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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   -!- SUBUNIT: Homotetramer.
CC   -!- MISCELLANEOUS: The thermostability of the enzyme is greatly
CC       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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   -!- 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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   --------------------------------------------------------------------------
CC   This SWISS-PROT entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use  by  non-profit  institutions as long  as its content  is  in  no  way
CC   modified and this statement is not removed.  Usage  by  and for commercial
CC   entities 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   -!- ALLERGEN: Causes an allergic reaction in human.
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; 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   -!- TISSUE SPECIFICITY: Cotyledons and endosperm protein bodies.
CC   -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins)
CC       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
//
