GLYG2_SOYBN
ID GLYG2_SOYBN Reviewed; 485 AA.
AC P04405; P04121; P04348; P04349; Q549Z4;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 2.
DT 25-MAY-2022, entry version 128.
DE RecName: Full=Glycinin G2 {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:2485233};
DE Short=Glycinin 11S G2 {ECO:0000305};
DE Short=Glycinin A2B1a {ECO:0000303|PubMed:23908048};
DE AltName: Allergen=Gly m 6 {ECO:0000305};
DE Contains:
DE RecName: Full=Glycinin A2 subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048};
DE Contains:
DE RecName: Full=Glycinin B1a subunit {ECO:0000303|PubMed:17524657, ECO:0000303|PubMed:23908048};
DE Flags: Precursor;
GN Name=GY2 {ECO:0000303|PubMed:2485233};
GN OrderedLocusNames=Glyma03g32020 {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=10.2307/3869011;
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 [GENOMIC DNA].
RC STRAIN=cv. Dare; TISSUE=Leaf;
RX PubMed=2740230; DOI=10.1093/nar/17.11.4387;
RA Thanh V.H., Tumer N.E., Nielsen N.C.;
RT "The glycinin Gy2 gene from soybean.";
RL Nucleic Acids Res. 17:4387-4387(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Shirotsurunoko;
RA Utsumi S., Kim C.S., Kohno M., Kito M.;
RT "Polymorphism and expression of cDNAs encoding glycinin subunits.";
RL Agric. Biol. Chem. 51:3267-3273(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3671077; DOI=10.1093/nar/15.19.8117;
RA Fukazawa C., Momma T., Higuchi W., Udaka K.;
RT "Complete nucleotide sequence of the gene encoding a glycinin A2B1a subunit
RT precursor of soybean.";
RL Nucleic Acids Res. 15:8117-8117(1987).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Momma T., Negoro T., Udaka K., Fukazawa C.;
RT "A complete cDNA coding for the sequence of glycinin A2B1a subunit
RT precursor.";
RL FEBS Lett. 188:117-122(1985).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=cv. Jack;
RA Urade R., Nakatani H.;
RT "mRNA of Soybean Proglycinin A2B1 Subunit.";
RL Submitted (JUN-2003) 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 PROTEIN SEQUENCE OF 19-296 AND 301-480 (A2 AND B1A SUBUNITS).
RX PubMed=6541652; DOI=10.1016/s0021-9258(18)90711-8;
RA Staswick P.E., Hermodson M.A., Nielsen N.C.;
RT "The amino acid sequence of the A2B1a subunit of glycinin.";
RL J. Biol. Chem. 259:13424-13430(1984).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 262-485.
RX PubMed=6092376; DOI=10.1016/s0021-9258(18)90713-1;
RA Marco Y.A., Thanh V.H., Tumer N.E., Scallon B.J., Nielsen N.C.;
RT "Cloning and structural analysis of DNA encoding an A2B1a subunit of
RT glycinin.";
RL J. Biol. Chem. 259:13436-13441(1984).
RN [10] {ECO:0000312|EMBL:CAA37480.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-36.
RX PubMed=2377465; DOI=10.1093/nar/18.14.4245;
RA Kitamura Y., Arahira M., Itoh Y., Fukazawa C.;
RT "The complete nucleotide sequence of soybean glycinin A2B1a gene spanning
RT to another glycinin gene A1aB1b.";
RL Nucleic Acids Res. 18:4245-4245(1990).
RN [11]
RP PROTEIN SEQUENCE OF 115-136 AND 202-224 (A2 SUBUNIT).
RC STRAIN=cv. Kishinevskaya-16;
RX PubMed=8898910; DOI=10.1111/j.1432-1033.1996.0221t.x;
RA Shutov A.D., Kakhovskaya I.A., Bastrygina A.S., Bulmaga V.P., Horstmann C.,
RA Muntz K.;
RT "Limited proteolysis of beta-conglycinin and glycinin, the 7S and 11S
RT storage globulins from soybean [Glycine max (L.) Merr.]. Structural and
RT evolutionary implications.";
RL Eur. J. Biochem. 241:221-228(1996).
RN [12]
RP DISULFIDE BOND.
RX PubMed=6541653; DOI=10.1016/s0021-9258(18)90712-x;
RA Staswick P.E., Hermodson M.A., Nielsen N.C.;
RT "Identification of the cystines which link the acidic and basic components
RT of the glycinin subunits.";
RL J. Biol. Chem. 259:13431-13435(1984).
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 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 [15]
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 [16]
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 [17]
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 [18]
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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 [29]
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 [30]
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.21, PubMed:28590128).
CC {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233,
CC ECO:0000269|PubMed:28590128, ECO:0000269|Ref.21}.
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 -!- 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). Binds to IgE of
CC patients with severe allergic reactions (anaphylaxis) to soybean
CC (PubMed:18996574). Allergy to soybean is most common for infants
CC (usually appears at the age of three months) which frequently outgrow
CC their soybean allergy by the age of two, but a severe soybean allergy
CC can last a lifetime; various symptoms involve skin, gastrointestinal
CC tract and respiratory tracts (PubMed:24499064). Damaged intestinal
CC function in piglets is associated with glycinin-mediated perturbation
CC of nuclear factor-kappa B (NF-kappaB), 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: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.21, 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.21}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {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; X15122; CAA33216.1; -; Genomic_DNA.
DR EMBL; D00216; BAA00154.1; -; mRNA.
DR EMBL; Y00398; CAA68460.1; -; Genomic_DNA.
DR EMBL; X02806; CAA26575.1; -; mRNA.
DR EMBL; AB113350; BAC78523.1; -; mRNA.
DR EMBL; CM000836; KRH67383.1; -; Genomic_DNA.
DR EMBL; K02646; AAA33963.1; -; Genomic_DNA.
DR EMBL; X53404; CAA37480.1; -; Genomic_DNA.
DR PIR; A91341; FWSYG1.
DR PIR; S11002; S11002.
DR RefSeq; NP_001235810.1; NM_001248881.1.
DR AlphaFoldDB; P04405; -.
DR SMR; P04405; -.
DR Allergome; 1143; Gly m 6.0201.
DR Allergome; 5821; Gly m 6.
DR PRIDE; P04405; -.
DR EnsemblPlants; KRH67383; KRH67383; GLYMA_03G163500.
DR GeneID; 547900; -.
DR Gramene; KRH67383; KRH67383; GLYMA_03G163500.
DR KEGG; gmx:547900; -.
DR InParanoid; P04405; -.
DR OMA; QRPSWET; -.
DR OrthoDB; 603461at2759; -.
DR Proteomes; UP000008827; Chromosome 3.
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; Direct protein sequencing; Disulfide bond; Endoplasmic reticulum;
KW Reference proteome; Seed storage protein; Signal; Storage protein; Vacuole.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:6541652"
FT CHAIN 19..296
FT /note="Glycinin A2 subunit"
FT /id="PRO_0000032013"
FT PROPEP 297..300
FT /evidence="ECO:0000269|PubMed:6541652"
FT /id="PRO_0000032014"
FT CHAIN 301..480
FT /note="Glycinin B1a subunit"
FT /id="PRO_0000032015"
FT PROPEP 481..485
FT /id="PRO_0000032016"
FT DOMAIN 33..238
FT /note="Cupin type-1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 313..462
FT /note="Cupin type-1 2"
FT /evidence="ECO:0000255"
FT REGION 108..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 476..485
FT /note="Vacuolar targeting signal"
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT COMPBIAS 284..298
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 28..61
FT /evidence="ECO:0000250|UniProtKB:P04776"
FT DISULFID 104..307
FT /note="Interchain (between A2 and B1a chains)"
FT /evidence="ECO:0000269|PubMed:6541653"
FT VARIANT 103
FT /note="G -> D"
FT VARIANT 318
FT /note="N -> T"
FT VARIANT 331
FT /note="I -> V"
FT VARIANT 413
FT /note="K -> R"
FT CONFLICT 39
FT /note="D -> G (in Ref. 5; CAA26575)"
FT /evidence="ECO:0000305"
FT CONFLICT 39
FT /note="D -> N (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="C -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="R -> C (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="W -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54391 MW; 78BB459837F77AD8 CRC64;
MAKLVLSLCF LLFSGCFALR EQAQQNECQI QKLNALKPDN RIESEGGFIE TWNPNNKPFQ
CAGVALSRCT LNRNALRRPS YTNGPQEIYI QQGNGIFGMI FPGCPSTYQE PQESQQRGRS
QRPQDRHQKV HRFREGDLIA VPTGVAWWMY NNEDTPVVAV SIIDTNSLEN QLDQMPRRFY
LAGNQEQEFL KYQQQQQGGS QSQKGKQQEE ENEGSNILSG FAPEFLKEAF GVNMQIVRNL
QGENEEEDSG AIVTVKGGLR VTAPAMRKPQ QEEDDDDEEE QPQCVETDKG CQRQSKRSRN
GIDETICTMR LRQNIGQNSS PDIYNPQAGS ITTATSLDFP ALWLLKLSAQ YGSLRKNAMF
VPHYTLNANS IIYALNGRAL VQVVNCNGER VFDGELQEGG VLIVPQNFAV AAKSQSDNFE
YVSFKTNDRP SIGNLAGANS LLNALPEEVI QHTFNLKSQQ ARQVKNNNPF SFLVPPQESQ
RRAVA
