Q75N34 · DB3S_DIOPO
- ProteinDioscorin DB3S
- GeneDB3S
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids268 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase and weak trypsin inhibitor activity detected by measuring the dehydration of sodium bicarbonate and the inhibition of trypsin-catalyzed hydrolysis of N-benzoyl-L-arginine-4-nitro anilide, respectively (PubMed:10552514).
Contrarily, no carbonate dehydratase or trypsin inhibitor activity detected by measuring the hydrolysis of 4-nitrophenyl acetate or the inhibition of bovine trypsin-catalyzed hydrolysis of N-benzoyl-L-arginine ethyl ester, respectively (PubMed:15047697).
Has dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities (Ref.5). Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H2O and CO2 (By similarity).
Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and hydroxyl radicals (PubMed:11600050).
Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages (By similarity).
Contrarily, no carbonate dehydratase or trypsin inhibitor activity detected by measuring the hydrolysis of 4-nitrophenyl acetate or the inhibition of bovine trypsin-catalyzed hydrolysis of N-benzoyl-L-arginine ethyl ester, respectively (PubMed:15047697).
Has dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities (Ref.5). Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H2O and CO2 (By similarity).
Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical and hydroxyl radicals (PubMed:11600050).
Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages (By similarity).
Catalytic activity
- H+ + hydrogencarbonate = CO2 + H2O
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 91 | Proton acceptor | ||||
Sequence: H | ||||||
Binding site | 92 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 117-119 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: HFH | ||||||
Binding site | 136 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: Q | ||||||
Binding site | 205-206 | L-ascorbate (UniProtKB | ChEBI) | ||||
Sequence: TA |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | antioxidant activity | |
Molecular Function | carbonate dehydratase activity | |
Molecular Function | L-ascorbic acid binding | |
Molecular Function | monodehydroascorbate reductase (NADH) activity | |
Molecular Function | nutrient reservoir activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | serine-type endopeptidase inhibitor activity | |
Molecular Function | zinc ion binding | |
Biological Process | carbon utilization | |
Biological Process | cellular oxidant detoxification | |
Biological Process | cellular response to carbon dioxide | |
Biological Process | negative regulation of endopeptidase activity | |
Biological Process | one-carbon metabolic process | |
Biological Process | positive regulation of gene expression | |
Biological Process | positive regulation of phagocytosis | |
Biological Process | response to oxygen radical |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDioscorin DB3S
- EC number
- Alternative names
- Allergen nameDio p TSP
Gene names
Organism names
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Dioscoreales > Dioscoreaceae > Dioscorea
Accessions
- Primary accessionQ75N34
Phenotypes & Variants
Allergenic properties
Causes an allergic reaction in human. Binds to IgE of patients allergic to Chinese yam (PubMed:18303202, PubMed:29423371).
Patients can be sensitized to this protein via an oral or inhalant route (PubMed:18303202).
Thermal stable oral allergen, which can to trigger anaphylactic reaction and oral allergy syndrome even when consumed as cooked. Activates human basophils (PubMed:29423371).
Patients can be sensitized to this protein via an oral or inhalant route (PubMed:18303202).
Thermal stable oral allergen, which can to trigger anaphylactic reaction and oral allergy syndrome even when consumed as cooked. Activates human basophils (PubMed:29423371).
Keywords
- Disease
Protein family/group databases
PTM/Processing
Features
Showing features for chain, signal, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5004286658 | ?-268 | Dioscorin DB3S | |||
Sequence: MSSSTLLHLLLLSSLLFSCLANVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGRLRRNYRAVDARLRNSGHDVLVEFKGNAGSLSINRVAYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFIFGRADPFLSDLEDFIKQFSSSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKVCAI | ||||||
Signal | 1-? | |||||
Disulfide bond | 50↔209 | |||||
Sequence: CGKGMEQSPIQLRDNRVIFDQTLGRLRRNYRAVDARLRNSGHDVLVEFKGNAGSLSINRVAYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFIFGRADPFLSDLEDFIKQFSSSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPC |
Post-translational modification
Not glycosylated.
Keywords
- PTM
Expression
Tissue specificity
Expressed in tuber (at protein level).
Interaction
Subunit
Monomer (By similarity).
Homodimer (PubMed:15047697).
Homodimer (PubMed:15047697).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 25-259 | Alpha-carbonic anhydrase | ||||
Sequence: DEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGRLRRNYRAVDARLRNSGHDVLVEFKGNAGSLSINRVAYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFIFGRADPFLSDLEDFIKQFSSSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFE |
Sequence similarities
Belongs to the alpha-class carbonic anhydrase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length268
- Mass (Da)30,460
- Last updated2004-07-05 v1
- Checksum30F2BC9D273FCB30
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 35 | in Ref. 4; AA sequence | ||||
Sequence: N → H |
Keywords
- Technical term