P59071 · PA2B8_DABRR
- ProteinBasic phospholipase A2 VRV-PL-VIIIa
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids121 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that shows weak neurotoxicity and medium anticoagulant effects by binding to factor Xa (F10) and inhibiting the prothrombinase activity (IC50 is 130 nM) (PubMed:18062812).
It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
It also damages vital organs such as lung, liver and kidney, displays edema-inducing activities when injected into the foot pads of mice and induces necrosis of muscle cells when injected into the thigh muscle. Has a low enzymatic activity. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
Miscellaneous
D.russelli pulchella is synonymous with D.russelii.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H+
Cofactor
Note: Binds 1 Ca2+ ion.
Activity regulation
Oxyphenbutazone (OPB), anisic acid and atropine inhibit the enzymatic activity by binding at the substrate-binding site (PubMed:15544328, PubMed:16596639).
P-coumaric acid, resveratrol, spermidine, corticosterone and gramine derivative inhibit the enzymatic activity by binding at the substrate-binding site (PubMed:25541253).
P-coumaric acid, resveratrol, spermidine, corticosterone and gramine derivative inhibit the enzymatic activity by binding at the substrate-binding site (PubMed:25541253).
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium-dependent phospholipase A2 activity | |
Molecular Function | phospholipid binding | |
Molecular Function | toxin activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | lipid catabolic process | |
Biological Process | negative regulation of T cell proliferation | |
Biological Process | phospholipid metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasic phospholipase A2 VRV-PL-VIIIa
- EC number
- Short namessvPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Viperinae > Daboia
Accessions
- Primary accessionP59071
- Secondary accessions
Subcellular Location
Phenotypes & Variants
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000161717 | 1-121 | Basic phospholipase A2 VRV-PL-VIIIa | |||
Sequence: SLLEFGKMILEETGKLAIPSYSSYGCYCGWGGKGTPKDATDRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELKC | ||||||
Disulfide bond | 26↔115 | |||||
Sequence: CYCGWGGKGTPKDATDRCCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNLNTYSKKYMLYPDFLC | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGWGGKGTPKDATDRCC | ||||||
Disulfide bond | 43↔95 | |||||
Sequence: CCFVHDCCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAIC | ||||||
Disulfide bond | 49↔121 | |||||
Sequence: CCYGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICECDKAAAICFRQNLNTYSKKYMLYPDFLCKGELKC | ||||||
Disulfide bond | 50↔88 | |||||
Sequence: CYGNLPDCNPKSDRYKYKRVNGAIVCEKGTSCENRICEC | ||||||
Disulfide bond | 57↔81 | |||||
Sequence: CNPKSDRYKYKRVNGAIVCEKGTSC | ||||||
Disulfide bond | 75↔86 | |||||
Sequence: CEKGTSCENRIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.