GLYG1_SOYBN
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 25-MAY-2022, entry version 144.
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=10.2307/3869011;
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=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 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 [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 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 [19]
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 [20]
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 [21]
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 [22]
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 [23]
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 [24]
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 [25]
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 [26]
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 [27]
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 [28]
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 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 (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: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 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. 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). 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.15}.
CC -!- SIMILARITY: Belongs to the 11S seed storage protein (globulins) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ACT53400.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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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_001235827.1; NM_001248898.2. [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 PDBsum; 1FXZ; -.
DR PDBsum; 1UCX; -.
DR PDBsum; 1UD1; -.
DR AlphaFoldDB; P04776; -.
DR SMR; P04776; -.
DR STRING; 3847.GLYMA03G32030.1; -.
DR Allergome; 1142; Gly m 6.0101.
DR Allergome; 5821; Gly m 6.
DR PRIDE; 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. [P04776-1]
DR Gramene; KRH67386; KRH67386; GLYMA_03G163500. [P04776-1]
DR KEGG; gmx:547901; -.
DR eggNOG; ENOG502QU1J; Eukaryota.
DR HOGENOM; CLU_026341_2_0_1; -.
DR InParanoid; P04776; -.
DR OrthoDB; 603461at2759; -.
DR EvolutionaryTrace; P04776; -.
DR Proteomes; UP000008827; Chromosome 3.
DR Genevisible; P04776; GM.
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; 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 286..301
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..233
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
