GLYG3_SOYBN
ID GLYG3_SOYBN Reviewed; 481 AA.
AC P11828; Q852U4; Q852U5;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Glycinin G3 {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:2485233};
DE Short=Glycinin 11S G3 {ECO:0000305};
DE Short=Glycinin A1bB2 {ECO:0000303|PubMed:23908048};
DE AltName: Allergen=Gly m 6 {ECO:0000305};
DE Contains:
DE RecName: Full=Glycinin A1b subunit {ECO:0000303|PubMed:23908048};
DE AltName: Full=Glycinin A subunit;
DE Contains:
DE RecName: Full=Glycinin B2 subunit {ECO:0000303|PubMed:23908048};
DE AltName: Full=Glycinin B subunit;
DE Flags: Precursor;
GN Name=GY3 {ECO:0000303|PubMed:2485233};
GN OrderedLocusNames=Glyma19g34780 {ECO:0000305};
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].
RC STRAIN=cv. Dare; TISSUE=Leaf;
RX PubMed=2740231; DOI=10.1093/nar/17.11.4388;
RA Cho T.-J., Nielsen N.C.;
RT "The glycinin Gy3 gene from soybean.";
RL Nucleic Acids Res. 17:4388-4388(1989).
RN [2]
RP DISCUSSION OF SEQUENCE, FUNCTION, AND GENE FAMILY.
RX PubMed=2485233; DOI=10.2307/3869011;
RA Nielsen N.C., Dickinson C.D., Cho T.-J., Thanh V.H., Scallon B.J.,
RA Fischer R.L., Sims T.L., Drews G.N., Goldberg R.B.;
RT "Characterization of the glycinin gene family in soybean.";
RL Plant Cell 1:313-328(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Matsuura; TISSUE=Seed;
RA Fukazawa C.;
RT "Cloning of two type glycinin A1bB2 from soybean (Glycine max L. Merril.
RT ver. Matsuura).";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP BIOTECHNOLOGY.
RX PubMed=10867183; DOI=10.1016/s0168-1656(00)00239-x;
RA Renkema J.M., Lakemond C.M., de Jongh H.H., Gruppen H., van Vliet T.;
RT "The effect of pH on heat denaturation and gel forming properties of soy
RT proteins.";
RL J. Biotechnol. 79:223-230(2000).
RN [5]
RP POLYMORPHISM, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17524657; DOI=10.1016/j.plaphy.2007.03.031;
RA Natarajan S., Xu C., Bae H., Bailey B.A., Cregan P., Caperna T.J.,
RA Garrett W.M., Luthria D.;
RT "Proteomic and genetic analysis of glycinin subunits of sixteen soybean
RT genotypes.";
RL Plant Physiol. Biochem. 45:436-444(2007).
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).
RN [7]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=22236762; DOI=10.1016/j.ijfoodmicro.2011.12.004;
RA Sitohy M.Z., Mahgoub S.A., Osman A.O.;
RT "In vitro and in situ antimicrobial action and mechanism of glycinin and
RT its basic subunit.";
RL Int. J. Food Microbiol. 154:19-29(2012).
RN [8]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=22245912; DOI=10.1016/j.plaphy.2011.12.007;
RA Asakura T., Tamura T., Terauchi K., Narikawa T., Yagasaki K., Ishimaru Y.,
RA Abe K.;
RT "Global gene expression profiles in developing soybean seeds.";
RL Plant Physiol. Biochem. 52:147-153(2012).
RN [9]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=23908048; DOI=10.1107/s1744309113019684;
RA Prak K., Mikami B., Itoh T., Fukuda T., Maruyama N., Utsumi S.;
RT "Purification, crystallization and preliminary crystallographic analysis of
RT soybean mature glycinin A1bB2.";
RL Acta Crystallogr. F 69:937-941(2013).
RN [10]
RP ALLERGEN.
RX PubMed=23426933; DOI=10.1002/jsfa.6113;
RA Taliercio E., Kim S.W.;
RT "Epitopes from two soybean glycinin subunits are antigenic in pigs.";
RL J. Sci. Food Agric. 93:2927-2932(2013).
RN [11]
RP ALLERGEN, AND REVIEW.
RX PubMed=24499064; DOI=10.1080/10408398.2011.613534;
RA Wang T., Qin G.-X., Sun Z.-W., Zhao Y.;
RT "Advances of research on glycinin and beta-conglycinin: a review of two
RT major soybean allergenic proteins.";
RL Crit. Rev. Food Sci. Nutr. 54:850-862(2014).
RN [12]
RP FUNCTION, AND BIOTECHNOLOGY.
RX DOI=10.1016/j.ifset.2015.07.009;
RA Li Y.-Q., Sun X.-X., Feng J.-L., Mo H.-Z.;
RT "Antibacterial activities and membrane permeability actions of glycinin
RT basic peptide against Escherichia coli.";
RL Innovative Food Sci. Emerg. Technol. 31:170-176(2015).
RN [13]
RP BIOTECHNOLOGY.
RX PubMed=30263339; DOI=10.1007/s10068-016-0135-2;
RA Li Y.-Q., Hao M., Yang J., Mo H.-Z.;
RT "Effects of glycinin basic polypeptide on sensory and physicochemical
RT properties of chilled pork.";
RL Food Sci. Biotechnol. 25:803-809(2016).
RN [14]
RP BIOTECHNOLOGY.
RX PubMed=25801436; DOI=10.1002/jsfa.7184;
RA He X.-T., Yuan D.-B., Wang J.-M., Yang X.-Q.;
RT "Thermal aggregation behaviour of soy protein: characteristics of different
RT polypeptides and sub-units.";
RL J. Sci. Food Agric. 96:1121-1131(2016).
RN [15]
RP FUNCTION, AND BIOTECHNOLOGY.
RX PubMed=28590128; DOI=10.1021/acs.jafc.7b02295;
RA Zhao G.-P., Li Y.-Q., Sun G.-J., Mo H.-Z.;
RT "Antibacterial actions of glycinin basic peptide against Escherichia
RT coli.";
RL J. Agric. Food Chem. 65:5173-5180(2017).
RN [16]
RP ALLERGEN.
RX PubMed=27620509; DOI=10.1002/jsfa.8036;
RA Bu G., Zhu T., Chen F.;
RT "The structural properties and antigenicity of soybean glycinin by
RT glycation with xylose.";
RL J. Sci. Food Agric. 97:2256-2262(2017).
RN [17]
RP PTM, BIOTECHNOLOGY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=29037738; DOI=10.1016/j.foodchem.2017.09.035;
RA Gonzalez-Montoya M., Hernandez-Ledesma B., Silvan J.M., Mora-Escobedo R.,
RA Martinez-Villaluenga C.;
RT "Peptides derived from in vitro gastrointestinal digestion of germinated
RT soybean proteins inhibit human colon cancer cells proliferation and
RT inflammation.";
RL Food Chem. 242:75-82(2018).
RN [18]
RP BIOTECHNOLOGY, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=30249015; DOI=10.3390/ijms19102883;
RA Gonzalez-Montoya M., Hernandez-Ledesma B., Mora-Escobedo R.,
RA Martinez-Villaluenga C.;
RT "Bioactive peptides from germinated soybean with anti-diabetic potential by
RT inhibition of dipeptidyl peptidase-IV, alpha-amylase, and alpha-glucosidase
RT enzymes.";
RL Int. J. Mol. Sci. 19:0-0(2018).
RN [19]
RP ALLERGEN.
RX PubMed=30139257; DOI=10.1021/acs.jafc.8b03641;
RA Peng C., Cao C., He M., Shu Y., Tang X., Wang Y., Zhang Y., Xia X., Li Y.,
RA Wu J.;
RT "Soybean Glycinin- and beta-Conglycinin-Induced Intestinal Damage in
RT Piglets via the p38/JNK/NF-kappaB Signaling Pathway.";
RL J. Agric. Food Chem. 66:9534-9541(2018).
RN [20]
RP BIOTECHNOLOGY.
RX PubMed=30372068; DOI=10.1021/acs.jafc.8b03398;
RA Peng X.Q., Xu Y.T., Liu T.X., Tang C.H.;
RT "Molecular Mechanism for Improving Emulsification Efficiency of Soy
RT Glycinin by Glycation with Soy Soluble Polysaccharide.";
RL J. Agric. Food Chem. 66:12316-12326(2018).
RN [21]
RP ALLERGEN.
RX PubMed=30300740; DOI=10.1016/j.fsi.2018.10.013;
RA Han F., Wang X., Guo J., Qi C., Xu C., Luo Y., Li E., Qin J.G., Chen L.;
RT "Effects of glycinin and beta-conglycinin on growth performance and
RT intestinal health in juvenile Chinese mitten crabs (Eriocheir sinensis).";
RL Fish Shellfish Immunol. 84:269-279(2019).
CC -!- FUNCTION: Glycinin is the major seed storage protein of soybean
CC (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower
CC extent, glycinin exhibit antibacterial activity against Gram-negative
CC and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli
CC and S.enteritidis) by forming pores and aggregating in transmembranes,
CC leading to membrane permeability and, eventually, cell death
CC (PubMed:22236762, Ref.12, PubMed:28590128).
CC {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233,
CC ECO:0000269|PubMed:28590128, ECO:0000269|Ref.12}.
CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a basic
CC chain derived from a single precursor and linked by a disulfide bond.
CC {ECO:0000250|UniProtKB:P04776}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000250|UniProtKB:P04776}. Protein storage vacuole
CC {ECO:0000250|UniProtKB:P04776}. Note=Hexamers are assembled in the
CC endoplasmic reticulum and later sorted to the protein storage vacuoles.
CC {ECO:0000250|UniProtKB:P04776}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P11828-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P11828-2; Sequence=VSP_060144;
CC -!- TISSUE SPECIFICITY: Confined to developing seeds.
CC {ECO:0000269|PubMed:22245912}.
CC -!- DEVELOPMENTAL STAGE: Progressive level increase from pod to full-size
CC seed growth. {ECO:0000269|PubMed:22245912}.
CC -!- PTM: During soybean germination, seed storage proteins are hydrolyzed
CC by protease/26S proteasome. {ECO:0000269|PubMed:29037738}.
CC -!- ALLERGEN: Causes an allergic reaction in human and animals (e.g. rats,
CC mouse and piglets); the acidic subunit is particularly allergenic
CC (PubMed:18996574, PubMed:24499064, PubMed:23426933). Binds to IgE of
CC patients with severe allergic reactions (anaphylaxis) to soybean
CC (PubMed:18996574). Allergy to soybean is most common for infants
CC (usually appears at the age of three months) which frequently outgrow
CC their soybean allergy by the age of two, but a severe soybean allergy
CC can last a lifetime; various symptoms involve skin, gastrointestinal
CC tract and respiratory tracts (PubMed:24499064). Damaged intestinal
CC function in piglets is associated with glycinin-mediated perturbation
CC of nuclear factor-kappa B (NF-kappaB), Jun N-terminal kinase (JNK) and
CC p38 levels (PubMed:30139257). Juvenile Chinese mitten crabs
CC (E.sinensis) supplemented with glycinin display impaired growth and
CC altered intestinal health due to gut inflammation, reshaped community
CC of gut microbiota and digestive dysfunction (PubMed:30300740).
CC Ingredient processing methods to reduce soybean allergenicity but
CC keeping its nutritional values have been developed, among them physical
CC processing includes extrusion, high-pressure (>300 MPa), heating
CC (between 70 and 90 degrees Celsius), roasting, chemical processing
CC includes ethanol extraction (55-76 percent between 70 and 80 degrees
CC Celsius), in vitro glycation (e.g. with xylose at 55 degrees Celsius)
CC and enzymatic hydrolysis with pepsin and trypsin, and biological
CC processing includes fermentation with A.oryzae, S.cerevisiae, L.lactic
CC subsplactis, B.subtilis, B.lactic and L.plantarum (PubMed:24499064,
CC PubMed:27620509). Resistant to hydrolysis by papain, alcalase, and
CC fungal protease (PubMed:24499064). {ECO:0000269|PubMed:18996574,
CC ECO:0000269|PubMed:23426933, ECO:0000269|PubMed:27620509,
CC ECO:0000269|PubMed:30139257, ECO:0000269|PubMed:30300740,
CC ECO:0000303|PubMed:24499064}.
CC -!- BIOTECHNOLOGY: Emulsification efficiency of glycinin is improved by
CC degree-dependent glycation with soy soluble polysaccharide (SSPS) at 60
CC degrees Celsius in both the acidic (A) and basic (B) polypeptides as a
CC result of subunit dissociation at the quaternary level
CC (PubMed:30372068). Thermal treatment of soybean seed proteins leads to
CC the aggregation of glycinin acidic and basic polypeptides (GAP and GBP,
CC respectively) (PubMed:10867183, PubMed:25801436). GBP improve sensory
CC properties of meat (e.g. pork) during chilled storage and inhibit
CC bacterial growth (e.g. L.monocytogenes, B.subtilis, E.coli and
CC S.enteritidis) (PubMed:30263339, PubMed:22236762). Antibacterial
CC properties of the GBP antimicrobial peptides (AMPs) associated with no
CC cytotoxicity on the viability of human embryonic kidney cells make them
CC promising candidates as natural antibacterial agents (PubMed:22236762,
CC Ref.12, PubMed:28590128). Fragmented peptides resulting from
CC gastrointestinal digestion of germinated soybeans seem to have
CC anticancer and anti-inflammatory actions on human colon cancer cells
CC (e.g. Caco-2, HT-29, and HCT-116) and macrophages (LPS-stimulated RAW
CC 264.7) (PubMed:29037738). Such peptides resulting from digested
CC germinated soybeans exhibit also anti-diabetic potential by inhibiting
CC dipeptidyl peptidase IV (DPP-IV), salivary alpha-amylase and intestinal
CC alpha-glucosidase enzymes (PubMed:30249015).
CC {ECO:0000269|PubMed:10867183, ECO:0000269|PubMed:22236762,
CC ECO:0000269|PubMed:25801436, ECO:0000269|PubMed:28590128,
CC ECO:0000269|PubMed:29037738, ECO:0000269|PubMed:30249015,
CC ECO:0000269|PubMed:30263339, ECO:0000269|PubMed:30372068,
CC ECO:0000269|Ref.12}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; X15123; CAA33217.1; -; Genomic_DNA.
DR EMBL; AB030494; BAC55937.1; -; mRNA.
DR EMBL; AB030495; BAC55938.1; -; mRNA.
DR PIR; S04605; S04605.
DR RefSeq; NP_001236840.1; NM_001249911.1. [P11828-1]
DR AlphaFoldDB; P11828; -.
DR SMR; P11828; -.
DR STRING; 3847.GLYMA19G34780.1; -.
DR Allergome; 5821; Gly m 6.
DR Allergome; 5824; Gly m 6.0301.
DR PRIDE; P11828; -.
DR EnsemblPlants; KRG95667; KRG95667; GLYMA_19G164900. [P11828-1]
DR GeneID; 547463; -.
DR Gramene; KRG95667; KRG95667; GLYMA_19G164900. [P11828-1]
DR KEGG; gmx:547463; -.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR InParanoid; P11828; -.
DR OMA; PHGKRVH; -.
DR OrthoDB; 603461at2759; -.
DR Proteomes; UP000008827; Chromosome 19.
DR Genevisible; P11828; GM.
DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR GO; GO:0000326; C:protein storage vacuole; ISS:UniProtKB.
DR GO; GO:0045735; F:nutrient reservoir activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.120.10; -; 2.
DR InterPro; IPR022379; 11S_seedstore_CS.
DR InterPro; IPR006044; 11S_seedstore_pln.
DR InterPro; IPR006045; Cupin_1.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR011051; RmlC_Cupin_sf.
DR Pfam; PF00190; Cupin_1; 2.
DR PRINTS; PR00439; 11SGLOBULIN.
DR SMART; SM00835; Cupin_1; 2.
DR SUPFAM; SSF51182; SSF51182; 1.
DR PROSITE; PS00305; 11S_SEED_STORAGE; 1.
PE 1: Evidence at protein level;
KW Allergen; Alternative splicing; Disulfide bond; Endoplasmic reticulum;
KW Reference proteome; Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..296
FT /note="Glycinin A1b subunit"
FT /id="PRO_0000032017"
FT CHAIN 297..476
FT /note="Glycinin B2 subunit"
FT /id="PRO_0000032018"
FT PROPEP 477..481
FT /id="PRO_0000032019"
FT DOMAIN 36..240
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 309..458
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 193..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 472..481
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT COMPBIAS 271..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 31..64
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT DISULFID 107..303
FT /note="Interchain (between A and B chains)"
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT VAR_SEQ 72..75
FT /note="CTLN -> YTLI (in isoform 2)"
FT /id="VSP_060144"
FT CONFLICT 42
FT /note="D -> G (in Ref. 3; BAC55938/BAC55937)"
FT /evidence="ECO:0000305"
FT CONFLICT 97
FT /note="S -> N (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="F -> L (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="P -> L (in Ref. 3; BAC55938/BAC55937)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="L -> I (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="FQ -> LE (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="E -> Q (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="P -> S (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="I -> M (in Ref. 3; BAC55938/BAC55937)"
FT /evidence="ECO:0000305"
FT CONFLICT 238
FT /note="I -> IV (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="K -> R (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 271..272
FT /note="QQ -> RR (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="R -> G (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
FT CONFLICT 399
FT /note="I -> T (in Ref. 3; BAC55938)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 481 AA; 54242 MW; 5F3C3148DF6241A7 CRC64;
MAKLVLSLCF LLFSGCCFAF SFREQPQQNE CQIQRLNALK PDNRIESEGG FIETWNPNNK
PFQCAGVALS RCTLNRNALR RPSYTNAPQE IYIQQGSGIF GMIFPGCPST FEEPQQKGQS
SRPQDRHQKI YHFREGDLIA VPTGFAYWMY NNEDTPVVAV SLIDTNSFQN QLDQMPRRFY
LAGNQEQEFL QYQPQKQQGG TQSQKGKRQQ EEENEGGSIL SGFAPEFLEH AFVVDRQIVR
KLQGENEEEE KGAIVTVKGG LSVISPPTEE QQQRPEEEEK PDCDEKDKHC QSQSRNGIDE
TICTMRLRHN IGQTSSPDIF NPQAGSITTA TSLDFPALSW LKLSAQFGSL RKNAMFVPHY
NLNANSIIYA LNGRALVQVV NCNGERVFDG ELQEGQVLIV PQNFAVAARS QSDNFEYVSF
KTNDRPSIGN LAGANSLLNA LPEEVIQQTF NLRRQQARQV KNNNPFSFLV PPKESQRRVV
A
