P04776 · GLYG1_SOYBN
- ProteinGlycinin G1
- GeneGY1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids495 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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, PubMed:28590128, Ref.15).
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, PubMed:28590128, Ref.15).
Biotechnology
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:22236762, PubMed:30263339).
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, PubMed:28590128, Ref.15). Fragmented peptides resulting from gastrointestinal digestion of germinated soybeans seem to have anticancer and anti-inflammatory 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).
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:22236762, PubMed:30263339).
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, PubMed:28590128, Ref.15). Fragmented peptides resulting from gastrointestinal digestion of germinated soybeans seem to have anticancer and anti-inflammatory 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).
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum | |
Cellular Component | protein storage vacuole | |
Molecular Function | nutrient reservoir activity |
Keywords
- Molecular function
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGlycinin G1
- Short namesGlycinin 11S G1 ; Glycinin A1aB1b
- Cleaved into 2 chains
- Allergen nameGly m 6
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Fabales > Fabaceae > Papilionoideae > 50 kb inversion clade > NPAAA clade > indigoferoid/millettioid clade > Phaseoleae > Glycine > Glycine subgen. Soja
Accessions
- Primary accessionP04776
- Secondary accessions
Proteomes
Genome annotation databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles.
Keywords
- Cellular component
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human and animals (e.g. rats, mouse and piglets); the acidic subunit is particularly allergenic (PubMed:18996574, PubMed:23426933, PubMed:24499064, 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 NF-kappa-B, 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).
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 NF-kappa-B, 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).
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MAKLVFSLCFLLFSGCCFA | ||||||
Chain | PRO_0000032009 | 20-306 | Glycinin A1a subunit | |||
Sequence: FSSREQPQQNECQIQKLNALKPDNRIESEGGLIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSK | ||||||
Disulfide bond | 31↔64 | |||||
Sequence: CQIQKLNALKPDNRIESEGGLIETWNPNNKPFQC | ||||||
Disulfide bond | 107↔317 | Interchain (between A1a and Bx chains) | ||||
Sequence: CPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAKNLQGENEGEDKGAIVTVKGGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSKSRRNGIDETIC | ||||||
Propeptide | PRO_0000032010 | 307-310 | ||||
Sequence: SRRN | ||||||
Chain | PRO_0000032011 | 311-490 | Glycinin Bx subunit | |||
Sequence: GIDETICTMRLRHNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAEFGSLRKNAMFVPHYNLNANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNALPEEVIQHTFNLKSQQARQIKNNNPFKFLVPPQESQ | ||||||
Propeptide | PRO_0000032012 | 491-495 | ||||
Sequence: KRAVA |
Post-translational modification
During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome.
The precursor is post-translationally processed to form a covalently linked A1a-Bx subunit complex.
Keywords
- PTM
Proteomic databases
Interaction
Subunit
Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond (PubMed:11124907, PubMed:14705889).
Interacts with the vacuolar-sorting receptor VSR via its vacuolar targeting signal (PubMed:29348620).
Interacts with the vacuolar-sorting receptor VSR via its vacuolar targeting signal (PubMed:29348620).
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 36-241 | Cupin type-1 1 | ||||
Sequence: LNALKPDNRIESEGGLIETWNPNNKPFQCAGVALSRCTLNRNALRRPSYTNGPQEIYIQQGKGIFGMIYPGCPSTFEEPQQPQQRGQSSRPQDRHQKIYNFREGDLIAVPTGVAWWMYNNEDTPVVAVSIIDTNSLENQLDQMPRRFYLAGNQEQEFLKYQQEQGGHQSQKGKHQQEEENEGGSILSGFTLEFLEHAFSVDKQIAK | ||||||
Region | 196-217 | Disordered | ||||
Sequence: QQEQGGHQSQKGKHQQEEENEG | ||||||
Region | 260-312 | Disordered | ||||
Sequence: GGLSVIKPPTDEQQQRPQEEEEEEEDEKPQCKGKDKHCQRPRGSQSKSRRNGI | ||||||
Compositional bias | 286-301 | Basic and acidic residues | ||||
Sequence: EKPQCKGKDKHCQRPR | ||||||
Domain | 323-472 | Cupin type-1 2 | ||||
Sequence: HNIGQTSSPDIYNPQAGSVTTATSLDFPALSWLRLSAEFGSLRKNAMFVPHYNLNANSIIYALNGRALIQVVNCNGERVFDGELQEGRVLIVPQNFVVAARSQSDNFEYVSFKTNDTPMIGTLAGANSLLNALPEEVIQHTFNLKSQQAR | ||||||
Motif | 486-495 | Vacuolar targeting signal | ||||
Sequence: PQESQKRAVA |
Sequence similarities
Belongs to the 11S seed storage protein (globulins) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
This entry describes 2 isoforms produced by Alternative splicing.
P04776-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length495
- Mass (Da)55,706
- Last updated1989-10-01 v2
- Checksum329CB0545B24D894
P04776-2
- Name2
Sequence caution
Features
Showing features for sequence conflict, compositional bias, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 42 | in Ref. 3; CAA26723 | ||||
Sequence: D → G | ||||||
Sequence conflict | 108 | in Ref. 3; CAA26723 | ||||
Sequence: P → S | ||||||
Sequence conflict | 136 | in Ref. 3; CAA26723 | ||||
Sequence: F → S | ||||||
Sequence conflict | 146 | in Ref. 6; ACT53401 | ||||
Sequence: T → A | ||||||
Sequence conflict | 216 | in Ref. 6; ACT53401 | ||||
Sequence: E → G | ||||||
Compositional bias | 286-301 | Basic and acidic residues | ||||
Sequence: EKPQCKGKDKHCQRPR | ||||||
Sequence conflict | 360 | in Ref. 3; CAA26723 | ||||
Sequence: E → G | ||||||
Alternative sequence | VSP_060142 | 369-386 | in isoform 2 | |||
Sequence: MFVPHYNLNANSIIYALN → EEAKAKAEEMALTRPYAP | ||||||
Alternative sequence | VSP_060143 | 387-495 | in isoform 2 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X15121 EMBL· GenBank· DDBJ | CAA33215.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X02985 EMBL· GenBank· DDBJ | CAA26723.1 EMBL· GenBank· DDBJ | mRNA | ||
M36686 EMBL· GenBank· DDBJ | AAA33966.1 EMBL· GenBank· DDBJ | mRNA | ||
AB113349 EMBL· GenBank· DDBJ | BAC78522.1 EMBL· GenBank· DDBJ | mRNA | ||
GQ259738 EMBL· GenBank· DDBJ | ACT53400.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
GQ259739 EMBL· GenBank· DDBJ | ACT53401.1 EMBL· GenBank· DDBJ | mRNA |