GLYG4_SOYBN
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 03-AUG-2022, entry version 132.
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=10.2307/3869011;
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 [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 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 [13]
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 [14]
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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [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).
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.17, PubMed:28590128).
CC {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233,
CC ECO:0000269|PubMed:28590128, ECO:0000269|Ref.17}.
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: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.17, 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.17}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
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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_001235795.1; NM_001248866.1.
DR RefSeq; NP_001238008.1; NM_001251079.1. [P02858-1]
DR AlphaFoldDB; P02858; -.
DR SMR; P02858; -.
DR STRING; 3847.GLYMA10G04280.1; -.
DR Allergome; 2541; Gly m 6.0401.
DR Allergome; 5821; Gly m 6.
DR PRIDE; P02858; -.
DR EnsemblPlants; KRH32185; KRH32185; GLYMA_10G037100. [P02858-1]
DR GeneID; 100101841; -.
DR Gramene; KRH32185; KRH32185; GLYMA_10G037100. [P02858-1]
DR KEGG; gmx:100101841; -.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR InParanoid; P02858; -.
DR OMA; PDNRVES; -.
DR OrthoDB; 603461at2759; -.
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; 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; Direct protein sequencing; Disulfide bond;
KW Endoplasmic reticulum; Reference proteome; Seed storage protein; Signal;
KW 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 265..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 199..213
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..293
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 294..310
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..334
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..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)"
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
