UniProt functional annotation for P04347



	UniProt functional annotation for P04347

UniProt code: P04347.

Organism: Glycine max (Soybean) (Glycine hispida).

Taxonomy: Eukaryota; 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.

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, Ref.15, PubMed:28590128). {ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:2485233, ECO:0000269|PubMed:28590128, ECO:0000269|Ref.15}.

Subunit: Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. {ECO:0000269|PubMed:12771376, ECO:0000269|PubMed:20215054}.

Subcellular location: Vacuole, aleurone grain. Endoplasmic reticulum {ECO:0000269|PubMed:29348620}. Protein storage vacuole {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles (PubMed:29348620). Cotyledonary membrane-bound vacuolar protein bodies. {ECO:0000269|PubMed:29348620}.

Tissue specificity: Exclusively in seeds during embryogenesis. {ECO:0000269|PubMed:2485233}.

Developmental stage: Accumulates early during embryogenesis, but repressed late in seed development. {ECO:0000269|PubMed:2485233}.

Ptm: During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269|PubMed:29037738}.

Allergen: 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). {ECO:0000269|PubMed:18996574, ECO:0000269|PubMed:23426933, ECO:0000269|PubMed:27620509, ECO:0000269|PubMed:30078589, ECO:0000269|PubMed:30139257, ECO:0000269|PubMed:30300740, ECO:0000303|PubMed:24499064}.

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: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). {ECO:0000269|PubMed:10867183, ECO:0000269|PubMed:22236762, ECO:0000269|PubMed:25801436, ECO:0000269|PubMed:27612614, ECO:0000269|PubMed:28590128, ECO:0000269|PubMed:29037738, ECO:0000269|PubMed:30249015, ECO:0000269|PubMed:30263339, ECO:0000269|PubMed:30372068, ECO:0000269|Ref.15}.

Similarity: Belongs to the 11S seed storage protein (globulins) family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Glycine max (Soybean) (Glycine hispida).
Taxonomy:		Eukaryota; 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.



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, Ref.15, PubMed:28590128). {ECO:0000269\|PubMed:22236762, ECO:0000269\|PubMed:2485233, ECO:0000269\|PubMed:28590128, ECO:0000269\|Ref.15}.


Subunit:		Hexamer; each subunit is composed of an acidic and a basic chain derived from a single precursor and linked by a disulfide bond. {ECO:0000269\|PubMed:12771376, ECO:0000269\|PubMed:20215054}.
Subcellular location:		Vacuole, aleurone grain. Endoplasmic reticulum {ECO:0000269\|PubMed:29348620}. Protein storage vacuole {ECO:0000269\|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles (PubMed:29348620). Cotyledonary membrane-bound vacuolar protein bodies. {ECO:0000269\|PubMed:29348620}.
Tissue specificity:		Exclusively in seeds during embryogenesis. {ECO:0000269\|PubMed:2485233}.
Developmental stage:		Accumulates early during embryogenesis, but repressed late in seed development. {ECO:0000269\|PubMed:2485233}.
Ptm:		During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269\|PubMed:29037738}.
Allergen:		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). {ECO:0000269\|PubMed:18996574, ECO:0000269\|PubMed:23426933, ECO:0000269\|PubMed:27620509, ECO:0000269\|PubMed:30078589, ECO:0000269\|PubMed:30139257, ECO:0000269\|PubMed:30300740, ECO:0000303\|PubMed:24499064}.
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: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). {ECO:0000269\|PubMed:10867183, ECO:0000269\|PubMed:22236762, ECO:0000269\|PubMed:25801436, ECO:0000269\|PubMed:27612614, ECO:0000269\|PubMed:28590128, ECO:0000269\|PubMed:29037738, ECO:0000269\|PubMed:30249015, ECO:0000269\|PubMed:30263339, ECO:0000269\|PubMed:30372068, ECO:0000269\|Ref.15}.
Similarity:		Belongs to the 11S seed storage protein (globulins) family. {ECO:0000305}.