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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 //