P82896 · PA2A5_TRIST
- ProteinAcidic phospholipase A2 5
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids122 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that inhibits platelet aggregation induced by ADP, arachidonic acid and PAF (Ref.1). Acts in a enzymatic independent manner on a proteinase-activated receptor (PAR1, F2R) to evoke calcium release through the inositol 1,4,5-trisphosphate receptor (ITPR1, IP3R) and induces mouse aorta contraction (PubMed:25447533).
PAR1, phospholipase C and IP3R inhibitors suppress PA2-induced aorta contraction (PubMed:25447533).
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
PAR1, phospholipase C and IP3R inhibitors suppress PA2-induced aorta contraction (PubMed:25447533).
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides
Miscellaneous
Hemolytic and neurotoxic activities are not detected.
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
Preincubation with heparin slightly increase the enzymatic activity.
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 | identical protein binding | |
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcidic phospholipase A2 5
- EC number
- Short namessvPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Viperidae > Crotalinae > Trimeresurus
Accessions
- Primary accessionP82896
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000161711 | 1-122 | Acidic phospholipase A2 5 | |||
Sequence: NLMQFELLIMKVAGRSGIVWYSDYGCFCGKGGHGRPQDATDRCCFVHDCCYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICECDKAAAICFRDNKDTYDNKYWNIPMEGCQEESEPC | ||||||
Disulfide bond | 26↔115 | |||||
Sequence: CFCGKGGHGRPQDATDRCCFVHDCCYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICECDKAAAICFRDNKDTYDNKYWNIPMEGC | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGKGGHGRPQDATDRCC | ||||||
Disulfide bond | 43↔95 | |||||
Sequence: CCFVHDCCYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICECDKAAAIC | ||||||
Disulfide bond | 49↔122 | |||||
Sequence: CCYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICECDKAAAICFRDNKDTYDNKYWNIPMEGCQEESEPC | ||||||
Disulfide bond | 50↔88 | |||||
Sequence: CYGKVTECDPKMDFYRYSSNNGDIVCEANNPCTKEICEC | ||||||
Disulfide bond | 57↔81 | |||||
Sequence: CDPKMDFYRYSSNNGDIVCEANNPC | ||||||
Disulfide bond | 75↔86 | |||||
Sequence: CEANNPCTKEIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Monomer (predominant). Non-covalently linked homodimers are also observed.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P82896 | - P82896 | 2 | EBI-10105591, EBI-10105591 |