ID GLYG4_SOYBN Reviewed; 563 AA. AC P02858; Q43452; Q9S9D0; Q9SB11; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 08-MAY-2019, sequence version 2. DT 04-NOV-2026, entry version 149. DE RecName: Full=Glycinin G4 {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:2485233}; DE Short=Glycinin 11S G4 {ECO:0000305}; DE Short=Glycinin A5A4B3 {ECO:0000303|PubMed:23908048}; DE AltName: Allergen=Gly m 6 {ECO:0000305}; DE Contains: DE RecName: Full=Glycinin A5 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048}; DE Contains: DE RecName: Full=Glycinin A4 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048}; DE Contains: DE RecName: Full=Glycinin B3 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048}; DE Flags: Precursor; GN Name=GY4 {ECO:0000303|PubMed:2485233}; GN OrderedLocusNames=Glyma10g04280 {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 [MRNA] (ISOFORM 1). RC STRAIN=cv. Bonminori; RX PubMed=2988947; DOI=10.1111/j.1432-1033.1985.tb08951.x; RA Momma T., Negoro T., Hirano H., Matsumoto A., Udaka K., Fukazawa C.; RT "Glycinin A5A4B3 mRNA: cDNA cloning and nucleotide sequencing of a RT splitting storage protein subunit of soybean."; RL Eur. J. Biochem. 149:491-496(1985). RN [2] RP PROTEIN SEQUENCE (A4/A5 SUBUNITS) (ISOFORM 1). RC STRAIN=cv. Bonminori; RA Hirano H., Fukazawa C., Harada K.; RT "The primary structures of the A4 and A5 subunits are highly homologous to RT that of the A3 subunit in the glycinin seed storage protein of soybean."; RL FEBS Lett. 181:124-128(1985). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM 2), FUNCTION, TISSUE SPECIFICITY, RP DEVELOPMENTAL STAGE, 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 [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=cv. Forrest; TISSUE=Leaf; RX PubMed=1316192; DOI=10.1007/bf00019204; RA Xue Z.-T., Xu M.-L., Shen W., Zhuang N.-L., Hu W.-M., Shen S.C.; RT "Characterization of a Gy4 glycinin gene from soybean Glycine max cv. RT forrest."; RL Plant Mol. Biol. 18:897-908(1992). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC TISSUE=Leaf; RA Chen S., Arahira M., Fukazawa C.; RT "Cloning of A5A4B3 glycinin gene from soybean."; RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RA Prak K., Maruyama N., Utsumi S.; RT "Glycine max glycinin A5A4B3 mRNA."; RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Williams 82; TISSUE=Callus; 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 [8] RP NUCLEOTIDE SEQUENCE [MRNA] OF 181-386 (ISOFORM 1/2). RC STRAIN=cv. CX635-1-1-1; RA Scallon B.J., Dickinson C.D., Nielsen N.C.; RT "Characterization of a null-allele for the Gy4 glycinin gene from RT soybean."; RL Mol. Gen. Genet. 208:107-113(1987). RN [9] 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 [10] 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 [11] 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 [12] 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 [13] 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 [14] 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 [15] 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 [16] 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 [17] 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 [18] 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 [19] 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 [20] 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 [21] 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 [22] 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 [23] 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 [24] 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 [25] 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 [26] 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 [27] 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 [28] 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 E.coli by CC forming pores and aggregating in membranes, leading to membrane CC permeability and, eventually, cell death (PubMed:28590128, Ref.18). CC {ECO:0000269|PubMed:2485233, ECO:0000269|PubMed:28590128, CC ECO:0000269|Ref.18}. 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=P02858-1; Sequence=Displayed; CC Name=2; CC IsoId=P02858-2; Sequence=VSP_060145; 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 -!- 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 nuclear factor-kappa B (NF-kappaB), Jun N- CC terminal kinase (JNK) and p38 levels (PubMed:30139257). Juvenile CC Chinese mitten crabs (E.sinensis) supplemented with glycinin display CC impaired growth and altered intestinal health due to gut inflammation, CC reshaped 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 developed, CC among them physical processing includes extrusion, high-pressure (>300 CC MPa), heating (between 70 and 90 degrees Celsius), roasting, chemical CC processing includes ethanol extraction (55-76 percent between 70 and 80 CC degrees Celsius), in vitro glycation (e.g. with xylose at 55 degrees CC Celsius) and enzymatic hydrolysis with pepsin and trypsin, and CC biological processing includes fermentation with A.oryzae, CC S.cerevisiae, L.lactic subsplactis, B.subtilis, B.lactic and CC L.plantarum (PubMed:24499064, PubMed:27620509). Resistant to hydrolysis CC by papain, alcalase, and fungal protease (PubMed:24499064). CC {ECO:0000269|PubMed:18996574, ECO:0000269|PubMed:23426933, CC ECO:0000269|PubMed:27620509, ECO:0000269|PubMed:30078589, 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. 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 --------------------------------------------------------------------------- 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; X02626; CAA26478.1; -; mRNA. DR EMBL; X52863; CAA37044.1; -; Genomic_DNA. DR EMBL; AB004062; BAA74953.1; -; Genomic_DNA. DR EMBL; AB195712; BAD72975.1; -; mRNA. DR EMBL; CM000843; KRH32185.1; -; Genomic_DNA. DR EMBL; X05652; CAB57802.1; -; mRNA. DR PIR; A91145; FWSYG5. DR PIR; JA0152; JA0152. DR PIR; PQ0199; PQ0199. DR PIR; S11004; S11004. DR PIR; S20946; S20946. DR RefSeq; NP_001238008.1; NM_001251079.2. [P02858-1] DR PDB; 9V45; EM; 3.41 A; A/B/C/D/E/F/G/H/I/J=1-563. DR PDB; 9V4F; EM; 3.52 A; A/B/C/D/E/F/G/H/I/J=1-563. DR AlphaFoldDB; P02858; -. DR EMDB; EMD-64767; -. DR EMDB; EMD-64778; -. DR SMR; P02858; -. DR FunCoup; P02858; 92. DR STRING; 3847.P02858; -. DR Allergome; 2541; Gly m 6.0401. DR Allergome; 5821; Gly m 6. DR PaxDb; 3847-P02858; -. DR EnsemblPlants; KRH32185; KRH32185; GLYMA_10G037100. [P02858-1] DR GeneID; 100101841; -. DR Gramene; KRH32185; KRH32185; GLYMA_10G037100. DR KEGG; gmx:100101841; -. DR eggNOG; ENOG502QU1J; Eukaryota. DR HOGENOM; CLU_026341_2_0_1; -. DR InParanoid; P02858; -. DR OMA; AAQTXTT; -. DR OrthoDB; 1903982at2759; -. DR Proteomes; UP000008827; Chromosome 10. 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; IBA:GO_Central. DR GO; GO:0071215; P:cellular response to abscisic acid stimulus; IBA:GO_Central. DR GO; GO:0010431; P:seed maturation; IBA:GO_Central. 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:SF63; GLYCININ G5; 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. PE 1: Evidence at protein level; KW 3D-structure; Allergen; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Endoplasmic reticulum; Reference proteome; KW Seed storage protein; Signal; Storage protein; Vacuole. FT SIGNAL 1..23 FT /evidence="ECO:0000255" FT CHAIN 24..120 FT /note="Glycinin A5 subunit" FT /id="PRO_0000032020" FT CHAIN 121..378 FT /note="Glycinin A4 subunit" FT /id="PRO_0000032021" FT CHAIN 379..563 FT /note="Glycinin B3 subunit" FT /id="PRO_0000032022" FT DOMAIN 37..250 FT /note="Cupin type-1 1" FT /evidence="ECO:0000255" FT DOMAIN 391..537 FT /note="Cupin type-1 2" FT /evidence="ECO:0000255" FT REGION 108..136 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 199..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 266..375 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 551..563 FT /note="Vacuolar targeting signal" FT /evidence="ECO:0000250|UniProtKB:P04776" FT COMPBIAS 279..294 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 335..346 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 347..356 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 364..375 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 32..65 FT /evidence="ECO:0000250|UniProtKB:P04776" FT DISULFID 108..385 FT /note="Interchain (between A5 and B3 chains)" FT /evidence="ECO:0000250|UniProtKB:P04776" FT VAR_SEQ 533..561 FT /note="QSQVSELKYEGNWGPLVNPESQQGSPRVK -> RQQARQVKNNNPFSFLVPP FT KESQRRV (in isoform 2)" FT /id="VSP_060145" FT CONFLICT 29 FT /note="L -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 48 FT /note="S -> F (in Ref. 4; CAA37044)" FT /evidence="ECO:0000305" FT CONFLICT 82 FT /note="L -> S (in Ref. 1; CAA26478)" FT CONFLICT 86 FT /note="S -> L (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 94 FT /note="I -> V (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 101..103 FT /note="LGV -> IGM (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 102..105 FT /note="GVAI -> QCK (in Ref. 4; CAA37044)" FT /evidence="ECO:0000305" FT CONFLICT 105 FT /note="I -> F (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 117 FT /note="E -> Q (in Ref. 2; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 152 FT /note="G -> S (in Ref. 1; CAA26478 and 2; AA sequence)" FT CONFLICT 253 FT /note="Q -> E (in Ref. 1; CAA26478 and 2; AA sequence)" FT CONFLICT 332..336 FT /note="EQDQD -> NKTG (in Ref. 1; CAA26478 and 2; AA FT sequence)" FT STRAND 166..171 FT /evidence="ECO:0007829|PDB:9V45" FT STRAND 174..177 FT /evidence="ECO:0007829|PDB:9V45" FT STRAND 180..182 FT /evidence="ECO:0007829|PDB:9V45" FT STRAND 185..189 FT /evidence="ECO:0007829|PDB:9V45" SQ SEQUENCE 563 AA; 63797 MW; 4ACC765C55AB9E18 CRC64; MGKPFTLSLS SLCLLLLSSA CFAISSSKLN ECQLNNLNAL EPDHRVESEG GLIQTWNSQH PELKCAGVTV SKLTLNRNGL HLPSYSPYPR MIIIAQGKGA LGVAIPGCPE TFEEPQEQSN RRGSRSQKQQ LQDSHQKIRH FNEGDVLVIP PGVPYWTYNT GDEPVVAISL LDTSNFNNQL DQTPRVFYLA GNPDIEYPET MQQQQQQKSH GGRKQGQHQQ EEEEEGGSVL SGFSKHFLAQ SFNTNEDIAE KLQSPDDERK QIVTVEGGLS VISPKWQEQQ DEDEDEDEDD EDEQIPSHPP RRPSHGKREQ DEDEDEDEDK PRPSRPSQGK REQDQDQDED EDEDEDQPRK SREWRSKKTQ PRRPRQEEPR ERGCETRNGV EENICTLKLH ENIARPSRAD FYNPKAGRIS TLNSLTLPAL RQFQLSAQYV VLYKNGIYSP HWNLNANSVI YVTRGQGKVR VVNCQGNAVF DGELRRGQLL VVPQNFVVAE QAGEQGFEYI VFKTHHNAVT SYLKDVFRAI PSEVLAHSYN LRQSQVSELK YEGNWGPLVN PESQQGSPRV KVA //