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GLCA1_SOYBN
ID   GLCA1_SOYBN             Reviewed;         605 AA.
AC   P0DO16; P13916; Q94LX2;
DT   16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-JAN-2019, sequence version 1.
DT   25-MAY-2022, entry version 15.
DE   RecName: Full=Beta-conglycinin alpha subunit 1 {ECO:0000305};
DE            Short=CG-alpha-1 {ECO:0000305};
DE   AltName: Full=Beta-conglycinin alpha subunit {ECO:0000303|Ref.3};
DE   AltName: Allergen=Gly m 5 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=CG-3 {ECO:0000303|Ref.3};
GN   ORFNames=GLYMA_20G148300 {ECO:0000312|EMBL:KRG91330.1};
OS   Glycine max (Soybean) (Glycine hispida).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Glycine;
OC   Glycine subgen. Soja.
OX   NCBI_TaxID=3847;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cotyledon;
RX   PubMed=2103438; DOI=10.1007/bf00017745;
RA   Sebastiani F.L., Farrel L.B., Schuler M.A., Beachy R.N.;
RT   "Complete sequence of a cDNA of alpha subunit of soybean beta-
RT   conglycinin.";
RL   Plant Mol. Biol. 15:197-201(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=11434464; DOI=10.1266/ggs.76.99;
RA   Yoshino M., Kanazawa A., Tsutsumi K.I., Nakamura I., Shimamoto Y.;
RT   "Structure and characterization of the gene encoding alpha subunit of
RT   soybean beta-conglycinin.";
RL   Genes Genet. Syst. 76:99-105(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   DOI=10.1270/jsbbs.52.285;
RA   Yoshino M., Kanazawa A., Tsutsumi K., Nakamura I., Takahashi K.,
RA   Shimamoto Y.;
RT   "Structural variation around the gene encoding the alpha subunit of soybean
RT   beta-conglycinin and correlation with the expression of the alpha
RT   subunit.";
RL   Breed. Sci. 52:285-292(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=16755137; DOI=10.1266/ggs.81.135;
RA   Yoshino M., Nagamatsu A., Tsutsumi K., Kanazawa A.;
RT   "The regulatory function of the upstream sequence of the beta-conglycinin
RT   alpha subunit gene in seed-specific transcription is associated with the
RT   presence of the RY sequence.";
RL   Genes Genet. Syst. 81:135-141(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Williams 82;
RX   PubMed=20075913; DOI=10.1038/nature08670;
RA   Schmutz J., Cannon S.B., Schlueter J., Ma J., Mitros T., Nelson W.,
RA   Hyten D.L., Song Q., Thelen J.J., Cheng J., Xu D., Hellsten U., May G.D.,
RA   Yu Y., Sakurai T., Umezawa T., Bhattacharyya M.K., Sandhu D.,
RA   Valliyodan B., Lindquist E., Peto M., Grant D., Shu S., Goodstein D.,
RA   Barry K., Futrell-Griggs M., Abernathy B., Du J., Tian Z., Zhu L., Gill N.,
RA   Joshi T., Libault M., Sethuraman A., Zhang X.-C., Shinozaki K.,
RA   Nguyen H.T., Wing R.A., Cregan P., Specht J., Grimwood J., Rokhsar D.,
RA   Stacey G., Shoemaker R.C., Jackson S.A.;
RT   "Genome sequence of the palaeopolyploid soybean.";
RL   Nature 463:178-183(2010).
RN   [6]
RP   PROTEIN SEQUENCE OF 63-75.
RC   STRAIN=cv. Raiden;
RX   DOI=10.1016/S0031-9422(00)81477-6;
RA   Hirano H., Kagawa H., Kamata Y., Yamauchi F.;
RT   "Structural homology among the major 7s globulin subunits of soybean seed
RT   storage proteins.";
RL   Phytochemistry 26:41-45(1987).
RN   [7]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=15447650; DOI=10.1111/j.1365-313x.2004.02204.x;
RA   Mori T., Maruyama N., Nishizawa K., Higasa T., Yagasaki K., Ishimoto M.,
RA   Utsumi S.;
RT   "The composition of newly synthesized proteins in the endoplasmic reticulum
RT   determines the transport pathways of soybean seed storage proteins.";
RL   Plant J. 40:238-249(2004).
RN   [8]
RP   ALLERGEN.
RX   PubMed=18996574; DOI=10.1016/j.jaci.2008.09.034;
RA   Holzhauser T., Wackermann O., Ballmer-Weber B.K., Bindslev-Jensen C.,
RA   Scibilia J., Perono-Garoffo L., Utsumi S., Poulsen L.K., Vieths S.;
RT   "Soybean (Glycine max) allergy in Europe: Gly m 5 (beta-conglycinin) and
RT   Gly m 6 (glycinin) are potential diagnostic markers for severe allergic
RT   reactions to soy.";
RL   J. Allergy Clin. Immunol. 123:452-458(2009).
RN   [9]
RP   DISULFIDE BOND.
RX   PubMed=22218927; DOI=10.1104/pp.111.189621;
RA   Wadahama H., Iwasaki K., Matsusaki M., Nishizawa K., Ishimoto M.,
RA   Arisaka F., Takagi K., Urade R.;
RT   "Accumulation of beta-conglycinin in soybean cotyledon through the
RT   formation of disulfide bonds between alpha'- and alpha-subunits.";
RL   Plant Physiol. 158:1395-1405(2012).
CC   -!- FUNCTION: Seed storage protein. Accumulates during seed development and
CC       is hydrolyzed after germination to provide a carbon and nitrogen source
CC       for the developing seedling. {ECO:0000305}.
CC   -!- SUBUNIT: The alpha-, alpha'-, and beta-subunits associate in various
CC       combinations to form trimeric proteins. {ECO:0000305|PubMed:15447650}.
CC   -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain {ECO:0000305}.
CC       Endoplasmic reticulum {ECO:0000269|PubMed:15447650}. Protein storage
CC       vacuole. Note=Localizes in protein storage vacuoles in cotyledons of
CC       developing and mature beans (PubMed:15447650). Synthesized and
CC       assembled into trimers in the endoplasmic reticulum, and transported to
CC       the protein storage vacuoles by the dense vesicles (PubMed:15447650).
CC       {ECO:0000269|PubMed:15447650}.
CC   -!- ALLERGEN: Causes an allergic reaction in human (PubMed:18996574). Binds
CC       to IgE of patients with severe allergic reactions (anaphylaxis) to
CC       soybean (PubMed:18996574). {ECO:0000269|PubMed:18996574}.
CC   -!- SIMILARITY: Belongs to the 7S seed storage protein family.
CC       {ECO:0000305}.
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DR   EMBL; X17698; CAA35691.1; -; mRNA.
DR   EMBL; AB051865; BAB56161.1; -; Genomic_DNA.
DR   EMBL; AB237643; BAE46788.1; -; Genomic_DNA.
DR   EMBL; CM000853; KRG91330.1; -; Genomic_DNA.
DR   EMBL; ACUP02012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; S14681; FWSYBA.
DR   AlphaFoldDB; P0DO16; -.
DR   SMR; P0DO16; -.
DR   STRING; 3847.GLYMA20G28650.1; -.
DR   EnsemblPlants; KRG91330; KRG91330; GLYMA_20G148300.
DR   EnsemblPlants; KRG91332; KRG91332; GLYMA_20G148400.
DR   Gramene; KRG91330; KRG91330; GLYMA_20G148300.
DR   Gramene; KRG91332; KRG91332; GLYMA_20G148400.
DR   OMA; SIWRNID; -.
DR   Proteomes; UP000008827; Chromosome 20.
DR   GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0000326; C:protein storage vacuole; IDA:UniProtKB.
DR   GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.10; -; 2.
DR   InterPro; IPR006045; Cupin_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   Pfam; PF00190; Cupin_1; 2.
DR   SMART; SM00835; Cupin_1; 2.
DR   SUPFAM; SSF51182; SSF51182; 2.
PE   1: Evidence at protein level;
KW   Allergen; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW   Glycoprotein; Reference proteome; Seed storage protein; Signal;
KW   Storage protein; Vacuole.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   PROPEP          23..62
FT                   /evidence="ECO:0000305|Ref.6"
FT                   /id="PRO_0000032186"
FT   CHAIN           63..605
FT                   /note="Beta-conglycinin alpha subunit 1"
FT                   /evidence="ECO:0000269|Ref.6"
FT                   /id="PRO_0000032187"
FT   DOMAIN          196..354
FT                   /note="Cupin type-1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          406..567
FT                   /note="Cupin type-1 2"
FT                   /evidence="ECO:0000255"
FT   REGION          65..195
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..135
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        150..167
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        261
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        517
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        68
FT                   /note="Interchain (with C-69 in alpha' subunit)"
FT                   /evidence="ECO:0000305|PubMed:22218927"
FT   CONFLICT        166..167
FT                   /note="KQ -> NE (in Ref. 1; CAA35691)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   605 AA;  70306 MW;  8ACE6F8532662984 CRC64;
     MMRARFPLLL LGLVFLASVS VSFGIAYWEK ENPKHNKCLQ SCNSERDSYR NQACHARCNL
     LKVEKEECEE GEIPRPRPRP QHPEREPQQP GEKEEDEDEQ PRPIPFPRPQ PRQEEEHEQR
     EEQEWPRKEE KRGEKGSEEE DEDEDEEQDE RQFPFPRPPH QKEERKQEED EDEEQQRESE
     ESEDSELRRH KNKNPFLFGS NRFETLFKNQ YGRIRVLQRF NQRSPQLQNL RDYRILEFNS
     KPNTLLLPNH ADADYLIVIL NGTAILSLVN NDDRDSYRLQ SGDALRVPSG TTYYVVNPDN
     NENLRLITLA IPVNKPGRFE SFFLSSTEAQ QSYLQGFSRN ILEASYDTKF EEINKVLFSR
     EEGQQQGEQR LQESVIVEIS KEQIRALSKR AKSSSRKTIS SEDKPFNLRS RDPIYSNKLG
     KFFEITPEKN PQLRDLDIFL SIVDMNEGAL LLPHFNSKAI VILVINEGDA NIELVGLKEQ
     QQEQQQEEQP LEVRKYRAEL SEQDIFVIPA GYPVVVNATS NLNFFAIGIN AENNQRNFLA
     GSQDNVISQI PSQVQELAFP GSAQAVEKLL KNQRESYFVD AQPKKKEEGN KGRKGPLSSI
     LRAFY
 
 
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