEAT 213 251 HEAT 6. FT REPEAT 252 290 HEAT 7. FT REPEAT 291 333 HEAT 8. FT REPEAT 334 372 HEAT 9. FT REPEAT 373 411 HEAT 10. FT REPEAT 412 450 HEAT 11. FT REPEAT 451 489 HEAT 12. FT REPEAT 490 528 HEAT 13. FT REPEAT 529 567 HEAT 14. FT REPEAT 568 601 HEAT 15. FT VARIANT 90 90 G -> D (IN LUNG CANCER). FT /FTId=VAR_006384. FT CONFLICT 27 30 VLID -> EFRP (IN REF. 2). FT CONFLICT 74 74 E -> V (IN REF. 2). FT CONFLICT 178 178 T -> I (IN REF. 3). FT CONFLICT 411 411 Q -> R (IN REF. 2). SQ SEQUENCE 601 AA; 66201 MW; 4A5B10EEF7432F74 CRC64; MAGASELGTG PGAAGGDGDD SLYPIAVLID ELRNEDVQLR LNSIKKLSTI ALALGVERTR SELLPFLTDT IYDEDEVLLA LAEQLGNFTG LVGGPDFAHC LLPPLENLAT VEETVVRDKA VESLRQISQE HTPVALEAYF VPLVKRLASG DWFTSRTSAC GLFSVCYPRA SNAVKAETRQ QFRSLCSDDT PMVRRAAASK LGEFAKVLEL DSVKSEIVPL FTSLASDEQD SVRLLAVEAC VSIAQLLSQD DLETLVMPTL RQAAEDKSWR VRYMVADRFS ELQKAMGPKI TLNDLIPAFQ NLLKDCEAEV RAAAAHKVKE LGENLPIEDR ETIIMNQILP YIKELVSDTN QHVKSALASV IMGLSTILGK ENTIEHLLPL FLAQLKDECP DVRLNIISNL DCVNEVIGIR QLSQSLLPAI VELAEDAKWR VRLAIIEYMP LLAGQLGVEF FDEKLNSLCM AWLVDHVYAI REAATNNLMK LVQKFGTEWA QNTIVPKVLV MANDPNYLHR MTTLFCINAL SEACGQEITT KQMLPIVLKM AGDQVANVRF NVAKSLQKIG PILDTNALQG EVKPVLQKLG QDEDMDVKYF AQEAISVLAL A // ID 2AAB_PIG STANDARD; PRT; 602 AA. AC P54613; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 65 kDa regulatory subunit A, DE beta isoform (PP2A, subunit A, PR65-beta isoform) (PP2A, subunit A, DE R1-beta isoform) (Fragment). GN PPP2R1B. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: THE PR65 SUBUNIT OF PROTEIN PHOSPHATASE 2A SERVES AS A CC SCAFFOLDING MOLECULE TO COORDINATE THE ASSEMBLY OF THE CATALYTIC CC SUBUNIT AND A VARIABLE REGULATORY B SUBUNIT. CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- DOMAIN: EACH HEAT REPEAT APPEARS TO CONSIST OF TWO ALPHA HELICES CC JOINED BY A HYDROPHILIC REGION, THE INTRAREPEAT LOOP. THE REPEAT CC UNITS MAY BE ARRANGED LATERALLY TO FORM A ROD-LIKE STRUCTURE. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT A CC FAMILY. CC -!- SIMILARITY: CONTAINS 15 HEAT REPEATS. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34931; CAA84403.1; -. DR HSSP; P30153; 1B3U. DR InterPro; IPR000357; HEAT_repeat. DR Pfam; PF02985; HEAT; 15. DR PROSITE; PS50077; HEAT_REPEAT; 11. KW Multigene family; Repeat. FT NON_TER 1 1 FT REPEAT 21 59 HEAT 1. FT REPEAT 60 97 HEAT 2. FT REPEAT 98 136 HEAT 3. FT REPEAT 137 174 HEAT 4. FT REPEAT 175 213 HEAT 5. FT REPEAT 214 252 HEAT 6. FT REPEAT 253 291 HEAT 7. FT REPEAT 292 334 HEAT 8. FT REPEAT 335 373 HEAT 9. FT REPEAT 374 412 HEAT 10. FT REPEAT 413 451 HEAT 11. FT REPEAT 452 490 HEAT 12. FT REPEAT 491 529 HEAT 13. FT REPEAT 530 568 HEAT 14. FT REPEAT 569 602 HEAT 15. SQ SEQUENCE 602 AA; 66213 MW; D71EAD46C2B7BB03 CRC64; NSAGAAAPGT GPVAAGGDGD DSLYPIAVLI DELRNEDVQL RLNSIKKLST IALALGVERT RTELLPFLTD TIYDEDEVLL ALAEQLGNFT GLVGGPDFAH CLLPPLESLA TVEETVVRDK AVESLRQISQ EHTPVALEAH FVPLVKRLAS GDWFTSRTSA CGLFSVCYPR ASNAVKAEIR QHFRSLCSDD TPMVRRAAAS KLGEFAKVLE LDSVKSEIVP LFTNLASDEQ DSVRLLAVEA CVSIAQLLSQ DDLEALVMPT LRQAAEDKSW RVRYMVADKF SELQRAVGPK ITLNDLIPAF QNLLKDCEAE VRAAAAHKVK ELCENLPIEG RETIIMNQIL PCIKELVSDT NQHVKSALAS VIMGLSTILG KENTIEHLLP LFLAQLKDEC PEVRLNIISN LDCVNEVIGI RQLSQSLLPA IVELAEDAKW RVRLAIIEYM PLLAGQLGVE FFDEKLNSLC MAWLVDHVYA IREAATNNLM KLVQKFGTEW AQNTIVPKVL VMANDPNYLH RMTTLFCINV LSEACGQEIT TKQMLPIVLK MAGDQVANVR FNVAKSLQKI GPILDTDALQ EEVKPVLQKL GQDEDMDVKY FAQEAISVLA LA // ID 2ABA_CANTR STANDARD; PRT; 508 AA. AC P53031; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Protein phosphatase PP2A regulatory subunit B (PR55) (Cell division DE control protein 55). GN CDC55. OS Candida tropicalis (Yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; mitosporic Saccharomycetales; Candida. OX NCBI_TaxID=5482; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NCYC 2512; RX MEDLINE=97082501; PubMed=8923737; RA Rodriguez P.L., Ali R., Serrano R.; RT "CtCdc55p and CtHa13p: two putative regulatory proteins from Candida RT tropicalis with long acidic domains."; RL Yeast 12:1321-1329(1996). CC -!- FUNCTION: PHOSPHATASE 2A AFFECTS A VARIETY OF BIOLOGICAL PROCESSES CC IN THE CELL SUCH AS TRANSCRIPTION, CELL CYCLE PROGRESSION AND CC CELLULAR MORPHOGENESIS, AND PROVIDES AN INITIAL IDENTIFICATION OF CC CRITICAL SUBSTRATES FOR THIS PHOSPHATASE. THE REGULATORY SUBUNIT CC MAY DIRECT THE CATALYTIC SUBUNIT TO DISTINCT, ALBEIT OVERLAPPING, CC SUBSETS OF SUBSTRATES (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA (PR65) (SUBUNIT A) AND A 55 KDA (PR55) (SUBUNIT B) CC REGULATORY SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; X88899; CAA61361.1; -. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 4. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Cell cycle. FT DOMAIN 396 407 POLY-ASP. SQ SEQUENCE 508 AA; 57914 MW; 619B4C78BBC7A324 CRC64; MNLDFSQCFG DKGDIENITE ADIISTVEFD HTGDFLATGD KGGRVVLFER NQSKKKQSCE YKFFTEFQSH DAEFDYLKSL EIEEKINKIK WLKSANDSLC LLSTNDKTIK LWKIQERQIK LVSENNLNGL NHLPSSNIGI ESLKLPQLQL HDKLISAQPK KIYANAHAYH INSISVNSDQ ETYLSADDLR INLWNLGIAD QSFNIVDIKP ANMEELTEVI TSAEFHPLQC NLFMYSSSKG TIKLSDMRSN SLCDSHAKIF EEYLDPSSHN FFTEITSSIS DVKFSHDGRY IASRDYMTVK IWDLAMENKP IKTIDVHEHL RERLCDTYEN DAIFDKFEVQ FGGDNKSVMT GSYNNQFVIY PNAVNTGNDD KPKFKSAFKN SSKRSKKNGF STRTTDDDDD DDDDDDDEEA DDEFDEEVPA TKNSPGSQLE DDDEQEEIIL QADKSAFKSK KSGQHPMRRR MTSGVGSNLG REFDDVDFKK SILHLSWHPR ENSVAIAATN NLYIFSTL // ID 2ABA_DROME STANDARD; PRT; 499 AA. AC P36872; Q9VH22; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein phosphatase PP2A, 55 kDa regulatory subunit (Protein DE phosphatase PP2A regulatory subunit B) (PR55) (Twins protein). GN TWS OR PP2A-85F OR AAR OR CG6235. OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Tracheata; Hexapoda; Insecta; OC Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; OC Ephydroidea; Drosophilidae; Drosophila. OX NCBI_TaxID=7227; RN [1] RP SEQUENCE FROM N.A., AND ALTERNATIVE SPLICING. RX MEDLINE=93177843; PubMed=8382567; RA Mayer-Jaekel R.E., Ohkura H., Gomes R., Sunkel C.E., Baumgartner S., RA Hemmings B.A., Glover D.M.; RT "The 55 kd regulatory subunit of Drosophila protein phosphatase 2A is RT required for anaphase."; RL Cell 72:621-633(1993). RN [2] RP SEQUENCE FROM N.A. (SHORT ISOFORM). RC STRAIN=OREGON-R; TISSUE=Eye imaginal disk; RX MEDLINE=93194062; PubMed=8383623; RA Uemura T., Shiomi K., Togashi S., Takeichi M.; RT "Mutation of twins encoding a regulator of protein phosphatase 2A RT leads to pattern duplication in Drosophila imaginal discs."; RL Genes Dev. 7:429-440(1993). RN [3] RP SEQUENCE FROM N.A. (LONG ISOFORM). RC STRAIN=BERKELEY; RX MEDLINE=20196006; PubMed=10731132; RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., RA Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., RA Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., RA Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., RA Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., RA Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., RA Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., RA Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., RA Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., RA de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., RA Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., RA Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., RA Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., RA Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., RA Harris N.L., Harvey D., Heiman T.J., Hernandez J.R., Houck J., RA Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., RA Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., RA Kimmel B.E., Kodira C.D., Kraft C., Kravitz S., Kulp D., Lai Z., RA Lasko P., Lei Y., Levitsky A.A., Li J., Li Z., Liang Y., Lin X., RA Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., RA Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., RA Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., RA Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., RA Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., RA Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., RA Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T., RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., RA Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., RA Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., RA Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., RA Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., RA Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S., Zhu X., Smith H.O., RA Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.; RT "The genome sequence of Drosophila melanogaster."; RL Science 287:2185-2195(2000). CC -!- FUNCTION: COULD PERFORM A SUBSTRATE RECOGNITION FUNCTION OR CC COULD BE RESPONSIBLE FOR TARGETING THE ENZYME COMPLEX TO THE CC APPROPRIATE SUBCELLULAR COMPARTMENT. CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA REGULATORY SUBUNIT (PR65) (SUBUNIT A). THE CORE COMPLEX CC ASSOCIATES WITH A THIRD, VARIABLE SUBUNIT (SUBUNIT B), WHICH CC CONFERS DISTINCT PROPERTIES TO THE HOLOENZYME. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; A LONG FORM (SHOWN HERE) AND CC A SHORT FORM; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: IT IS UNCERTAIN WHETHER MET-1, MET-18, MET-33 OR MET-44 CC IS THE INITIATOR. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D13004; BAA02367.1; -. DR EMBL; L07581; AAA99870.1; -. DR EMBL; L07583; AAA99871.1; -. DR EMBL; L07585; -; NOT_ANNOTATED_CDS. DR EMBL; L07586; AAB00371.1; -. DR EMBL; L12544; AAB00371.1; JOINED. DR EMBL; L07586; AAB00372.1; -. DR EMBL; L12544; AAB00372.1; JOINED. DR EMBL; AE003685; AAF54498.1; -. DR PIR; A45778; A45778. DR PIR; B45778; B45778. DR PIR; A46300; A46300. DR FlyBase; FBgn0004889; tws. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Alternative splicing. FT VARSPLIC 1 56 MISSING (IN SHORT ISOFORM). FT VARSPLIC 57 59 PAS -> MAG (IN SHORT ISOFORM). FT CONFLICT 211 211 K -> M (IN REF. 1; AAA99871). SQ SEQUENCE 499 AA; 56966 MW; D871A7E3058B7286 CRC64; MGRWGRQSPV LEPPDPQMQT TPPPPTLPPR TFMRQSSITK IGNMLNTAIN INGAKKPASN GEASWCFSQI KGALDDDVTD ADIISCVEFN HDGELLATGD KGGRVVIFQR DPASKAANPR RGEYNVYSTF QSHEPEFDYL KSLEIEEKIN KIRWLQQKNP VHFLLSTNDK TVKLWKVSER DKSFGGYNTK EENGLIRDPQ NVTALRVPSV KQIPLLVEAS PRRTFANAHT YHINSISVNS DQETFLSADD LRINLWHLEV VNQSYNIVDI KPTNMEELTE VITAAEFHPT ECNVFVYSSS KGTIRLCDMR SAALCDRHSK QFEEPENPTN RSFFSEIISS ISDVKLSNSG RYMISRDYLS IKVWDLHMET KPIETYPVHE YLRAKLCSLY ENDCIFDKFE CCWNGKDSSI MTGSYNNFFR VFDRNSKKDV TLEASRDIIK PKTVLKPRKV CTGGKRKKDE ISVDCLDFNK KILHTAWHPE ENIIAVAATN NLFIFQDKF // ID 2ABA_HUMAN STANDARD; PRT; 447 AA. AC Q00007; P50409; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform). GN PPP2R2A. OS Homo sapiens (Human), and OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606, 9986; RN [1] RP SEQUENCE FROM N.A. RC SPECIES=Human; TISSUE=Lung fibroblast; RX MEDLINE=91198016; PubMed=1849734; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., Goris J., RA Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase RT 2A: evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). RN [2] RP SEQUENCE FROM N.A. RC SPECIES=Rabbit; STRAIN=NEW ZEALAND WHITE; TISSUE=Skeletal muscle; RA Depaoli-Roach A.A.; RL Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: IN ALL TISSUES EXAMINED. CC -!- PTM: THE N-TERMINUS IS BLOCKED. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64929; AAA36490.1; -. DR EMBL; U09356; AAA18497.1; -. DR PIR; A38351; A38351. DR MIM; 604941; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 447 AA; 51692 MW; F4D407FF7ADA4ED6 CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKI WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_PIG STANDARD; PRT; 426 AA. AC Q29090; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform) (Fragment). GN PPP2R2A. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34932; CAA84404.1; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 426 AA; 49613 MW; 3AAD7EB338B03534 CRC64; DDDVAEADII STVEFNHSGE LLATGDKGGR VVIFQQEQEN KIQSHSRGEY NVYSTFQSHE PEFDYLKSLE IEEKINKIRW LPQKNAAQFL LSTNDKTIKL WKISERDKRP EGYNLKEEDG RYRDPTTVTT LRVPVFRPMD LMVEASPRRI FANAHTYHIN SISINSDYET YLSADDLRIN LWHLEITDRS FNIVDIKPAN MEELTEVITA AEFHPNSCNT FVYSSSKGTI RLCDMRASAL CDRHSKLFEE PEDPSNRSFF SEIISSISDV KFSHSGRYMM TRDYLSVKIW DLNMENRPVE TYQVHEYLRS KLCSLYENDC IFDKFECCWN GSDSVVMTGS YNNFFRMFDR NTKRDITLEA SRENNKPRTV LKPRKVCASG KRKKDEISVD SLDFNKKILH TAWHPKENII AVATTNNLYI FQDKVN // ID 2ABA_RAT STANDARD; PRT; 447 AA. AC P36876; P36878; O35512; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE alpha isoform (PP2A, subunit B, B-alpha isoform) (PP2A, subunit B, DE B55-alpha isoform) (PP2A, subunit B, PR55-alpha isoform) (PP2A, DE subunit B, R2-alpha isoform) (PP2A, subunit B, BRA isoform). GN PPP2R2A. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92114192; PubMed=1370560; RA Pallas D.C., Weller W., Jaspers S., Miller T.B. Jr., Lane W.S., RA Roberts T.M.; RT "The third subunit of protein phosphatase 2A (PP2A), a 55-kilodalton RT protein which is apparently substituted for by T antigens in RT complexes with the 36- and 63-kilodalton PP2A subunits, bears little RT resemblance to T antigens."; RL J. Virol. 66:886-893(1992). RN [2] RP SEQUENCE OF 80-272 FROM N.A. RC STRAIN=FISCHER 344; RX MEDLINE=93279382; PubMed=8389301; RA Hatano Y., Shima H., Haneji T., Miura A.B., Sugimura T., Nagao M.; RT "Expression of PP2A B regulatory subunit beta isotype in rat RT testis."; RL FEBS Lett. 324:71-75(1993). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M83298; AAA41910.1; -. DR EMBL; M83297; AAA41909.1; -. DR EMBL; D14419; BAA21904.1; -. DR PIR; A41805; A41805. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. FT VARIANT 60 60 E -> ESFKVHAALREASNLSMQ. FT CONFLICT 105 105 K -> E (IN REF. 1; AAA41909). FT CONFLICT 105 105 K -> R (IN REF. 2). FT CONFLICT 213 213 N -> S (IN REF. 2). FT CONFLICT 222 222 M -> V (IN REF. 2). SQ SEQUENCE 447 AA; 51678 MW; 180AC837D9DA4ECE CRC64; MAGAGGGNDI QWCFSQVKGA VDDDVAEADI ISTVEFNHSG ELLATGDKGG RVVIFQQEQE NKIQSHSRGE YNVYSTFQSH EPEFDYLKSL EIEEKINKIR WLPQKNAAQF LLSTNDKTIK LWKISERDKR PEGYNLKEED GRYRDPTTVT TLRVPVFRPM DLMVEASPRR IFANAHTYHI NSISINSDYE TYLSADDLRI NLWHLEITDR SFNIVDIKPA NMEELTEVIT AAEFHPNSCN TFVYSSSKGT IRLCDMRASA LCDRHSKLFE EPEDPSNRSF FSEIISSISD VKFSHSGRYM MTRDYLSVKV WDLNMENRPV ETYQVHEYLR SKLCSLYEND CIFDKFECCW NGSDSVVMTG SYNNFFRMFD RNTKRDITLE ASRENNKPRT VLKPRKVCAS GKRKKDEISV DSLDFNKKIL HTAWHPKENI IAVATTNNLY IFQDKVN // ID 2ABA_SCHPO STANDARD; PRT; 463 AA. AC Q12702; Q9UTD2; DT 15-JUL-1999 (Rel. 38, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Protein phosphatase PP2A regulatory subunit B (PR55) (Protein DE phosphatase 2A 55 kDa regulatory subunit). GN PAB1 OR SPAC227.07C. OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP SEQUENCE FROM N.A. RA Kinoshita K., Nemoto T., Nabeshima K., Kondoh H., Niwa H., RA Yanagida M.; RT "Fission yeast protein phosphatase 2A (PP2A) regulatory subunits RT affect cell morphogenesis, cell wall synthesis, osmoregulation and RT cytokinesis."; RL Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP SEQUENCE FROM N.A. RC STRAIN=972; RA Zimmermann W., Wambutt R., McDougall R.C., Rajandream M.A., RA Barrell B.G.; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: PHOSPHATASE 2A AFFECTS A VARIETY OF BIOLOGICAL PROCESSES CC IN THE CELL SUCH AS TRANSCRIPTION, CELL CYCLE PROGRESSION AND CC CELLULAR MORPHOGENESIS, AND PROVIDES AN INITIAL IDENTIFICATION OF CC CRITICAL SUBSTRATES FOR THIS PHOSPHATASE. THE REGULATORY SUBUNIT CC MAY DIRECT THE CATALYTIC SUBUNIT TO DISTINCT, ALBEIT OVERLAPPING, CC SUBSETS OF SUBSTRATES (BY SIMILARITY). CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA (PR65) (SUBUNIT A) AND A 55 KDA (PR55) (SUBUNIT B) CC REGULATORY SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D63915; BAA09945.1; -. DR EMBL; AL133156; CAB61456.1; -. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. FT CONFLICT 126 126 K -> R (IN REF. 1). FT CONFLICT 145 145 L -> V (IN REF. 1). SQ SEQUENCE 463 AA; 52795 MW; 43B289222A2D8CC3 CRC64; MDDIEDSLDQ WKFAQCFGDK GDVEDITEAD IISAVEFDHT GDYLATGDKG GRVVLFERNH SKKGCEYKFF TEFQSHEPEF DYLKSLEIEE KINKIRWCKR TNRAHFLLST NDKTIKLWKL YEKNLKVVAE NNLSDSFHSP MQGPLTTPSQ LRLPRLNHHD MIIAAYPRRV YANAHAYHIN SISVNSDAET YISADDLRIN LWNLSISDHS FNIVDIKPEN MEELTEVITS AEFHPINCNH LMYSSSKGNI KLLDLRQSAL CDNPCKLFED QEDQDSKSFF SEIISSISDV KFSQNGRYIL SRDYLTLKIW DVNMEKAPVK TIPLHDVLRS KLCDLYENDC IFDKFECTFS GDDKHVLSGS YSNNFGIYPT DSSLPGDRGQ IVLQADKAAF RARKSAANNV PKLNAVKNND WRSQPQAAMG SASVGLDPDN LDYNKKILHA SWHPFEDSVA IAATNNLFVF SKL // ID 2ABA_YEAST STANDARD; PRT; 526 AA. AC Q00362; DT 01-APR-1993 (Rel. 25, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 15-JUL-1999 (Rel. 38, Last annotation update) DE Protein phosphatase PP2A regulatory subunit B (PR55) (Cell division DE control protein 55). GN CDC55 OR YGL190C OR G1345. OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=92017858; PubMed=1656238; RA Healy A.M., Zolnierowicz S., Stapleton A.E., Goebl M., RA Depaoli-Roach A.A., Pringle J.R.; RT "CDC55, a Saccharomyces cerevisiae gene involved in cellular RT morphogenesis: identification, characterization, and homology to the RT B subunit of mammalian type 2A protein phosphatase."; RL Mol. Cell. Biol. 11:5767-5780(1991). RN [2] RP SEQUENCE FROM N.A. RC STRAIN=S288C / FY1679; RX MEDLINE=97197971; PubMed=9046087; RA Coglievina M., Klima R., Bertani I., Delneri D., Zaccaria P., RA Bruschi C.V.; RT "Sequencing of a 40.5 kb fragment located on the left arm of RT chromosome VII from Saccharomyces cerevisiae."; RL Yeast 13:55-64(1997). CC -!- FUNCTION: PHOSPHATASE 2A AFFECTS A VARIETY OF BIOLOGICAL PROCESSES CC IN THE CELL SUCH AS TRANSCRIPTION, CELL CYCLE PROGRESSION AND CC CELLULAR MORPHOGENESIS, AND PROVIDES AN INITIAL IDENTIFICATION OF CC CRITICAL SUBSTRATES FOR THIS PHOSPHATASE. THE REGULATORY SUBUNIT CC MAY DIRECT THE CATALYTIC SUBUNIT TO DISTINCT, ALBEIT OVERLAPPING, CC SUBSETS OF SUBSTRATES. CC -!- SUBUNIT: PP2A EXISTS IN SEVERAL TRIMERIC FORMS, ALL OF WHICH CC CONSIST OF A CORE COMPOSED OF A CATALYTIC SUBUNIT ASSOCIATED WITH CC A 65 KDA (PR65) (SUBUNIT A) AND A 55 KDA (PR55) (SUBUNIT B) CC REGULATORY SUBUNIT. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M72716; AAA34482.1; -. DR EMBL; Z72712; CAA96902.1; -. DR EMBL; X91837; CAA62954.1; -. DR EMBL; X91489; CAA62785.1; -. DR PIR; A41698; A41698. DR SGD; S0003158; CDC55. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Cell cycle. FT DOMAIN 416 419 POLY-SER. FT CONFLICT 500 500 I -> N (IN REF. 1). SQ SEQUENCE 526 AA; 59662 MW; 6DA12C2805FA6A82 CRC64; MAQNNFDFKF SQCFGDKADI VVTEADLITA VEFDYTGNYL ATGDKGGRVV LFERSNSRHC EYKFLTEFQS HDAEFDYLKS LEIEEKINEI KWLRPTQRSH FLLSTNDKTI KLWKVYEKNI KLVSQNNLTE GVTFAKKGKP DNHNSRGGSV RAVLSLQSLK LPQLSQHDKI IAATPKRIYS NAHTYHINSI SLNSDQETFL SADDLRINLW NLDIPDQSFN IVDIKPTNME ELTEVITSAE FHPQECNLFM YSSSKGTIKL CDMRQNSLCD NKTKTFEEYL DPINHNFFTE ITSSISDIKF SPNGRYIASR DYLTVKIWDV NMDNKPLKTI NIHEQLKERL SDTYENDAIF DKFEVNFSGD SSSVMTGSYN NNFMIYPNVV TSGDNDNGIV KTFDEHNAPN SNSNKNIHNS IQNKDSSSSG NSHKRRSNGR NTGMVGSSNS SRSSIAGGEG ANSEDSGTEM NEIVLQADKT AFRNKRYGSL AQRSARNKDW GDDIDFKKNI LHFSWHPREN SIAVAATNNL FIFSAL // ID 2ABB_HUMAN STANDARD; PRT; 443 AA. AC Q00005; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN PPP2R2B. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Fetal brain; RX MEDLINE=91198016; PubMed=1849734; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., RA Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase RT 2A: evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64930; AAA36493.1; -. DR PIR; B38351; B38351. DR MIM; 604325; -. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_PIG STANDARD; PRT; 443 AA. AC P54614; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform). GN PPP2R2B. OS Sus scrofa (Pig). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Suina; Suidae; Sus. OX NCBI_TaxID=9823; RN [1] RP SEQUENCE FROM N.A. RA Mayer-Jaekel R.E.; RL Thesis (1992), Friedrich Miescher Institut / Basel, Switzerland. CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; Z34933; CAA84405.1; -. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 4. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 443 AA; 51459 MW; F8562FC696719F41 CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISAV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI ADIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASACVTG TPNFLKEPED PSNRSFSLKL SSSISDVKFS QQWEDIMTRD YLTVKVWDLN MENRPIETYQ VHNYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_RABIT STANDARD; PRT; 413 AA. AC Q00006; DT 01-APR-1993 (Rel. 25, Created) DT 01-APR-1993 (Rel. 25, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform) (Fragment). GN PPP2R2B. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Fetal brain; RX MEDLINE=91198016; PubMed=1849734; RA Mayer R.E., Hendrix P., Cron P., Matthies R., Stone S.R., RA Goris J., Merlevede W., Hofsteenge J., Hemmings B.A.; RT "Structure of the 55-kDa regulatory subunit of protein phosphatase RT 2A: evidence for a neuronal-specific isoform."; RL Biochemistry 30:3589-3597(1991). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; M64931; AAA31458.1; -. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 5. DR SMART; SM00320; WD40; 2. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. FT NON_TER 1 1 SQ SEQUENCE 413 AA; 48243 MW; 49237B7817EB8FE2 CRC64; EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABB_RAT STANDARD; PRT; 443 AA. AC P36877; DT 01-JUN-1994 (Rel. 29, Created) DT 01-NOV-1997 (Rel. 35, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE beta isoform (PP2A, subunit B, B-beta isoform) (PP2A, subunit B, B55- DE beta isoform) (PP2A, subunit B, PR55-beta isoform) (PP2A, subunit B, DE R2-beta isoform) (PP2A, subunit B, BRB isoform). GN PPP2R2B. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Brain; RX MEDLINE=95331316; PubMed=7607250; RA Akiyama N., Shima H., Hatano Y., Osawa Y., Sugimura T., Nagao M.; RT "cDNA cloning of BR gamma, a novel brain-specific isoform of the B RT regulatory subunit of type-2A protein phosphatase."; RL Eur. J. Biochem. 230:766-772(1995). RN [2] RP SEQUENCE OF 8-177 FROM N.A. RC TISSUE=Testis; RX MEDLINE=93279382; PubMed=8389301; RA Hatano Y., Shima H., Haneji T., Miura A.B., Sugimura T., Nagao M.; RT "Expression of PP2A B regulatory subunit beta isotype in rat testis."; RL FEBS Lett. 324:71-75(1993). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: BRAIN AND TESTIS. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D38260; BAA07412.1; -. DR EMBL; D14421; BAA03313.1; -. DR PIR; S33257; S33257. DR InterPro; IPR000009; PP2A_PR55. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 3. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 443 AA; 51668 MW; 0089EF6E8ED53082 CRC64; MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD YLTAKVWDLN MENRPVETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW HPSENIIAVA ATNNLYIFQD KVN // ID 2ABD_RAT STANDARD; PRT; 453 AA. AC P56932; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 kDa regulatory subunit B, DE delta isoform (PP2A, subunit B, B-delta isoform) (PP2A, subunit B, DE B55-delta isoform) (PP2A, subunit B, PR55-delta isoform) (PP2A, DE subunit B, R2-delta isoform). GN PPP2R2D. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Brain; RX MEDLINE=20026081; PubMed=10556517; RA Strack S., Chang D., Zaucha J.A., Colbran R.J., Wadzinski B.E.; RT "Cloning and characterization of B delta, a novel regulatory subunit RT of protein phosphatase 2A."; RL FEBS Lett. 460:462-466(1999). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SUBCELLULAR LOCATION: CYTOPLASMIC. CC -!- TISSUE SPECIFICITY: WIDELY EXPRESSED WITH HIGH LEVELS IN BRAIN, CC HEART, PLACENTA, SKELETAL MUSCLE, TESTIS, THYMUS AND SPLEEN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF180350; AAF08536.1; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 6. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 2. KW Multigene family. FT DOMAIN 3 8 POLY-GLY. SQ SEQUENCE 453 AA; 51982 MW; 733E80A93A5BC2BB CRC64; MAGAGGGGCP TGGNDFQWCF SQVKGAVDED VAEADIISTV EFNYSGDLLA TGDKGGRVVI FQREQENKGR AHSRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAHFLLST NDKTIKLWKI SERDKRAEGY NLKDEDGRLR DPFRITALRV PILKPMDLMV EASPRRIFAN AHTYHINSIS VNSDHETYLS ADDLRINLWH LEITDRSFNI VDIKPANMEE LTEVITAAEF HPHQCNVFVY SSSKGTIRLC DMRSSALCDR HAKFFEEPED PSSRSFFSEI ISSISDVKFS HSGRYMMTRD YLSVKVWDLN MEGRPVETHH VHEYLRSKLC SLYENDCIFD KFECCWNGSD SAIMTGSYNN FFRMFDRNTR RDVTLEASRE NSKPRASLKP RKVCSGGKRK KDEISVDSLD FNKKILHTAW HPMESIIAVA ATNNLYIFQD KIN // ID 2ABG_HUMAN STANDARD; PRT; 447 AA. AC Q9Y2T4; Q9H3G7; DT 30-MAY-2000 (Rel. 39, Created) DT 16-OCT-2001 (Rel. 40, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform) (IMYPNO1). GN PPP2R2C. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=20039617; PubMed=10574460; RA Torres R., Ide S.E., Dehejia A., Baras A., Polymeropoulos M.H.; RT "Genomic structure and localization of the Homo sapiens phosphatase 2A RT BR gamma regulatory subunit."; RL DNA Res. 6:323-327(1999). RN [2] RP SEQUENCE FROM N.A. RX MEDLINE=20399570; PubMed=10945473; RA Hu P., Yu L., Zhang M., Zheng L., Zhao Y., Fu Q., Zhao S.; RT "Molecular cloning and mapping of the brain-abundant B1gamma subunit RT of protein phosphatase 2A, PPP2R2C, to human chromosome 4p16."; RL Genomics 67:83-86(2000). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -!- CAUTION: THE EMBL ENTRY FOR REF.1 IS NOT COMPLETE, THE PAPER SHOWS CC THE REST OF THE SEQUENCE (RESIDUES 1 TO 23). CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; AF096160; AAD20987.1; -. DR EMBL; AF096153; AAD20987.1; JOINED. DR EMBL; AF096154; AAD20987.1; JOINED. DR EMBL; AF096155; AAD20987.1; JOINED. DR EMBL; AF096156; AAD20987.1; JOINED. DR EMBL; AF096157; AAD20987.1; JOINED. DR EMBL; AF096158; AAD20987.1; JOINED. DR EMBL; AF096159; AAD20987.1; JOINED. DR EMBL; AF086924; AAG39636.1; -. DR MIM; 605997; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 4. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 5. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. FT CONFLICT 24 24 MISSING (IN REF. 1). FT CONFLICT 66 66 D -> E (IN REF. 1). FT CONFLICT 253 253 P -> R (IN REF. 1). FT CONFLICT 293 293 D -> G (IN REF. 1). SQ SEQUENCE 447 AA; 51500 MW; 76FFE2A76410FD24 CRC64; MGEDTDTRKI NHSFLRDHSY VTEADIISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGDYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMPAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSDRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYENDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ABG_RABIT STANDARD; PRT; 447 AA. AC P50410; DT 01-OCT-1996 (Rel. 34, Created) DT 01-OCT-1996 (Rel. 34, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform). GN PPP2R2C. OS Oryctolagus cuniculus (Rabbit). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Lagomorpha; Leporidae; Oryctolagus. OX NCBI_TaxID=9986; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=NEW ZEALAND WHITE; TISSUE=Skeletal muscle, and Brain; RX MEDLINE=95001896; PubMed=7918404; RA Zolnierowicz S., Csortos C., Bondor J., Verin A., Mumby M.C., RA Depaoli-Roach A.A.; RT "Diversity in the regulatory B-subunits of protein phosphatase 2A: RT identification of a novel isoform highly expressed in brain."; RL Biochemistry 33:11858-11867(1994). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; U09355; AAA58956.1; -. DR EMBL; U09354; AAA58955.1; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 2. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 447 AA; 51468 MW; C6847C2381E41A7A CRC64; MGEDTDTRKI NHSFLRDHSY VTEADIISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAVTDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYENDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDVH // ID 2ABG_RAT STANDARD; PRT; 447 AA. AC P97888; DT 15-JUL-1999 (Rel. 38, Created) DT 15-JUL-1999 (Rel. 38, Last sequence update) DT 30-MAY-2000 (Rel. 39, Last annotation update) DE Serine/threonine protein phosphatase 2A, 55 KDA regulatory subunit B, DE gamma isoform (PP2A, subunit B, B-gamma isoform) (PP2A, subunit B, DE B55-gamma isoform) (PP2A, subunit B, PR55-gamma isoform) (PP2A, DE subunit B, R2-gamma isoform) (PP2A, subunit B, BRGAMMA isoform). GN PPP2R2C. OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Rodentia; Sciurognathi; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=SPRAGUE-DAWLEY; TISSUE=Brain; RX MEDLINE=95331316; PubMed=7607250; RA Akiyama N., Shima H., Hatano Y., Osawa Y., Sugimura T., Nagao M.; RT "cDNA cloning of BR gamma, a novel brain-specific isoform of the B RT regulatory subunit of type-2A protein phosphatase."; RL Eur. J. Biochem. 230:766-772(1995). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- TISSUE SPECIFICITY: HIGHLY EXPRESSED IN BRAIN. CC -!- SIMILARITY: BELONGS TO THE PHOSPHATASE 2A REGULATORY SUBUNIT B CC FAMILY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; D38261; BAA07413.1; -. DR InterPro; IPR000009; PP2A_PR55. DR InterPro; IPR001680; WD40. DR Pfam; PF00400; WD40; 5. DR PRINTS; PR00600; PP2APR55. DR SMART; SM00320; WD40; 2. DR PROSITE; PS01024; PR55_1; 1. DR PROSITE; PS01025; PR55_2; 1. KW Multigene family. SQ SEQUENCE 447 AA; 51474 MW; DE16E4EFC775F3C5 CRC64; MGEDTDTRKI NHSFLRDHSY VTEADVISTV EFNHTGELLA TGDKGGRVVI FQREPESKNA PHSQGEYDVY STFQSHEPEF DYLKSLEIEE KINKIKWLPQ QNAAHSLLST NDKTIKLWKI TERDKRPEGY NLKDEEGKLK DLSTVTSLQV PVLKPMDLMV EVSPRRIFAN GHTYHINSIS VNSDCETYMS ADDLRINLWH LAITDRSFNI VDIKPANMED LTEVITASEF HPHHCNLFVY SSSKGSLRLC DMRAAALCDK HSKLFEEPED PSNRSFFSEI ISSVSDVKFS HSGRYMLTRD YLTVKVWDLN MEARPIETYQ VHDYLRSKLC SLYESDCIFD KFECAWNGSD SVIMTGAYNN FFRMFDRNTK RDVTLEASRE SSKPRAVLKP RRVCVGGKRR RDDISVDSLD FTKKILHTAW HPAENIIAIA ATNNLYIFQD KVNSDMH // ID 2ACA_HUMAN STANDARD; PRT; 1150 AA. AC Q06190; Q06189; DT 01-JUN-1994 (Rel. 29, Created) DT 01-JUN-1994 (Rel. 29, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 72/130 KDA regulatory subunit DE B (PP2A, subunit B, B''-PR72/PR130) (PP2A, subunit B, B72/B130 DE isoforms) (PP2A, subunit B, PR72/PR130 isoforms) (PP2A, subunit B, R3 DE isoform). GN PPP2R3. OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A., PARTIAL SEQUENCE, AND ALTERNATIVE SPLICING. RC TISSUE=Fetal brain; RX MEDLINE=93315512; PubMed=8392071; RA Hendrix P., Mayer-Jaekel R.E., Cron P., Goris J., Hofsteenge J., RA Merlevede W., Hemmings B.A.; RT "Structure and expression of a 72-kDa regulatory subunit of protein RT phosphatase 2A. Evidence for different size forms produced by RT alternative splicing."; RL J. Biol. Chem. 268:15267-15276(1993). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR65 OR SUBUNIT A), THAT ASSOCIATES CC WITH A VARIETY OF REGULATORY SUBUNITS. PROTEINS THAT ASSOCIATE CC WITH THE CORE DIMER INCLUDE THREE FAMILIES OF REGULATORY SUBUNITS CC B (THE R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 AND R5/B'/B56 CC FAMILIES), THE 48 KDA VARIABLE REGULATORY SUBUNIT, VIRAL PROTEINS, CC AND CELL SIGNALING MOLECULES. CC -!- ALTERNATIVE PRODUCTS: 2 ISOFORMS; PR130/130 KDA (SHOWN HERE) AND CC PR72/72; ARE PRODUCED BY ALTERNATIVE SPLICING. CC -!- TISSUE SPECIFICITY: EXPRESSED IN HEART, BRAIN, PLACENTA, LUNG, CC MUSCLE AND KIDNEY. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- DR EMBL; L07590; AAB02613.1; -. DR EMBL; L12146; AAB02614.1; -. DR PIR; A47114; A47114. DR PIR; B47114; B47114. DR MIM; 604944; -. DR Pfam; PF00036; efhand; 1. KW Multigene family; Alternative splicing. FT DOMAIN 670 695 PRO-RICH. FT VARSPLIC 1 621 MISSING (IN ISOFORM PR72). FT VARSPLIC 622 665 MQILQETLTTSSQANLSVCRSPVGDKAKDTTSAVLIQQTPE FT VIK -> MMIKETSLRRDPDLRGELAFLARGCDFVLPSRFK FT KRLKSFQQTQ (IN ISOFORM PR72). SQ SEQUENCE 1150 AA; 130277 MW; 97A31BA4206518A3 CRC64; MAATYRLVVS TVNHYSSVVI DRRFEQAIHY CTGTCHTFTH GIDCIVVHHS VCADLLHIPV SQFKDADLNS MFLPHENGLS SAEGDYPQQA FTGIPRVKRG STFQNTYNLK DIAGEAISFA SGKIKEFSFE KLKNSNHAAY RKGRKVKSDS FNRRSVDLDL LCGHYNNDGN APSFGLLRSS SVEEKPLSHR NSLDTNLTSM FLQNFSEEDL VTQILEKHKI DNFSSGTDIK MCLDILLKCS EDLKKCTDII KQCIKKKSGS SISEGSGNDT ISSSETVYMN VMTRLASYLK KLPFEFMQSG NNEALDLTEL ISNMPSLQLT PFSPVFGTEQ PPKYEDVVQL SASDSGRFQT IELQNDKPNS RKMDTVQSIP NNSTNSLYNL EVNDPRTLKA VQVQSQSLTM NPLENVSSDD LMETLYIEEE SDGKKALDKG QKTENGPSHE LLKVNEHRAE FPEHATHLKK CPTPMQNEIG KIFEKSFVNL PKEDCKSKVS KFEEGDQRDF TNSSSQEEID KLLMDLESFS QKMETSLREP LAKGKNSNFL NSHSQLTGQT LVDLEPKSKV SSPIEKVSPS CLTRIIETNG HKIEEEDRAL LLRILESIED FAQELVECKS SRGSLSQEKE MMQILQETLT TSSQANLSVC RSPVGDKAKD TTSAVLIQQT PEVIKIQNKP EKKPGTPLPP PATSPSSPRP LSPVPHVNNV VNAPLSINIP RFYFPEGLPD TCSNHEQTLS RIETAFMDIE EQKADIYEMG KIAKVCGCPL YWKAPMFRAA GGEKTGFVTA QSFIAMWRKL LNNHHDDASK FICLLAKPNC SSLEQEDFIP LLQDVVDTHP GLTFLKDAPE FHSRYITTVI QRIFYTVNRS WSGKITSTEI RKSNFLQTLA LLEEEEDINQ ITDYFSYEHF YVIYCKFWEL DTDHDLYISQ ADLSRYNDQA SSSRIIERIF SGAVTRGKTI QKEGRMSYAD FVWFLISEED KRNPTSIEYW FRCMDVDGDG VLSMYELEYF YEEQCERMEA MGIEPLPFHD LLCQMLDLVK PAVDGKITLR DLKRCRMAHI FYDTFFNLEK YLDHEQRDPF AVQKDVENDG PEPSDWDRFA AEEYETLVAE ESAQAQFQEG FEDYETDEPA SPSEFGNKSN KILSASLPEK CGKLQSVDEE // ID 2ACC_HUMAN STANDARD; PRT; 414 AA. AC Q9Y5P8; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Serine/threonine protein phosphatase 2A, 48 KDA regulatory subunit B DE (PP2A, subunit B, PR48 isoform). OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Primates; Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP SEQUENCE FROM N.A. RC TISSUE=Placenta; RX MEDLINE=20094981; PubMed=10629059; RA Yan Z., Fedorov S.A., Mumby M.C., Williams R.S.; RT "PR48, a novel regulatory subunit of protein phosphatase 2A, interacts RT with cdc6 and modulates DNA replication in human cells."; RL Mol. Cell. Biol. 20:1021-1029(2000). CC -!- FUNCTION: THE B REGULATORY SUBUNIT MIGHT MODULATE SUBSTRATE CC SELECTIVITY AND CATALYTIC ACTIVITY, AND ALSO MIGHT DIRECT THE CC LOCALIZATION OF THE CATALYTIC ENZYME TO A PARTICULAR SUBCELLULAR CC COMPARTMENT. INTERACTS WITH AMINO-TERMINAL REGION (AA 2 TO 181) OF CC CDC6. CC -!- SUBUNIT: PP2A CONSISTS OF A COMMON HETERODIMERIC CORE ENZYME, CC COMPOSED OF A 36 KDA CATALYTIC SUBUNIT (SUBUNIT C) AND A 65 KDA CC CONSTANT REGULATORY SUBUNIT (PR6