GLCA2_SOYBN
ID GLCA2_SOYBN Reviewed; 605 AA.
AC P0DO15; 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 2 {ECO:0000305};
DE Short=CG-alpha-2 {ECO:0000305};
DE AltName: Full=Beta-conglycinin alpha-related subunit {ECO:0000303|Ref.3};
DE AltName: Allergen=Gly m 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=CG-2 {ECO:0000303|Ref.3};
GN ORFNames=GLYMA_20G148400 {ECO:0000312|EMBL:KRG91332.1};
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; KRG91332.1; -; Genomic_DNA.
DR EMBL; ACUP02012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S20007; S20007.
DR RefSeq; NP_001236856.1; NM_001249927.1.
DR AlphaFoldDB; P0DO15; -.
DR SMR; P0DO15; -.
DR EnsemblPlants; KRG91330; KRG91330; GLYMA_20G148300.
DR EnsemblPlants; KRG91332; KRG91332; GLYMA_20G148400.
DR GeneID; 547464; -.
DR Gramene; KRG91330; KRG91330; GLYMA_20G148300.
DR Gramene; KRG91332; KRG91332; GLYMA_20G148400.
DR KEGG; gmx:547464; -.
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 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; Signal; Vacuole.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT PROPEP 23..62
FT /evidence="ECO:0000305|Ref.6"
FT /id="PRO_0000446073"
FT CHAIN 63..605
FT /note="Beta-conglycinin alpha subunit 2"
FT /id="PRO_5014589218"
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
