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 13-NOV-2019, entry version 114. 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; OC Pentapetalae; rosids; fabids; Fabales; Fabaceae; Papilionoideae; OC 50 kb inversion clade; NPAAA clade; indigoferoid/millettioid clade; OC Phaseoleae; Glycine; 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=10.1105/tpc.1.3.313; 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. RT Merril. 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 RT soy 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 RT soybean 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) RT and Gly m 6 (glycinin) are potential diagnostic markers for severe RT allergic 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 RT and 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., RA Ishimaru Y., 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 RT analysis of 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 RT two 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 RT glycinin 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 RT different 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., RA Mora-Escobedo R., Martinez-Villaluenga C.; RT "Peptides derived from in vitro gastrointestinal digestion of RT germinated soybean proteins inhibit human colon cancer cells RT proliferation and 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 RT potential by inhibition of dipeptidyl peptidase-IV, alpha-amylase, and RT alpha-glucosidase 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., RA Li Y., 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., RA Chen L.; RT "Effects of glycinin and beta-conglycinin on growth performance and RT intestinal health in juvenile Chinese mitten crabs (Eriocheir RT 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- CC negative and Gram-positive bacteria (e.g. L.monocytogenes, CC B.subtilis, E.coli and S.enteritidis) by forming pores and CC aggregating in transmembranes, leading to membrane permeability CC and, eventually, cell death (PubMed:22236762, Ref.12, CC PubMed:28590128). {ECO:0000269|PubMed:22236762, CC ECO:0000269|PubMed:2485233, ECO:0000269|PubMed:28590128, CC ECO:0000269|Ref.12}. CC -!- SUBUNIT: Hexamer; each subunit is composed of an acidic and a CC basic chain derived from a single precursor and linked by a CC disulfide bond. {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 CC vacuoles. {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 Note=No experimental confirmation available. CC {ECO:0000312|EMBL:BAC55938.1}; CC -!- TISSUE SPECIFICITY: Confined to developing seeds. CC {ECO:0000269|PubMed:22245912}. CC -!- DEVELOPMENTAL STAGE: Progressive level increase from pod to full- CC size seed growth. {ECO:0000269|PubMed:22245912}. CC -!- PTM: During soybean germination, seed storage proteins are CC hydrolyzed by protease/26S proteasome. CC {ECO:0000269|PubMed:29037738}. CC -!- ALLERGEN: Causes an allergic reaction in human and animals (e.g. CC rats, mouse and piglets); the acidic subunit is particularly CC allergenic (PubMed:18996574, PubMed:24499064, PubMed:23426933). CC Binds to IgE of patients with severe allergic reactions CC (anaphylaxis) to soybean (PubMed:18996574). Allergy to soybean is CC most common for infants (usually appears at the age of three CC months) which frequently outgrow their soybean allergy by the age CC of two, but a severe soybean allergy can last a lifetime; various CC symptoms involve skin, gastrointestinal tract and respiratory CC tracts (PubMed:24499064). Damaged intestinal function in piglets CC is associated with glycinin-mediated perturbation of nuclear CC factor-kappa B (NF-kappaB), Jun N-terminal kinase (JNK) and p38 CC levels (PubMed:30139257). Juvenile Chinese mitten crabs CC (E.sinensis) supplemented with glycinin display impaired growth CC and altered intestinal health due to gut inflammation, reshaped CC community of gut microbiota and digestive dysfunction CC (PubMed:30300740). Ingredient processing methods to reduce soybean CC allergenicity but keeping its nutritional values have been CC developed, among them physical processing includes extrusion, CC high-pressure (>300 MPa), heating (between 70 and 90 degrees CC Celsius), roasting, chemical processing includes ethanol CC extraction (55-76 percent between 70 and 80 degrees Celsius), in CC vitro glycation (e.g. with xylose at 55 degrees Celsius) and CC enzymatic hydrolysis with pepsin and trypsin, and biological CC processing includes fermentation with A.oryzae, S.cerevisiae, CC L.lactic subsplactis, B.subtilis, B.lactic and L.plantarum CC (PubMed:24499064, PubMed:27620509). Resistant to hydrolysis by CC papain, alcalase, and fungal protease (PubMed:24499064). CC {ECO:0000269|PubMed:18996574, ECO:0000269|PubMed:23426933, CC ECO:0000269|PubMed:27620509, ECO:0000269|PubMed:30139257, CC ECO:0000269|PubMed:30300740, ECO:0000303|PubMed:24499064}. CC -!- BIOTECHNOLOGY: Emulsification efficiency of glycinin is improved CC by degree-dependent glycation with soy soluble polysaccharide CC (SSPS) at 60 degrees Celsius in both the acidic (A) and basic (B) CC polypeptides as a result of subunit dissociation at the quaternary CC level (PubMed:30372068). Thermal treatment of soybean seed CC proteins leads to the aggregation of glycinin acidic and basic CC polypeptides (GAP and GBP, respectively) (PubMed:10867183, CC PubMed:25801436). GBP improve sensory properties of meat (e.g. CC pork) during chilled storage and inhibit bacterial growth (e.g. CC L.monocytogenes, B.subtilis, E.coli and S.enteritidis) CC (PubMed:30263339, PubMed:22236762). Antibacterial properties of CC the GBP antimicrobial peptides (AMPs) associated with no CC cytotoxicity on the viability of human embryonic kidney cells make CC them promising candidates as natural antibacterial agents CC (PubMed:22236762, Ref.12, PubMed:28590128). Fragmented peptides CC resulting from gastrointestinal digestion of germinated soybeans CC seem to have anticancer and antiinflammatory actions on human CC colon cancer cells (e.g. Caco-2, HT-29, and HCT-116) and CC macrophages (LPS-stimulated RAW 264.7) (PubMed:29037738). Such CC peptides resulting from digested germinated soybeans exhibit also CC anti-diabetic potential by inhibiting dipeptidyl peptidase IV CC (DPP-IV), salivary alpha-amylase and intestinal alpha-glucosidase CC enzymes (PubMed:30249015). {ECO:0000269|PubMed:10867183, CC ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:25801436, CC ECO:0000269|PubMed:28590128, ECO:0000269|PubMed:29037738, CC ECO:0000269|PubMed:30249015, ECO:0000269|PubMed:30263339, CC ECO:0000269|PubMed:30372068, ECO:0000269|Ref.12}. CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) CC family. {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 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; ENOG410IHSE; Eukaryota. DR eggNOG; ENOG410YATH; LUCA. DR InParanoid; P11828; -. DR OMA; SQNECQI; -. 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; Complete proteome; Disulfide bond; KW Endoplasmic reticulum; Reference proteome; Seed storage protein; KW Signal; Storage protein; Vacuole. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 296 Glycinin A1b subunit. FT /FTId=PRO_0000032017. FT CHAIN 297 476 Glycinin B2 subunit. FT /FTId=PRO_0000032018. FT PROPEP 477 481 FT /FTId=PRO_0000032019. FT DOMAIN 36 240 Cupin type-1 1. {ECO:0000255}. FT DOMAIN 309 458 Cupin type-1 2. {ECO:0000255}. FT MOTIF 472 481 Vacuolar targeting signal. FT {ECO:0000250|UniProtKB:P04776}. FT COMPBIAS 169 210 Gln-rich. {ECO:0000255|PROSITE- FT ProRule:PRU00006}. FT COMPBIAS 245 250 Poly-Glu. {ECO:0000255}. FT DISULFID 31 64 {ECO:0000250|UniProtKB:P04776}. FT DISULFID 107 303 Interchain (between A and B chains). FT {ECO:0000250|UniProtKB:P04776}. FT VAR_SEQ 72 75 CTLN -> YTLI (in isoform 2). FT /FTId=VSP_060144. FT CONFLICT 42 42 D -> G (in Ref. 3; BAC55938/BAC55937). FT {ECO:0000305}. FT CONFLICT 97 97 S -> N (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 145 145 F -> L (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 156 156 P -> L (in Ref. 3; BAC55938/BAC55937). FT {ECO:0000305}. FT CONFLICT 162 162 L -> I (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 168 169 FQ -> LE (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 186 186 E -> Q (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 194 194 P -> S (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 219 219 I -> M (in Ref. 3; BAC55938/BAC55937). FT {ECO:0000305}. FT CONFLICT 238 238 I -> IV (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 258 258 K -> R (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 271 272 QQ -> RR (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 306 306 R -> G (in Ref. 3; BAC55938). FT {ECO:0000305}. FT CONFLICT 399 399 I -> T (in Ref. 3; BAC55938). FT {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 //