GLCB2_SOYBN
ID GLCB2_SOYBN Reviewed; 439 AA.
AC F7J077;
DT 16-JAN-2019, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 1.
DT 25-MAY-2022, entry version 80.
DE RecName: Full=Beta-conglycinin beta subunit 2 {ECO:0000305};
DE Short=CG-beta-2 {ECO:0000303|PubMed:16755137};
DE AltName: Allergen=Gly m 5 {ECO:0000305};
DE Flags: Precursor;
GN Name=CG-4 {ECO:0000305};
GN ORFNames=GLYMA_20G148200 {ECO:0000312|EMBL:KRG91329.1};
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 [GENOMIC DNA].
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 [2]
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 [3]
RP PROTEIN SEQUENCE OF 24-50.
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 [4]
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 [5]
RP SUBCELLULAR LOCATION.
RX DOI=10.1016/j.plantsci.2004.06.004;
RA Nishizawa K., Maruyama N., Satoh R., Higasa T., Utsumi S.;
RT "A vacuolar sorting determinant of soybean beta-conglycinin beta subunit
RT resides in a C-terminal sequence.";
RL Plant Sci. 167:937-947(2004).
RN [6]
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).
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 {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.5}.
CC Note=Localizes in protein storage vacuoles in cotyledons of developing
CC and mature beans (PubMed:15447650, Ref.5). Synthesized and assembled
CC into trimers in the endoplasmic reticulum, and transported to the
CC protein storage vacuoles by the dense vesicles (PubMed:15447650).
CC {ECO:0000269|PubMed:15447650, ECO:0000269|Ref.5}.
CC -!- PTM: The N-linked glycans are not essential for the folding and
CC assembly into trimers. {ECO:0000250|UniProtKB:P25974}.
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; AB604031; BAK39720.1; -; Genomic_DNA.
DR EMBL; CM000853; KRG91329.1; -; Genomic_DNA.
DR EMBL; ACUP02012676; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003556052.1; XM_003556004.3.
DR AlphaFoldDB; F7J077; -.
DR SMR; F7J077; -.
DR STRING; 3847.GLYMA20G28640.1; -.
DR Allergome; 5816; Gly m 5.
DR EnsemblPlants; KRG91329; KRG91329; GLYMA_20G148200.
DR GeneID; 100806840; -.
DR Gramene; KRG91329; KRG91329; GLYMA_20G148200.
DR eggNOG; ENOG502QQEP; Eukaryota.
DR HOGENOM; CLU_018703_0_1_1; -.
DR InParanoid; F7J077; -.
DR OMA; ELTGDEC; -.
DR OrthoDB; 1072107at2759; -.
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; IPR013096; Cupin_2.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 1.
DR Pfam; PF07883; Cupin_2; 1.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 2.
PE 1: Evidence at protein level;
KW Allergen; Direct protein sequencing; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal; Vacuole.
FT SIGNAL 1..23
FT /evidence="ECO:0000305|Ref.3"
FT CHAIN 24..439
FT /note="Beta-conglycinin beta subunit 2"
FT /id="PRO_5014571663"
FT DOMAIN 34..193
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 240..401
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 411..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..439
FT /note="Necessary for sorting to protein storage vacuole"
FT /evidence="ECO:0000269|Ref.5"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 439 AA; 50442 MW; 76D20042274C688A CRC64;
MMRVRFPLLV LLGTVFLASV CVSLKVREDE NNPFYLRSSN SFQTLFENQN GRIRLLQRFN
KRSPQLENLR DYRIVQFQSK PNTILLPHHA DADFLLFVLS GRAILTLVNN DDRDSYNLHP
GDAQRIPAGT TYYLVNPHDH QNLKIIKLAI PVNKPGRYDD FFLSSTQAQQ SYLQGFSHNI
LETSFHSEFE EINRVLLGEE EEQRQQEGVI VELSKEQIRQ LSRRAKSSSR KTISSEDEPF
NLRSRNPIYS NNFGKFFEIT PEKNPQLRDL DIFLSSVDIN EGALLLPHFN SKAIVILVIN
EGDANIELVG IKEQQQKQKQ EEEPLEVQRY RAELSEDDVF VIPAAYPFVV NATSNLNFLA
FGINAENNQR NFLAGEKDNV VRQIERQVQE LAFPGSAQDV ERLLKKQRES YFVDAQPQQK
EEGSKGRKGP FPSILGALY
