Q1RP79 · PA2B1_VIPNI
- ProteinBasic phospholipase A2 chain HDP-1P
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids138 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Heterodimer: shows the same activities as the monomer, but with a lower potency.
Monomer: snake venom phospholipase A2 (PLA2) that shows presynaptic neurotoxicity, anticoagulant activity and that weakly inhibits ADP-induced platelet aggregation (PubMed:18083205).
Inhibits exocytosis in pancreatic beta cells, confirming it can act presynaptically in inhibiting the exocytosis of neurotransmitters in neurons (PubMed:19500614).
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
Inhibits exocytosis in pancreatic beta cells, confirming it can act presynaptically in inhibiting the exocytosis of neurotransmitters in neurons (PubMed:19500614).
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
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
Enzymatic activity and neurotoxicity are inhibited by Triton X-100, which has been determined to be located in the center of the hydrophobic channel of the enzyme.
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 | phospholipid metabolic process |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBasic phospholipase A2 chain HDP-1P
- 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 > Vipera
Accessions
- Primary accessionQ1RP79
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MRILWIVAVCLIGVEG | ||||||
Chain | PRO_5000079752 | 17-138 | Basic phospholipase A2 chain HDP-1P | |||
Sequence: NLFQFAKMINGKLGAFSVWNYISYGCYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNQNTYNKNYKFLSSSRCRQTSEQC | ||||||
Disulfide bond | 42↔131 | |||||
Sequence: CYCGWGGQGTPKDATDRCCFVHDCCYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNQNTYNKNYKFLSSSRC | ||||||
Disulfide bond | 44↔60 | |||||
Sequence: CGWGGQGTPKDATDRCC | ||||||
Disulfide bond | 59↔111 | |||||
Sequence: CCFVHDCCYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANC | ||||||
Disulfide bond | 65↔138 | |||||
Sequence: CCYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICECDRVAANCFHQNQNTYNKNYKFLSSSRCRQTSEQC | ||||||
Disulfide bond | 66↔104 | |||||
Sequence: CYGRVRGCNPKLAIYAYSFKKGNIVCGKNNGCLRDICEC | ||||||
Disulfide bond | 73↔97 | |||||
Sequence: CNPKLAIYAYSFKKGNIVCGKNNGC | ||||||
Disulfide bond | 91↔102 | |||||
Sequence: CGKNNGCLRDIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Heterodimer; non-covalently linked. The toxic basic protein has phospholipase A2 activity (chain HDP-1P) and the non-toxic acidic protein functions as its inhibitor (chain HPD-1I (AC A4VBF0)).
Structure
Family & Domains
Sequence similarities
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length138
- Mass (Da)15,566
- Last updated2006-05-16 v1
- Checksum72D55BD516C3E5D9
Mass Spectrometry
Keywords
- Technical term