f2cc86e3506c2d5fefe00dbe85e7f05f0f33f43f jcasper Wed Mar 6 11:33:33 2024 -0800 Updates for new uniProt import, refs #30476 diff --git src/hg/protein/spToDb/input/test1 src/hg/protein/spToDb/input/test1 index e02937e..9609796 100644 --- src/hg/protein/spToDb/input/test1 +++ src/hg/protein/spToDb/input/test1 @@ -1,1005 +1,965 @@ 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; OH NCBI_TaxID=9913; OH NCBI_TaxID=9901; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Muguga; RX MEDLINE=90158697; PubMed=1689460; DOI=10.1016/0166-6851(90)90007-9; RA Iams K.P., Young J.R., Nene V., Desai J., Webster P., Ole-Moiyoi O.K., RA 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. DR TIGRFAMs; TIGR01870; cas_TM1810; 1. PE 3: Inferred from homology; KW Antigen; Repeat; Sporozoite. 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; asterids; OC lamiids; 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; DOI=10.1104/pp.101.4.1413; 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 PIR; S26409; S26409. DR InterPro; IPR003612; AAI. DR Pfam; PF00234; Tryp_alpha_amyl; 1. DR SMART; SM00499; AAI; 1. PE 2: Evidence at transcript level; 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; rosids; 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 plant defensin 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; P81929; 1JKZ. DR InterPro; IPR008176; Gamma-thionin. DR InterPro; IPR003614; Knot1. DR Pfam; PF00304; Gamma-thionin; 1. DR ProDom; PD002594; G_Purothionin; 1. DR SMART; SM00505; Knot1; 1. DR PROSITE; PS00940; GAMMA_THIONIN; 1. PE 2: Evidence at transcript level; 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 29-MAR-2004 (Rel. 43, 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; DOI=10.1016/0166-6851(87)90007-7; 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. PE 1: Evidence at protein level; KW Antigen; Malaria; Repeat. FT NON_TER 1 1 FT DOMAIN 132 296 13.5 X 12 AA approximate tandem repeats FT of E-E-T-Q-K-T-V-E-P-E-Q-T. FT REPEAT 132 143 1 (approximate). FT REPEAT 144 155 2 (approximate). FT REPEAT 156 167 3. FT REPEAT 168 179 4 (approximate). FT REPEAT 180 191 5. FT REPEAT 192 203 6 (approximate). FT REPEAT 204 215 7. FT REPEAT 216 227 8. FT REPEAT 228 239 9. FT REPEAT 240 251 10. FT REPEAT 252 263 11. FT REPEAT 264 275 12. FT REPEAT 276 287 13 (approximate). FT REPEAT 288 293 14 (incomplete). 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 05-JUL-2004 (Rel. 44, Last annotation update) DE 11S globulin seed storage protein G3 precursor (Helianthinin G3) DE [Contains: 11S globulin seed storage protein G3 acidic chain; 11S DE globulin seed storage protein G3 basic chain]. GN Name=HAG3; OS Helianthus annuus (Common sunflower). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; asterids; OC campanulids; Asterales; Asteraceae; Asteroideae; Heliantheae; OC Helianthus. OX NCBI_TaxID=4232; RN [1] RP SEQUENCE FROM N.A. RX MEDLINE=89232734; PubMed=2469623; DOI=10.1016/0378-1119(88)90176-X; 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 -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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 HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR007113; Cupin_region. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. PE 1: Evidence at protein level; KW Multigene family; Seed storage protein; Signal. FT SIGNAL 1 20 FT CHAIN 21 305 11S globulin seed storage protein G3 FT acidic chain. FT CHAIN 306 493 11S globulin seed storage protein G3 FT 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 05-JUL-2004 (Rel. 44, Last annotation update) DE 11S globulin beta subunit precursor [Contains: 11S globulin gamma DE chain (11S globulin acidic chain); 11S globulin delta chain (11S DE globulin basic chain)]. OS Cucurbita maxima (Pumpkin) (Winter squash). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; 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 -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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 HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR007113; Cupin_region. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Pyrrolidone carboxylic acid; KW Seed storage protein; Signal. FT SIGNAL 1 21 FT CHAIN 22 480 11S globulin beta subunit. FT CHAIN 22 296 11S globulin gamma chain. FT CHAIN 297 480 11S globulin delta chain. 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 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 05-JUL-2004 (Rel. 44, Last annotation update) DE GTP-binding protein 128UP. GN Name=128up; Synonyms=GTP-bp; OS Drosophila melanogaster (Fruit fly). OC Eukaryota; Metazoa; Arthropoda; Hexapoda; Insecta; Pterygota; OC 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 of RT 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; S42582; S42582. DR HSSP; P20964; 1LNZ. DR IntAct; P32234; -. DR FlyBase; FBgn0010339; 128up. DR GO; GO:0005525; F:GTP binding; IDA. DR InterPro; IPR006074; GTP1/OBG_dom. DR InterPro; IPR006073; GTP1_OBG. DR InterPro; IPR006169; GTP1_OBG_sub. DR InterPro; IPR005225; Small_GTP. DR InterPro; IPR004095; TGS. DR Pfam; PF01018; GTP1_OBG; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00905; GTP1_OBG; 1. PE 3: Inferred from homology; 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 05-JUL-2004 (Rel. 44, Last annotation update) DE 12-alpha-hydroxysteroid dehydrogenase (EC 1.1.1.176) (Fragment). OS Clostridium sp. (strain C 48-50). OC Bacteria; Firmicutes; Clostridia; Clostridiales; 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: Catalyzes 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 -!- FUNCTION: Catalyzes the oxidation of the 12-alpha-hydroxyl group of bile acids, both in their free and conjugated form. Also acts on bile alcohols. +CC -!- CATALYTIC ACTIVITY: 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta- cholanate + NADP(+) = 3-alpha,7-alpha-dihydroxy-12-oxo-5-beta- cholanate + NADPH. CC -!- SUBUNIT: Homotetramer. -CC -!- MISCELLANEOUS: The thermostability of the enzyme is greatly -CC increased due to NADP binding. +CC -!- MISCELLANEOUS: The thermostability of the enzyme is greatly increased due to NADP binding. DR PIR; S14099; S14099. PE 3: Inferred from homology; KW Bile acid catabolism; Direct protein sequencing; NADP; Oxidoreductase. 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; rosids; 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 auxin- RT 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; -. DR PIR; S11850; S11850. DR InterPro; IPR008406; Auxin_repressed. DR Pfam; PF05564; Auxin_repressed; 1. PE 3: Inferred from homology; 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 05-JUL-2004 (Rel. 44, Last annotation update) DE 12 kDa protein (Fragment). OS Mycobacterium smegmatis. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium. OX NCBI_TaxID=1772; RN [1] RP SEQUENCE. RA Pahl A., Keller U.; RL Submitted (MAR-1995) to Swiss-Prot. PE 3: Inferred from homology; KW Direct protein sequencing. 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; Q9FFH7; DT 01-APR-1990 (Rel. 14, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE 12S seed storage protein CRA1 precursor [Contains: 12S seed storage DE protein CRA1 alpha chain (12S seed storage protein CRA1 acidic chain); DE 12S seed storage protein CRA1 beta chain (12S seed storage protein DE CRA1 basic chain)]. GN Name=CRA1; OrderedLocusNames=At5g44120; ORFNames=MLN1.4; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; 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 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). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP SEQUENCE OF 420-472 FROM N.A. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). 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 -!- ALTERNATIVE PRODUCTS: -CC Event=Alternative splicing; Named isoforms=1; -CC Comment=A number of isoforms are produced. According to EST -CC sequences; -CC Name=1; -CC IsoId=P15455-1; Sequence=Displayed; -CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) -CC family. +CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. +CC -!- ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=1; Comment=A number of isoforms are produced. According to EST sequences; Name=1; IsoId=P15455-1; Sequence=Displayed; +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AB005239; BAB10979.1; -. DR EMBL; AY070730; AAL50071.1; -. DR EMBL; Z17590; CAA79005.1; -. DR PIR; S08509; S08509. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. PE 3: Inferred from homology; KW Alternative splicing; Multigene family; Seed storage protein; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 282 12S seed storage protein CRA1 alpha chain FT (By similarity). FT CHAIN 283 472 12S seed storage protein CRA1 beta chain FT (By similarity). FT DISULFID 112 289 Interchain (alpha-beta) (Potential). FT CONFLICT 167 167 E -> Q (in Ref. 1). FT CONFLICT 356 356 V -> E (in Ref. 1). SQ SEQUENCE 472 AA; 52595 MW; 700B468E4D251994 CRC64; MARVSSLLSF CLTLLILFHG YAAQQGQQGQ QFPNECQLDQ LNALEPSHVL KSEAGRIEVW DHHAPQLRCS GVSFARYIIE SKGLYLPSFF NTAKLSFVAK GRGLMGKVIP GCAETFQDSS EFQPRFEGQG QSQRFRDMHQ KVEHIRSGDT IATTPGVAQW FYNDGQEPLV IVSVFDLASH QNQLDRNPRP FYLAGNNPQG QVWLQGREQQ PQKNIFNGFG PEVIAQALKI DLQTAQQLQN QDDNRGNIVR VQGPFGVIRP PLRGQRPQEE EEEEGRHGRH GNGLEETICS ARCTDNLDDP SRADVYKPQL GYISTLNSYD LPILRFIRLS ALRGSIRQNA MVLPQWNANA NAILYVTDGE AQIQIVNDNG NRVFDGQVSQ GQLIAVPQGF SVVKRATSNR FQWVEFKTNA NAQINTLAGR TSVLRGLPLE VITNGFQISP EEARRVKFNT LETTLTHSSG PASYGRPRVA AA // ID 12S2_ARATH STANDARD; PRT; 455 AA. AC P15456; Q9SAW0; DT 01-APR-1990 (Rel. 14, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE 12S seed storage protein CRB precursor [Contains: 12S seed storage DE protein CRB alpha chain (12S seed storage protein CRB acidic chain); DE 12S seed storage protein CRB beta chain (12S seed storage protein CRB DE basic chain)]. GN Name=CRB; OrderedLocusNames=At1g03880; ORFNames=F21M11.19; OS Arabidopsis thaliana (Mouse-ear cress). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; rosids; 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 FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=21016719; PubMed=11130712; DOI=10.1038/35048500; 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). RN [3] RP SEQUENCE FROM N.A. RC STRAIN=cv. Columbia; RX MEDLINE=22954850; PubMed=14593172; DOI=10.1126/science.1088305; RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., RA Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., RA Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G., RA Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., RA Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., RA Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., RA Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., RA Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., RA Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., RA Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., RA Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., RA Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.; RT "Empirical analysis of transcriptional activity in the Arabidopsis RT genome."; RL Science 302:842-846(2003). RN [4] RP SEQUENCE OF 240-360 FROM N.A. RC STRAIN=cv. Columbia; TISSUE=Green siliques; RX MEDLINE=94108489; PubMed=8281187; RX DOI=10.1046/j.1365-313X.1993.04061051.x; RA Hoefte H., Desprez T., Amselem J., Chiapello H., Rouze P., Caboche M., RA Moisan A., Jourjon M.-F., Charpenteau J.-L., Berthomieu P., RA Guerrier D., Giraudat J., Quigley F., Thomas F., Yu D.-Y., Mache R., RA Raynal M., Cooke R., Grellet F., Delseny M., Parmentier Y., RA de Marcillac G., Gigot C., Fleck J., Philipps G., Axelos M., RA Bardet C., Tremousaygue D., Lescure B.; RT "An inventory of 1152 expressed sequence tags obtained by partial RT sequencing of cDNAs from Arabidopsis thaliana."; RL Plant J. 4:1051-1061(1993). 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 -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AC003027; AAD10680.1; -. DR EMBL; AY093005; AAM13004.1; -. DR EMBL; Z17654; CAA79024.1; -. DR PIR; E86169; E86169. DR PIR; S08510; S08510. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR007113; Cupin_region. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. PE 3: Inferred from homology; KW Multigene family; Seed storage protein; Signal. FT SIGNAL 1 24 Potential. FT CHAIN 25 269 12S seed storage protein CRB alpha chain FT (By similarity). FT CHAIN 270 455 12S seed storage protein CRB beta chain FT (By similarity). FT DISULFID 106 276 Interchain (alpha-beta) (Potential). FT CONFLICT 383 383 A -> R (in Ref. 1). SQ SEQUENCE 455 AA; 50558 MW; BE24BCBD2F69B538 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 KHAIGEQFEW IEFKTNENAQ VNTLAGRTSV MRGLPLEVIT NGYQISPEEA KRVKFSTIET TLTHSSPMSY GRPRA // ID 13S1_FAGES STANDARD; PRT; 565 AA. AC O23878; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE 13S globulin seed storage protein 1 precursor (Legumin-like protein DE 1). GN Name=FA02; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP SEQUENCE FROM N.A., TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. RC STRAIN=cv. Kitayuki; TISSUE=Immature seed; RX MEDLINE=21205935; PubMed=11308332; DOI=10.1021/jf0011485; RA Fujino K., Funatsuki H., Inada M., Shimono Y., Kikuta Y.; RT "Expression, cloning, and immunological analysis of buckwheat RT (Fagopyrum esculentum Moench) seed storage proteins."; RL J. Agric. Food Chem. 49:1825-1829(2001). CC -!- FUNCTION: 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 (By similarity). +CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond (By similarity). CC -!- TISSUE SPECIFICITY: Expressed only in immatures seeds. -CC -!- DEVELOPMENTAL STAGE: Expressed between 7 and 28 days after -CC pollination. -CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly -CC homologous to the N-terminal sequence of BW24KD, a major buckwheat -CC allergen. -CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) -CC family. +CC -!- DEVELOPMENTAL STAGE: Expressed between 7 and 28 days after pollination. +CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly homologous to the N-terminal sequence of BW24KD, a major buckwheat allergen. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; D87980; BAA21758.1; -. DR PIR; T10696; T10696. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. PE 3: Inferred from homology; KW Multigene family; Seed storage protein; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 377 13S globulin seed storage protein 1 FT acidic chain (By similarity). FT CHAIN 378 565 13S globulin seed storage protein 1 basic FT chain (By similarity). FT DISULFID 120 384 Interchain (alpha-beta) (Potential). SQ SEQUENCE 565 AA; 64518 MW; 2DD7FCC64E3CD4F0 CRC64; MSTKLILSFS LCLMVLSCSA QLLPWRKGQR SRPHRGHQQF HHQCDVQRLT ASEPSRRVRS EAGVTEIWDN DTPEFRCAGF VAVRVVIQPG GLLLPSYSNA PYITFVEQGR GVQGVVVPGC PETFQSESEF EYPQSQRDQR SRQSESEESS RGDQRTRQSE SEEFSRGDQR TRQSESEEFS RGDQRTRQSE SEEFSRGDQR TRQSESEEFS RGDQHQKIFR IRDGDVIPSP AGVVQWTHND GDNDLISITL YDANSFQNQL DGNVRNFFLA GQSKQSREDR RSQRQTREEG SDRQSRESDD DEALLEANIL TGFQDEILQE IFRNVDQETI SKLRGDNDQR GFIVQARDLK LRVPEEYEEE LQRERGDRKR GGSGRSNGLE QAFCNLKFKQ NVNRPSRADV FNPRAGRINT VNSNNLPILE FIQLSAQHVV LYKNAILGPR WNLNAHSALY VTRGEGRVQV VGDEGRSVFD DNVQRGQILV VPQGFAVVLK AGREGLEWVE LKNDDNAITS PIAGKTSVLR AIPVEVLANS YDISTKEAFR LKNGRQEVEV FLPFQSRDEK ERERF // ID 13S2_FAGES STANDARD; PRT; 504 AA. AC O23880; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE 13S globulin seed storage protein 2 precursor (Legumin-like protein DE 2). GN Name=FA18; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Kitayuki; TISSUE=Immature seed; RX MEDLINE=21205935; PubMed=11308332; DOI=10.1021/jf0011485; RA Fujino K., Funatsuki H., Inada M., Shimono Y., Kikuta Y.; RT "Expression, cloning, and immunological analysis of buckwheat RT (Fagopyrum esculentum Moench) seed storage proteins."; RL J. Agric. Food Chem. 49:1825-1829(2001). CC -!- FUNCTION: 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 (By similarity). -CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly -CC homologous to the N-terminal sequence of BW24KD, a major buckwheat -CC allergen. -CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) -CC family. +CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond (By similarity). +CC -!- MISCELLANEOUS: The sequence of the probable beta chain is highly homologous to the N-terminal sequence of BW24KD, a major buckwheat allergen. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; D87982; BAA21760.1; -. DR PIR; T10698; T10698. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. PE 3: Inferred from homology; KW Multigene family; Seed storage protein; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 313 13S globulin seed storage protein 2 FT acidic chain (By similarity). FT CHAIN 314 504 13S globulin seed storage protein 2 basic FT chain (By similarity). FT DISULFID 122 320 Interchain (alpha-beta) (Potential). SQ SEQUENCE 504 AA; 57043 MW; CDCA322394A28194 CRC64; MSTKLILSFS LCLMVLSCSA QLWPWQKGQG SRPHHGRQQH QFQHQCDIQR LTASEPSRRV RSEAGVTEIW DHDTPEFRCT GFVAVRVVIQ PGGLLLPSYS NAPYITFVEQ GRGVQGVVIP GCPETFQSDS EFEYPQSQRG RHSRQSESEE ESSRGDQHQK IFRIREGDVI PSPAGVVQWT HNDGNDDLIS VTLLDANSYH KQLDENVRSF FLAGQSQRET REEGSDRQSR ESDDDEALLG ANILSGFQDE ILHELFRDVD RETISKLRGE NDQRGFIVQA QDLKLRVPQD FEEEYERERG DRRRGQGGSG RSNGVEQGFC NLKFRRNFNT PTNTYVFNPR AGRINTVNSN SLPILEFLQL SAQHVVLYKN AIIGPRWNLN AHSALYVTRG EGRVQVVGDE GKSVFDDKVQ RGQILVVPQG FAVVLKAGRE GLEWVELKNS GNAITSPIGG RTSVLRAIPV EVLANSYDIS TKEAYKLKNG RQEVEVFRPF QSRDEKERER FSIV // ID 13S3_FAGES STANDARD; PRT; 538 AA. AC Q9XFM4; Q9M641; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE 13S globulin seed storage protein 3 precursor (Legumin-like protein 3) DE (Allergen Fag e 1). GN Name=FAGAG1; OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=cv. Miyazaki zairai; RA Nair A., Ohmoto T., Woo S.H., Adachi T.; RT "A molecular-genetic approach for hypoallergenic buckwheat."; RL Fagopyrum 16:29-36(1999). RN [2] RP SEQUENCE OF 348-538 FROM N.A. RX MEDLINE=22690748; PubMed=12806007; DOI=10.1100/tsw.2002.157; RA Nair A., Adachi T.; RT "Screening and selection of hypoallergenic buckwheat species."; RL ScientificWorldJournal 2:818-826(2002). CC -!- FUNCTION: 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 (By similarity). +CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond (By similarity). CC -!- ALLERGEN: Causes an allergic reaction in human. -CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) -CC family. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) 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; AF152003; AAD32713.1; -. DR EMBL; AF216801; AAF34635.1; -. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 2. DR PRINTS; PR00439; 11SGLOBULIN. PE 3: Inferred from homology; KW Allergen; Multigene family; Seed storage protein; Signal. FT SIGNAL 1 20 Potential. FT CHAIN 21 347 13S globulin seed storage protein 3 FT acidic chain (By similarity). FT CHAIN 348 538 13S globulin seed storage protein 3 basic FT chain (By similarity). FT DISULFID 120 354 Interchain (alpha-beta) (Potential). SQ SEQUENCE 538 AA; 61163 MW; 41D6BA55220CFDAC CRC64; MSTKLILSFS LCLMVLSCSA QLLPWQKGQR SRPHHGHQQF QHQCDIQRLT ASEPSRRVRS EAGVTEIWDH DTPEFRCAGF VAVRVVIQPG GLLLPSYSNA PYITFVEQGR GVQGVVVPGC PETFQSGSEF EYPRSQRDQR SRQSESGESS RGDQRSRQSE SEESSRGDQR SRQSESEEFS RGDQHQKIFR IRDGDVIPSP AGVVQWTHNN GDNDLISITL YDANSFQNQL DENVRNFFLA GQSKQSREDR RSQRQTREEG SDRQSRESQD DEALLEANIL SGFEDEILQE IFRNVDQETI SKLRGENDQR GFIVQARDLK LRVPEEYEEE LQRERGDRKR GGSGRSNGLE QAFCNLKFRQ NVNRPSRADV FNPRAGRINT VDSNNLPILE FIQLSAQHVV LYKNAILGPR WNLNAHSALY VTRGEGRVQV VGDEGRSVFD DNVQRGQILV VPQGFAVVLK AGREGLEWVE LKNDDNAITS PIAGKTSVLR AIPVEVLANS YDISTKEAFR LKNGRQEVEV FRPFQSRDEK ERERFSIV // ID 13SB_FAGES STANDARD; PRT; 194 AA. AC P83004; DT 10-OCT-2003 (Rel. 42, Created) DT 10-OCT-2003 (Rel. 42, Last sequence update) DT 05-JUL-2004 (Rel. 44, Last annotation update) DE 13S globulin basic chain. OS Fagopyrum esculentum (Common buckwheat). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; core eudicots; OC Caryophyllales; Polygonaceae; Fagopyrum. OX NCBI_TaxID=3617; RN [1] RP SEQUENCE, FUNCTION, AND TISSUE SPECIFICITY. RC STRAIN=cv. BDS-1354; TISSUE=Endosperm; RX MEDLINE=22545158; PubMed=12657290; DOI=10.1016/S0031-9422(02)00755-0; RA Bharali S., Chrungoo N.K.; RT "Amino acid sequence of the 26 kDa subunit of legumin-type seed RT storage protein of common buckwheat (Fagopyrum esculentum Moench): RT molecular characterization and phylogenetic analysis."; RL Phytochemistry 63:1-5(2003). RN [2] RP SEQUENCE OF 1-17. RX MEDLINE=97357448; PubMed=9214774; DOI=10.1016/S0031-9422(97)00051-4; RA Rout M.K., Chrungoo N.K., Rao K.S.; RT "Amino acid sequence of the basic subunit of 13S globulin of RT buckwheat."; RL Phytochemistry 45:865-867(1997). -CC -!- FUNCTION: Seed storage protein with a relatively high level of Lys -CC and Met. -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 (By similarity). +CC -!- FUNCTION: Seed storage protein with a relatively high level of Lys and Met. +CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond (By similarity). CC -!- TISSUE SPECIFICITY: Cotyledons and endosperm protein bodies. -CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) -CC family. +CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family. DR HSSP; P04776; 1FXZ. DR InterPro; IPR006045; Cupin. DR InterPro; IPR011051; RmlC_like_cupin. DR InterPro; IPR006044; Seedstore_11s. DR Pfam; PF00190; Cupin; 1. DR PRINTS; PR00439; 11SGLOBULIN. PE 3: Inferred from homology; KW Direct protein sequencing; Multigene family; Seed storage protein. FT DISULFID 7 7 Interchain (alpha-beta) (Potential). SQ SEQUENCE 194 AA; 21846 MW; 65A6FC49AFC1E9D0 CRC64; GIDENVCTMK LRENIKSPQE ADFYNPKAGR ITTANSQKLP ALRSLQMSAE RGFLYSNGIY APHWNINAHS ALYVTRGNAK VQVVGDEGNK VFDDEVKQGQ LIIVPQYFAV IKKAGNQGFE YVAFKTNDNA MINPLVGRLS AFRAIPEEVL RSSFQISSEE AEELKYGRQE ALLLSEQSQQ GKREVADEKE RERF //