GLYG5_SOYBN
ID GLYG5_SOYBN Reviewed; 516 AA.
AC P04347; C0KG62; C6T7B0; P93707; P93708; Q7GC77; Q9SB12;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-1987, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glycinin G5 {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:2485233};
DE Short=Glycinin 11S G5 {ECO:0000303|PubMed:27612614};
DE Short=Glycinin A3B4 {ECO:0000303|PubMed:23908048};
DE AltName: Allergen=Gly m 6 {ECO:0000305};
DE Contains:
DE RecName: Full=Glycinin A3 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048};
DE Contains:
DE RecName: Full=Glycinin B4 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048};
DE Flags: Precursor;
GN Name=GY5 {ECO:0000303|PubMed:2485233};
GN OrderedLocusNames=Glyma13g18450 {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 (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND GENE FAMILY.
RC STRAIN=cv. Dare; TISSUE=Leaf;
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Bonminori; TISSUE=Cotyledon;
RX PubMed=3838983; DOI=10.1016/s0021-9258(18)88962-1;
RA Fukazawa C., Momma T., Hirano H., Harada K., Udaka K.;
RT "Glycinin A3B4 mRNA. Cloning and sequencing of double-stranded cDNA
RT complementary to a soybean storage protein.";
RL J. Biol. Chem. 260:6234-6239(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Bonminori;
RA Fukazawa C.;
RT "Glycine max mRNA for glycinin.";
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Williams 82; TISSUE=Leaf;
RA Chen S., Arahira M., Fukazawa C.;
RT "cloning of A3B4 glycinin gene from soybean.";
RL Submitted (MAY-1997) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC STRAIN=cv. Wasesuzunari; TISSUE=Cotyledon;
RA Adachi M., Katsube T., Masuda T., Utsumi S.;
RT "cDNA of Glycinin A3B4 Subunit.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=cv. Heidou No.1;
RA Liu Z., Wang H., Ma H.;
RT "The molecule mechanism of mutant soybean cultivars lacking the glycinin
RT A3B4 subunit.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-429 (ISOFORM 1/2).
RA Cheung F., Xiao Y., Chan A., Moskal W., Town C.D.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
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 [10]
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 [11]
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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
RP BIOTECHNOLOGY.
RX PubMed=27612614; DOI=10.1016/j.peptides.2016.09.004;
RA Xiang N., Lyu Y., Zhu X., Bhunia A.K., Narsimhan G.;
RT "Methodology for identification of pore forming antimicrobial peptides from
RT soy protein subunits beta-conglycinin and glycinin.";
RL Peptides 85:27-40(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.
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 (2.10 ANGSTROMS) OF 26-516, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=12771376; DOI=10.1073/pnas.0832158100;
RA Adachi M., Kanamori J., Masuda T., Yagasaki K., Kitamura K., Mikami B.,
RA Utsumi S.;
RT "Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7395-7400(2003).
RN [29]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 25-516, SUBUNIT, AND DISULFIDE
RP BONDS.
RX PubMed=20215054; DOI=10.1016/j.bbapap.2010.02.016;
RA Tandang-Silvas M.R.G., Fukuda T., Fukuda C., Prak K., Cabanos C.,
RA Kimura A., Itoh T., Mikami B., Utsumi S., Maruyama N.;
RT "Conservation and divergence on plant seed 11S globulins based on crystal
RT structures.";
RL Biochim. Biophys. Acta 1804:1432-1442(2010).
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.15, PubMed:28590128).
CC {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233,
CC ECO:0000269|PubMed:28590128, ECO:0000269|Ref.15}.
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:0000269|PubMed:12771376, ECO:0000269|PubMed:20215054}.
CC -!- SUBCELLULAR LOCATION: Vacuole, aleurone grain. 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 (PubMed:29348620). Cotyledonary membrane-bound vacuolar protein bodies.
CC {ECO:0000269|PubMed:29348620}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04347-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04347-2; Sequence=VSP_060146;
CC -!- TISSUE SPECIFICITY: Exclusively in seeds during embryogenesis.
CC {ECO:0000269|PubMed:2485233}.
CC -!- DEVELOPMENTAL STAGE: Accumulates early during embryogenesis, but
CC repressed late in seed development. {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:24499064, PubMed:23426933, 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. 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.15, PubMed:28590128). The commercially synthesized peptide G5466
CC (250-269) exhibits antimicrobial activity toward L.monocytogenes and
CC E.coli probably by forming pores and aggregating in transmembranes,
CC thus being a promising candidate as a natural antibacterial agent
CC (PubMed:27612614). Fragmented peptides resulting from gastrointestinal
CC digestion of germinated soybeans seem to have anticancer and anti-
CC inflammatory actions on human colon cancer cells (e.g. Caco-2, HT-29,
CC and HCT-116) and macrophages (LPS-stimulated RAW 264.7)
CC (PubMed:29037738). Such peptides resulting from digested germinated
CC soybeans exhibit also anti-diabetic potential by inhibiting dipeptidyl
CC peptidase IV (DPP-IV), salivary alpha-amylase and intestinal alpha-
CC glucosidase enzymes (PubMed:30249015). {ECO:0000269|PubMed:10867183,
CC ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:25801436,
CC ECO:0000269|PubMed:27612614, 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.15}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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DR EMBL; M10962; AAA33964.1; -; mRNA.
DR EMBL; AB000168; BAA19058.1; -; mRNA.
DR EMBL; AB000169; BAA19059.1; -; mRNA.
DR EMBL; AB003680; BAA74952.1; -; Genomic_DNA.
DR EMBL; AB049440; BAB15802.1; -; mRNA.
DR EMBL; FJ599666; ACN11532.1; -; mRNA.
DR EMBL; BT093334; ACU17712.1; -; mRNA.
DR PIR; A92524; FWSYG3.
DR PIR; PQ0200; PQ0200.
DR PIR; PQ0806; PQ0806.
DR PIR; PQ0807; PQ0807.
DR PIR; PQ0808; PQ0808.
DR RefSeq; NP_001236676.1; NM_001249747.2.
DR PDB; 1OD5; X-ray; 2.10 A; A/B=26-516.
DR PDB; 2D5F; X-ray; 1.90 A; A/B=25-516.
DR PDB; 2D5H; X-ray; 2.80 A; A/B/C/D/E/F=25-516.
DR PDBsum; 1OD5; -.
DR PDBsum; 2D5F; -.
DR PDBsum; 2D5H; -.
DR AlphaFoldDB; P04347; -.
DR SMR; P04347; -.
DR STRING; 3847.GLYMA13G18450.2; -.
DR Allergome; 5821; Gly m 6.
DR Allergome; 5826; Gly m 6.0501.
DR TCDB; 1.C.121.1.2; the soybean glycinin-derived pore-forming peptide (sgpp) family.
DR PRIDE; P04347; -.
DR GeneID; 547452; -.
DR KEGG; gmx:547452; -.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR OrthoDB; 603461at2759; -.
DR EvolutionaryTrace; P04347; -.
DR Proteomes; UP000008827; Unplaced.
DR GO; GO:0033095; C:aleurone grain; IEA:UniProtKB-SubCell.
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: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 3D-structure; Allergen; Alternative splicing; Disulfide bond;
KW Endoplasmic reticulum; Glycoprotein; Reference proteome;
KW Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..344
FT /note="Glycinin A3 subunit"
FT /id="PRO_0000032023"
FT CHAIN 345..516
FT /note="Glycinin B4 subunit"
FT /id="PRO_0000032024"
FT DOMAIN 38..249
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 357..502
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 113..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 244..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 318..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 33..66
FT /evidence="ECO:0000269|PubMed:12771376"
FT DISULFID 109..351
FT /note="Interchain (between A3 and B4 chains)"
FT /evidence="ECO:0000269|PubMed:12771376"
FT VAR_SEQ 516
FT /note="P -> PQITTSIYEGVVRPSYMK (in isoform 2)"
FT /id="VSP_060146"
FT CONFLICT 81
FT /note="S -> L (in Ref. 4; BAA74952, 5; BAB15802, 7;
FT ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 87
FT /note="L -> S (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802, 7; ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="A -> E (in Ref. 3; BAA19059)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="L -> P (in Ref. 4; BAA74952, 5; BAB15802, 7;
FT ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 170
FT /note="P -> L (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802, 7; ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..221
FT /note="RQQ -> QQP (in Ref. 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="R -> Q (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802 and 7; ACU17712)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="G -> R (in Ref. 7; ACU17712)"
FT /evidence="ECO:0000305"
FT CONFLICT 290..291
FT /note="GR -> EQ (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802, 7; ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 315
FT /note="E -> G (in Ref. 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="E -> G (in Ref. 7; ACU17712)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="D -> H (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802, 7; ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 416..417
FT /note="TM -> IYV (in Ref. 3; BAA19058/BAA19059, 4;
FT BAA74952, 5; BAB15802, 7; ACU17712 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 451..452
FT /note="PA -> FV (in Ref. 3; BAA19058/BAA19059, 4; BAA74952,
FT 5; BAB15802 and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="V -> A (in Ref. 3; BAA19058/BAA19059, 5; BAB15802
FT and 6; ACN11532)"
FT /evidence="ECO:0000305"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 62..67
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 70..76
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 80..86
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 91..97
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 99..104
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 113..115
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 138..142
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 155..159
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 187..191
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 234..240
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:2D5F"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:2D5H"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 366..369
FT /evidence="ECO:0007829|PDB:2D5F"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:2D5F"
FT TURN 380..382
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 386..389
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 392..398
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 403..411
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 414..427
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 444..447
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 452..470
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 475..477
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 478..484
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 487..494
FT /evidence="ECO:0007829|PDB:2D5F"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:2D5F"
FT STRAND 510..514
FT /evidence="ECO:0007829|PDB:2D5F"
SQ SEQUENCE 516 AA; 57956 MW; FE464753A8D20715 CRC64;
MGKPFFTLSL SSLCLLLLSS ACFAITSSKF NECQLNNLNA LEPDHRVESE GGLIETWNSQ
HPELQCAGVT VSKRTLNRNG SHLPSYLPYP QMIIVVQGKG AIGFAFPGCP ETFEKPQQQS
SRRGSRSQQQ LQDSHQKIRH FNEGDVLVIP LGVPYWTYNT GDEPVVAISP LDTSNFNNQL
DQNPRVFYLA GNPDIEHPET MQQQQQQKSH GGRKQGQHRQ QEEEGGSVLS GFSKHFLAQS
FNTNEDTAEK LRSPDDERKQ IVTVEGGLSV ISPKWQEQED EDEDEDEEYG RTPSYPPRRP
SHGKHEDDED EDEEEDQPRP DHPPQRPSRP EQQEPRGRGC QTRNGVEENI CTMKLHENIA
RPSRADFYNP KAGRISTLNS LTLPALRQFG LSAQYVVLYR NGIYSPDWNL NANSVTMTRG
KGRVRVVNCQ GNAVFDGELR RGQLLVVPQN PAVAEQGGEQ GLEYVVFKTH HNAVSSYIKD
VFRVIPSEVL SNSYNLGQSQ VRQLKYQGNS GPLVNP
