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Entry version 121 (12 Aug 2020)
Sequence version 1 (20 Mar 1987)
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Protein

Glycinin G5

Gene

GY5

Organism
Glycine max (Soybean) (Glycine hispida)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating in transmembranes, leading to membrane permeability and, eventually, cell death (PubMed:22236762, Ref. 15, PubMed:28590128).4 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionSeed storage protein, Storage protein

Protein family/group databases

Transport Classification Database

More...
TCDBi
1.C.121.1.2, the soybean glycinin-derived pore-forming peptide (sgpp) family

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Glycinin G52 Publications
Short name:
Glycinin 11S G51 Publication
Short name:
Glycinin A3B41 Publication
Alternative name(s):
Allergen: Gly m 6Curated
Cleaved into the following 2 chains:
Glycinin A3 subunit2 Publications
Glycinin B4 subunit2 Publications
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:GY51 Publication
Ordered Locus Names:Glyma13g18450Curated
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiGlycine max (Soybean) (Glycine hispida)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri3847 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliopsidaeudicotyledonsGunneridaePentapetalaerosidsfabidsFabalesFabaceaePapilionoideae50 kb inversion cladeNPAAA cladeindigoferoid/millettioid cladePhaseoleaeGlycineGlycine subgen. Soja
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000008827 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Unplaced

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Vacuole

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section is used for proteins that cause an allergic reaction in mammals. We usually specify in which species the protein is allergenic.<p><a href='/help/allergenic_properties' target='_top'>More...</a></p>Allergenic propertiesi

Causes an allergic reaction in human and animals (e.g. rats, mouse and piglets); the acidic subunit is particularly allergenic (PubMed:18996574, PubMed:24499064, PubMed:23426933, PubMed:30078589). Binds to IgE of patients with severe allergic reactions (anaphylaxis) to soybean (PubMed:18996574). Allergy to soybean is most common for infants (usually appears at the age of three months) which frequently outgrow their soybean allergy by the age of two, but a severe soybean allergy can last a lifetime; various symptoms involve skin, gastrointestinal tract and respiratory tracts (PubMed:24499064). Damaged intestinal function in piglets is associated with glycinin-mediated perturbation of nuclear factor-kappa B (NF-kappaB), Jun N-terminal kinase (JNK) and p38 levels (PubMed:30139257). Juvenile Chinese mitten crabs (E.sinensis) supplemented with glycinin display impaired growth and altered intestinal health due to gut inflammation, reshaped community of gut microbiota and digestive dysfunction (PubMed:30300740). Ingredient processing methods to reduce soybean allergenicity but keeping its nutritional values have been developed, among them physical processing includes extrusion, high-pressure (>300 MPa), heating (between 70 and 90 degrees Celsius), roasting, chemical processing includes ethanol extraction (55-76 percent between 70 and 80 degrees Celsius), in vitro glycation (e.g. with xylose at 55 degrees Celsius) and enzymatic hydrolysis with pepsin and trypsin, and biological processing includes fermentation with A.oryzae, S.cerevisiae, L.lactic subsplactis, B.subtilis, B.lactic and L.plantarum (PubMed:24499064, PubMed:27620509). Resistant to hydrolysis by papain, alcalase, and fungal protease (PubMed:24499064).1 Publication6 Publications

<p>This subsection of the 'Pathology and Biotech' section describes the use of a specific protein in the biotechnological industry.<p><a href='/help/biotechnological_use' target='_top'>More...</a></p>Biotechnological usei

Emulsification efficiency of glycinin is improved by degree-dependent glycation with soy soluble polysaccharide (SSPS) at 60 degrees Celsius in both the acidic (A) and basic (B) polypeptides as a result of subunit dissociation at the quaternary level (PubMed:30372068). Thermal treatment of soybean seed proteins leads to the aggregation of glycinin acidic and basic polypeptides (GAP and GBP, respectively) (PubMed:10867183, PubMed:25801436). GBP improve sensory properties of meat (e.g. pork) during chilled storage and inhibit bacterial growth (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) (PubMed:30263339, PubMed:22236762). Antibacterial properties of the GBP antimicrobial peptides (AMPs) associated with no cytotoxicity on the viability of human embryonic kidney cells make them promising candidates as natural antibacterial agents (PubMed:22236762, Ref. 15, PubMed:28590128). The commercially synthesized peptide G5466 (250-269) exhibits antimicrobial activity toward L.monocytogenes and E.coli probably by forming pores and aggregating in transmembranes, thus being a promising candidate as a natural antibacterial agent (PubMed:27612614). Fragmented peptides resulting from gastrointestinal digestion of germinated soybeans seem to have anticancer and antiinflammatory actions on human colon cancer cells (e.g. Caco-2, HT-29, and HCT-116) and macrophages (LPS-stimulated RAW 264.7) (PubMed:29037738). Such peptides resulting from digested germinated soybeans exhibit also anti-diabetic potential by inhibiting dipeptidyl peptidase IV (DPP-IV), salivary alpha-amylase and intestinal alpha-glucosidase enzymes (PubMed:30249015).10 Publications

Keywords - Diseasei

Allergen

Protein family/group databases

Allergome; a platform for allergen knowledge

More...
Allergomei
5821, Gly m 6
5826, Gly m 6.0501

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 24Sequence analysisAdd BLAST24
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000003202325 – 344Glycinin A3 subunitAdd BLAST320
ChainiPRO_0000032024345 – 516Glycinin B4 subunitAdd BLAST172

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi33 ↔ 661 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi79N-linked (GlcNAc...) asparaginePROSITE-ProRule annotation1
Disulfide bondi109 ↔ 351Interchain (between A3 and B4 chains)1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P04347

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the 'Expression' section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Exclusively in seeds during embryogenesis.1 Publication

<p>This subsection of the 'Expression' section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified 'at the protein level'.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

Accumulates early during embryogenesis, but repressed late in seed development.1 Publication

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond.

2 Publications

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
3847.GLYMA13G18450.2

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1516
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P04347

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P04347

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini38 – 249Cupin type-1 1Sequence analysisAdd BLAST212
Domaini357 – 502Cupin type-1 2Sequence analysisAdd BLAST146

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi117 – 136Gln-richPROSITE-ProRule annotationAdd BLAST20
Compositional biasi202 – 231Gln-richPROSITE-ProRule annotationAdd BLAST30

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG502QU1J, Eukaryota

Database of Orthologous Groups

More...
OrthoDBi
603461at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.120.10, 2 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR022379, 11S_seedstore_CS
IPR006044, 11S_seedstore_pln
IPR006045, Cupin_1
IPR014710, RmlC-like_jellyroll
IPR011051, RmlC_Cupin_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00190, Cupin_1, 2 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00439, 11SGLOBULIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00835, Cupin_1, 2 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF51182, SSF51182, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00305, 11S_SEED_STORAGE, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: P04347-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MGKPFFTLSL SSLCLLLLSS ACFAITSSKF NECQLNNLNA LEPDHRVESE
60 70 80 90 100
GGLIETWNSQ HPELQCAGVT VSKRTLNRNG SHLPSYLPYP QMIIVVQGKG
110 120 130 140 150
AIGFAFPGCP ETFEKPQQQS SRRGSRSQQQ LQDSHQKIRH FNEGDVLVIP
160 170 180 190 200
LGVPYWTYNT GDEPVVAISP LDTSNFNNQL DQNPRVFYLA GNPDIEHPET
210 220 230 240 250
MQQQQQQKSH GGRKQGQHRQ QEEEGGSVLS GFSKHFLAQS FNTNEDTAEK
260 270 280 290 300
LRSPDDERKQ IVTVEGGLSV ISPKWQEQED EDEDEDEEYG RTPSYPPRRP
310 320 330 340 350
SHGKHEDDED EDEEEDQPRP DHPPQRPSRP EQQEPRGRGC QTRNGVEENI
360 370 380 390 400
CTMKLHENIA RPSRADFYNP KAGRISTLNS LTLPALRQFG LSAQYVVLYR
410 420 430 440 450
NGIYSPDWNL NANSVTMTRG KGRVRVVNCQ GNAVFDGELR RGQLLVVPQN
460 470 480 490 500
PAVAEQGGEQ GLEYVVFKTH HNAVSSYIKD VFRVIPSEVL SNSYNLGQSQ
510
VRQLKYQGNS GPLVNP
Length:516
Mass (Da):57,956
Last modified:March 20, 1987 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFE464753A8D20715
GO
Isoform 2 (identifier: P04347-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     516-516: P → PQITTSIYEGVVRPSYMK

Show »
Length:533
Mass (Da):59,910
Checksum:i372BC4EB11B4BB90
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti81S → L in BAA74952 (Ref. 4) Curated1
Sequence conflicti81S → L in BAB15802 (Ref. 5) Curated1
Sequence conflicti81S → L in ACU17712 (Ref. 7) Curated1
Sequence conflicti81S → L in ACN11532 (Ref. 6) Curated1
Sequence conflicti87L → S in BAA19058 (Ref. 3) Curated1
Sequence conflicti87L → S in BAA19059 (Ref. 3) Curated1
Sequence conflicti87L → S in BAA74952 (Ref. 4) Curated1
Sequence conflicti87L → S in BAB15802 (Ref. 5) Curated1
Sequence conflicti87L → S in ACU17712 (Ref. 7) Curated1
Sequence conflicti87L → S in ACN11532 (Ref. 6) Curated1
Sequence conflicti101A → E in BAA19059 (Ref. 3) Curated1
Sequence conflicti151L → P in BAA74952 (Ref. 4) Curated1
Sequence conflicti151L → P in BAB15802 (Ref. 5) Curated1
Sequence conflicti151L → P in ACU17712 (Ref. 7) Curated1
Sequence conflicti151L → P in ACN11532 (Ref. 6) Curated1
Sequence conflicti170P → L in BAA19058 (Ref. 3) Curated1
Sequence conflicti170P → L in BAA19059 (Ref. 3) Curated1
Sequence conflicti170P → L in BAA74952 (Ref. 4) Curated1
Sequence conflicti170P → L in BAB15802 (Ref. 5) Curated1
Sequence conflicti170P → L in ACU17712 (Ref. 7) Curated1
Sequence conflicti170P → L in ACN11532 (Ref. 6) Curated1
Sequence conflicti219 – 221RQQ → QQP in ACN11532 (Ref. 6) Curated3
Sequence conflicti219R → Q in BAA19058 (Ref. 3) Curated1
Sequence conflicti219R → Q in BAA19059 (Ref. 3) Curated1
Sequence conflicti219R → Q in BAA74952 (Ref. 4) Curated1
Sequence conflicti219R → Q in BAB15802 (Ref. 5) Curated1
Sequence conflicti219R → Q in ACU17712 (Ref. 7) Curated1
Sequence conflicti225G → R in ACU17712 (Ref. 7) Curated1
Sequence conflicti290 – 291GR → EQ in BAA19058 (Ref. 3) Curated2
Sequence conflicti290 – 291GR → EQ in BAA19059 (Ref. 3) Curated2
Sequence conflicti290 – 291GR → EQ in BAA74952 (Ref. 4) Curated2
Sequence conflicti290 – 291GR → EQ in BAB15802 (Ref. 5) Curated2
Sequence conflicti290 – 291GR → EQ in ACU17712 (Ref. 7) Curated2
Sequence conflicti290 – 291GR → EQ in ACN11532 (Ref. 6) Curated2
Sequence conflicti315E → G in ACN11532 (Ref. 6) Curated1
Sequence conflicti357E → G in ACU17712 (Ref. 7) Curated1
Sequence conflicti407D → H in BAA19058 (Ref. 3) Curated1
Sequence conflicti407D → H in BAA19059 (Ref. 3) Curated1
Sequence conflicti407D → H in BAA74952 (Ref. 4) Curated1
Sequence conflicti407D → H in BAB15802 (Ref. 5) Curated1
Sequence conflicti407D → H in ACU17712 (Ref. 7) Curated1
Sequence conflicti407D → H in ACN11532 (Ref. 6) Curated1
Sequence conflicti416 – 417TM → IYV in BAA19058 (Ref. 3) Curated2
Sequence conflicti416 – 417TM → IYV in BAA19059 (Ref. 3) Curated2
Sequence conflicti416 – 417TM → IYV in BAA74952 (Ref. 4) Curated2
Sequence conflicti416 – 417TM → IYV in BAB15802 (Ref. 5) Curated2
Sequence conflicti416 – 417TM → IYV in ACU17712 (Ref. 7) Curated2
Sequence conflicti416 – 417TM → IYV in ACN11532 (Ref. 6) Curated2
Sequence conflicti451 – 452PA → FV in BAA19058 (Ref. 3) Curated2
Sequence conflicti451 – 452PA → FV in BAA19059 (Ref. 3) Curated2
Sequence conflicti451 – 452PA → FV in BAA74952 (Ref. 4) Curated2
Sequence conflicti451 – 452PA → FV in BAB15802 (Ref. 5) Curated2
Sequence conflicti451 – 452PA → FV in ACN11532 (Ref. 6) Curated2
Sequence conflicti484V → A in BAA19058 (Ref. 3) Curated1
Sequence conflicti484V → A in BAA19059 (Ref. 3) Curated1
Sequence conflicti484V → A in BAB15802 (Ref. 5) Curated1
Sequence conflicti484V → A in ACN11532 (Ref. 6) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_060146516P → PQITTSIYEGVVRPSYMK in isoform 2. 1

Sequence databases

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EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
M10962 mRNA Translation: AAA33964.1
AB000168 mRNA Translation: BAA19058.1
AB000169 mRNA Translation: BAA19059.1
AB003680 Genomic DNA Translation: BAA74952.1
AB049440 mRNA Translation: BAB15802.1
FJ599666 mRNA Translation: ACN11532.1
BT093334 mRNA Translation: ACU17712.1

Protein sequence database of the Protein Information Resource

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PIRi
A92524, FWSYG3
PQ0200
PQ0806
PQ0807
PQ0808

NCBI Reference Sequences

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RefSeqi
NP_001236676.1, NM_001249747.2

Genome annotation databases

Database of genes from NCBI RefSeq genomes

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GeneIDi
547452

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
gmx:547452

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M10962 mRNA Translation: AAA33964.1
AB000168 mRNA Translation: BAA19058.1
AB000169 mRNA Translation: BAA19059.1
AB003680 Genomic DNA Translation: BAA74952.1
AB049440 mRNA Translation: BAB15802.1
FJ599666 mRNA Translation: ACN11532.1
BT093334 mRNA Translation: ACU17712.1
PIRiA92524, FWSYG3
PQ0200
PQ0806
PQ0807
PQ0808
RefSeqiNP_001236676.1, NM_001249747.2

3D structure databases

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Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OD5X-ray2.10A/B26-516[»]
2D5FX-ray1.90A/B25-516[»]
2D5HX-ray2.80A/B/C/D/E/F25-516[»]
SMRiP04347
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

STRINGi3847.GLYMA13G18450.2

Protein family/group databases

Allergomei5821, Gly m 6
5826, Gly m 6.0501
TCDBi1.C.121.1.2, the soybean glycinin-derived pore-forming peptide (sgpp) family

Proteomic databases

PRIDEiP04347

Genome annotation databases

GeneIDi547452
KEGGigmx:547452

Phylogenomic databases

eggNOGiENOG502QU1J, Eukaryota
OrthoDBi603461at2759

Miscellaneous databases

EvolutionaryTraceiP04347

Family and domain databases

Gene3Di2.60.120.10, 2 hits
InterProiView protein in InterPro
IPR022379, 11S_seedstore_CS
IPR006044, 11S_seedstore_pln
IPR006045, Cupin_1
IPR014710, RmlC-like_jellyroll
IPR011051, RmlC_Cupin_sf
PfamiView protein in Pfam
PF00190, Cupin_1, 2 hits
PRINTSiPR00439, 11SGLOBULIN
SMARTiView protein in SMART
SM00835, Cupin_1, 2 hits
SUPFAMiSSF51182, SSF51182, 1 hit
PROSITEiView protein in PROSITE
PS00305, 11S_SEED_STORAGE, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiGLYG5_SOYBN
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P04347
Secondary accession number(s): C0KG62
, C6T7B0, P93707, P93708, Q7GC77, Q9SB12
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 20, 1987
Last sequence update: March 20, 1987
Last modified: August 12, 2020
This is version 121 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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