ID GLYG1_SOYBN Reviewed; 495 AA. AC P04776; C7EA91; C7EA92; DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1989, sequence version 2. DT 02-SEP-2026, entry version 159. DE RecName: Full=Glycinin G1 {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:2485233}; DE Short=Glycinin 11S G1 {ECO:0000305}; DE Short=Glycinin A1aB1b {ECO:0000303|PubMed:23908048}; DE AltName: Allergen=Gly m 6 {ECO:0000305}; DE Contains: DE RecName: Full=Glycinin A1a subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048}; DE Short=Glycinin acidic 1a subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048}; DE Contains: DE RecName: Full=Glycinin Bx subunit {ECO:0000303|PubMed:17524657}; DE Short=Glycinin basic x subunit {ECO:0000303|PubMed:17524657}; DE AltName: Full=Glycinin B1b subunit {ECO:0000303|PubMed:23908048}; DE Short=Glycinin basic 1b subunit {ECO:0000303|PubMed:23908048}; DE Flags: Precursor; GN Name=GY1 {ECO:0000303|PubMed:2485233}; GN OrderedLocusNames=Glyma03g32030 {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, FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND RP GENE FAMILY. RC STRAIN=cv. Dare; TISSUE=Leaf; 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 [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Dare; TISSUE=Leaf; RX PubMed=2740229; DOI=10.1093/nar/17.11.4386; RA Sims T.L., Goldberg R.B.; RT "The glycinin Gy1 gene from soybean."; RL Nucleic Acids Res. 17:4386-4386(1989). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Bonminori; RX PubMed=2997720; DOI=10.1093/nar/13.18.6719; RA Negoro T., Momma T., Fukazawa C.; RT "A cDNA clone encoding a glycinin A1a subunit precursor of soybean."; RL Nucleic Acids Res. 13:6719-6731(1985). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX AGRICOLA=ADL87040545; DOI=10.1021/jf00074a011; RA Utsumi S., Kohno M., Mori T., Kito M.; RT "An alternate cDNA encoding glycinin A1a Bx subunit."; RL J. Agric. Food Chem. 35:210-214(1987). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=cv. Jack; RX PubMed=17181539; DOI=10.1111/j.1742-4658.2006.05613.x; RA Wadahama H., Kamauchi S., Ishimoto M., Kawada T., Urade R.; RT "Protein disulfide isomerase family proteins involved in soybean protein RT biogenesis."; RL FEBS J. 274:687-703(2007). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 2). RC STRAIN=cv. Guiyangzijindou; RA Liu Z., Liu C., Ma H.; RT "Identification and inheritance of A1aB1b-subunit deficiency of storage RT protein in soybean (Glycine max L. Merrill)."; RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [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 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] RP RETRACTED PAPER. 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 [15] RP RETRACTION NOTICE OF PUBMED:22236762. RX PubMed=40912968; DOI=10.1016/j.ijfoodmicro.2025.111411; RA Sitohy M.Z., Mahgoub S.A., Osman A.O.; RL Int. J. Food Microbiol. 443:111411-111411(2025). RN [16] RP FUNCTION. 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] RP SUBCELLULAR LOCATION, AND INTERACTION WITH VSR. RX PubMed=29348620; DOI=10.1038/s41598-017-18697-w; RA Maruyama N., Matsuoka Y., Yokoyama K., Takagi K., Yamada T., Hasegawa H., RA Terakawa T., Ishimoto M.; RT "A vacuolar sorting receptor-independent sorting mechanism for storage RT vacuoles in soybean seeds."; RL Sci. Rep. 8:1108-1108(2018). RN [26] RP ALLERGEN. RX PubMed=30078589; DOI=10.1016/j.vetimm.2018.06.003; RA Zheng S., Qin G., Chen J., Zhang F.; RT "Acidic polypeptides A1a, A3 and A4 of Gly m 6 (glycinin) are allergenic RT for piglets."; RL Vet. Immunol. Immunopathol. 202:147-152(2018). RN [27] 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). RN [28] RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 20-495, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=11124907; DOI=10.1006/jmbi.2000.4310; RA Adachi M., Takenaka Y., Gidamis A.B., Mikami B., Utsumi S.; RT "Crystal structure of soybean proglycinin A1aB1b homotrimer."; RL J. Mol. Biol. 305:291-305(2001). RN [29] RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 20-495, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=14705889; DOI=10.1021/jf026065y; RA Adachi M., Okuda E., Kaneda Y., Hashimoto A., Shutov A.D., Becker C., RA Muntz K., Utsumi S.; RT "Crystal structures and structural stabilities of the disulfide bond- RT deficient soybean proglycinin mutants C12G and C88S."; RL J. Agric. Food Chem. 51:4633-4639(2003). 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 E.coli by CC forming pores and aggregating in membranes, leading to membrane CC permeability and, eventually, cell death (PubMed:28590128, Ref.16). CC {ECO:0000269|PubMed:2485233, ECO:0000269|PubMed:28590128, CC ECO:0000269|Ref.16}. 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 (PubMed:11124907, PubMed:14705889). Interacts with the vacuolar-sorting CC receptor VSR via its vacuolar targeting signal (PubMed:29348620). CC {ECO:0000269|PubMed:11124907, ECO:0000269|PubMed:14705889, CC ECO:0000269|PubMed:29348620}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000269|PubMed:29348620}. Protein storage vacuole CC {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the CC endoplasmic reticulum and later sorted to the protein storage vacuoles. CC {ECO:0000269|PubMed:29348620}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=P04776-1; Sequence=Displayed; CC Name=2; CC IsoId=P04776-2; Sequence=VSP_060142, VSP_060143; CC -!- TISSUE SPECIFICITY: Exclusively in seeds during embryogenesis. CC {ECO:0000269|PubMed:22245912, ECO:0000269|PubMed:2485233}. CC -!- DEVELOPMENTAL STAGE: Accumulates early during embryogenesis, but CC repressed late in seed development (PubMed:2485233). Progressive level CC increase from pod to full-size seed growth (PubMed:22245912). CC {ECO:0000269|PubMed:22245912, ECO:0000269|PubMed:2485233}. CC -!- PTM: During soybean germination, seed storage proteins are hydrolyzed CC by protease/26S proteasome. {ECO:0000269|PubMed:29037738}. CC -!- PTM: The precursor is post-translationally processed to form a CC covalently linked A1a-Bx subunit complex. 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:23426933, PubMed:24499064, PubMed:30078589). CC Binds to IgE of patients with severe allergic reactions (anaphylaxis) CC to soybean (PubMed:18996574). Allergy to soybean is most common for CC infants (usually appears at the age of three months) which frequently CC outgrow their soybean allergy by the age of two, but a severe soybean CC allergy can last a lifetime; various symptoms involve skin, CC gastrointestinal tract and respiratory tracts (PubMed:24499064). CC Damaged intestinal function in piglets is associated with glycinin- CC mediated perturbation of NF-kappa-B, 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:30078589, ECO:0000269|PubMed:30139257, CC ECO:0000269|PubMed:30300740, 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. E.coli)(PubMed:30263339). 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:28590128). CC Fragmented peptides resulting from gastrointestinal digestion of CC germinated soybeans seem to have anticancer and anti-inflammatory CC actions on human colon cancer cells (e.g. Caco-2, HT-29, and HCT-116) CC and macrophages (LPS-stimulated RAW 264.7) (PubMed:29037738). Such CC peptides resulting from digested germinated soybeans exhibit also anti- CC diabetic potential by inhibiting dipeptidyl peptidase IV (DPP-IV), CC salivary alpha-amylase and intestinal alpha-glucosidase enzymes CC (PubMed:30249015). {ECO:0000269|PubMed:10867183, 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 -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family. CC {ECO:0000305}. CC -!- CAUTION: Has previously been shown to disrupt the membrane integrity CC and inhibit growth of L.monocytogenes, B.subtilis and S.enteritidis. CC The publication was retracted due to suspected image manipulation. CC {ECO:0000305|PubMed:22236762, ECO:0000305|PubMed:40912968}. CC -!- SEQUENCE CAUTION: CC Sequence=ACT53400.1; Type=Erroneous gene model prediction; Evidence={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; X15121; CAA33215.1; -; Genomic_DNA. DR EMBL; X02985; CAA26723.1; -; mRNA. DR EMBL; M36686; AAA33966.1; -; mRNA. DR EMBL; AB113349; BAC78522.1; -; mRNA. DR EMBL; GQ259738; ACT53400.1; ALT_SEQ; Genomic_DNA. DR EMBL; GQ259739; ACT53401.1; -; mRNA. DR PIR; A23497; FWSYG2. DR PIR; S10851; S10851. DR RefSeq; NP_001235827.2; NM_001248898.3. [P04776-1] DR PDB; 1FXZ; X-ray; 2.80 A; A/B/C=20-495. DR PDB; 1UCX; X-ray; 3.20 A; A/B/C=20-495. DR PDB; 1UD1; X-ray; 3.10 A; A/B/C=20-495. DR AlphaFoldDB; P04776; -. DR SMR; P04776; -. DR FunCoup; P04776; 742. DR STRING; 3847.P04776; -. DR Allergome; 1142; Gly m 6.0101. DR Allergome; 5821; Gly m 6. DR PaxDb; 3847-P04776; -. DR EnsemblPlants; KRH67385; KRH67385; GLYMA_03G163500. [P04776-1] DR EnsemblPlants; KRH67386; KRH67386; GLYMA_03G163500. [P04776-1] DR GeneID; 547901; -. DR Gramene; KRH67385; KRH67385; GLYMA_03G163500. DR Gramene; KRH67386; KRH67386; GLYMA_03G163500. DR KEGG; gmx:547901; -. DR eggNOG; ENOG502QU1J; Eukaryota. DR HOGENOM; CLU_026341_2_0_1; -. DR InParanoid; P04776; -. DR OrthoDB; 1389300at2759; -. DR EvolutionaryTrace; P04776; -. DR PRO; PR:P04776; -. DR Proteomes; UP000008827; Chromosome 3. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB. DR GO; GO:0000326; C:protein storage vacuole; IDA:UniProtKB. DR GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro. DR CDD; cd02243; cupin_11S_legumin_C; 1. DR CDD; cd02242; cupin_11S_legumin_N; 1. DR FunFam; 2.60.120.10:FF:000073; Glycinin G1; 1. DR FunFam; 2.60.120.10:FF:000124; Glycinin G5; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 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 InterPro; IPR050253; Seed_Storage-Functional. DR PANTHER; PTHR31189:SF77; GLYCININ G3; 1. DR PANTHER; PTHR31189; OS03G0336100 PROTEIN-RELATED; 1. DR Pfam; PF00190; Cupin_1; 2. DR PRINTS; PR00439; 11SGLOBULIN. DR SMART; SM00835; Cupin_1; 2. DR SUPFAM; SSF51182; RmlC-like cupins; 1. DR PROSITE; PS00305; 11S_SEED_STORAGE; 1. DR PDBsum; 1FXZ; -. DR PDBsum; 1UCX; -. DR PDBsum; 1UD1; -. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Alternative splicing; Disulfide bond; KW Endoplasmic reticulum; Reference proteome; Seed storage protein; Signal; KW Storage protein; Vacuole. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..306 FT /note="Glycinin A1a subunit" FT /id="PRO_0000032009" FT PROPEP 307..310 FT /id="PRO_0000032010" FT CHAIN 311..490 FT /note="Glycinin Bx subunit" FT /id="PRO_0000032011" FT PROPEP 491..495 FT /id="PRO_0000032012" FT DOMAIN 36..241 FT /note="Cupin type-1 1" FT /evidence="ECO:0000255" FT DOMAIN 323..472 FT /note="Cupin type-1 2" FT /evidence="ECO:0000255" FT REGION 196..217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 260..312 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 486..495 FT /note="Vacuolar targeting signal" FT /evidence="ECO:0000269|PubMed:29348620" FT COMPBIAS 268..277 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 287..297 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 31..64 FT /evidence="ECO:0000269|PubMed:11124907, FT ECO:0000269|PubMed:14705889, ECO:0007744|PDB:1FXZ, FT ECO:0007744|PDB:1UD1" FT DISULFID 107..317 FT /note="Interchain (between A1a and Bx chains)" FT /evidence="ECO:0000269|PubMed:11124907, FT ECO:0000269|PubMed:14705889, ECO:0007744|PDB:1FXZ, FT ECO:0007744|PDB:1UCX" FT VAR_SEQ 369..386 FT /note="MFVPHYNLNANSIIYALN -> EEAKAKAEEMALTRPYAP (in isoform FT 2)" FT /id="VSP_060142" FT VAR_SEQ 387..495 FT /note="Missing (in isoform 2)" FT /id="VSP_060143" FT CONFLICT 42 FT /note="D -> G (in Ref. 3; CAA26723)" FT /evidence="ECO:0000305" FT CONFLICT 108 FT /note="P -> S (in Ref. 3; CAA26723)" FT /evidence="ECO:0000305" FT CONFLICT 136 FT /note="F -> S (in Ref. 3; CAA26723)" FT /evidence="ECO:0000305" FT CONFLICT 146 FT /note="T -> A (in Ref. 6; ACT53401)" FT /evidence="ECO:0000305" FT CONFLICT 216 FT /note="E -> G (in Ref. 6; ACT53401)" FT /evidence="ECO:0000305" FT CONFLICT 360 FT /note="E -> G (in Ref. 3; CAA26723)" FT /evidence="ECO:0000305" FT STRAND 44..47 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 50..54 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 60..65 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 68..74 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 78..87 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 89..95 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 98..103 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 133..136 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 140..144 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 149..154 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 156..158 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 160..166 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 181..187 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 193..196 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 220..223 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 226..229 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 230..234 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 237..243 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 254..257 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 322..324 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 326..329 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 332..335 FT /evidence="ECO:0007829|PDB:1FXZ" FT TURN 336..338 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 339..344 FT /evidence="ECO:0007829|PDB:1FXZ" FT TURN 346..348 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 350..352 FT /evidence="ECO:0007829|PDB:1FXZ" FT TURN 353..356 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 359..364 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 369..375 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 380..394 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 400..407 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 411..414 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 419..424 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 429..439 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 442..447 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 452..454 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 457..464 FT /evidence="ECO:0007829|PDB:1FXZ" FT HELIX 468..476 FT /evidence="ECO:0007829|PDB:1FXZ" FT STRAND 481..484 FT /evidence="ECO:0007829|PDB:1FXZ" SQ SEQUENCE 495 AA; 55706 MW; 329CB0545B24D894 CRC64; MAKLVFSLCF LLFSGCCFAF SSREQPQQNE CQIQKLNALK PDNRIESEGG LIETWNPNNK PFQCAGVALS RCTLNRNALR RPSYTNGPQE IYIQQGKGIF GMIYPGCPST FEEPQQPQQR GQSSRPQDRH QKIYNFREGD LIAVPTGVAW WMYNNEDTPV VAVSIIDTNS LENQLDQMPR RFYLAGNQEQ EFLKYQQEQG GHQSQKGKHQ QEEENEGGSI LSGFTLEFLE HAFSVDKQIA KNLQGENEGE DKGAIVTVKG GLSVIKPPTD EQQQRPQEEE EEEEDEKPQC KGKDKHCQRP RGSQSKSRRN GIDETICTMR LRHNIGQTSS PDIYNPQAGS VTTATSLDFP ALSWLRLSAE FGSLRKNAMF VPHYNLNANS IIYALNGRAL IQVVNCNGER VFDGELQEGR VLIVPQNFVV AARSQSDNFE YVSFKTNDTP MIGTLAGANS LLNALPEEVI QHTFNLKSQQ ARQIKNNNPF KFLVPPQESQ KRAVA //