P0CAS5 · PA2BE_CRODU
- ProteinBasic phospholipase A2 F15
- 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 shows moderate neurotoxic activity in isolated mouse phrenic nerve diaphragm but shows high neurotoxic activity in a chick biventer cervis preparation. Also shows a high bactericidal effect against both Gram-negative and Gram-positive bacteria. 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
Activated by heparin. Inhibited by its chaperone crotapotin.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
38.5 mM | 4-nitro-3-(octanoyloxy)benzoic acid |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
8.5 nmol/min/mg |
pH Dependence
Optimum pH is 8.5.
Temperature Dependence
Optimum temperature is 18 degrees Celsius.
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 | defense response to bacterium | |
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 F15
- 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 > Crotalus
Accessions
- Primary accessionP0CAS5
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000376922 | 1-122 | Basic phospholipase A2 F15 | |||
Sequence: HLLQFNKMIKFETRKNAVPFYAFYGCYCGWGGQRRPKDATDRCCFVHDCCYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPKSRCRRPSETC | ||||||
Disulfide bond | 26↔115 | |||||
Sequence: CYCGWGGQRRPKDATDRCCFVHDCCYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPKSRC | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGWGGQRRPKDATDRCC | ||||||
Disulfide bond | 43↔95 | |||||
Sequence: CCFVHDCCYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAEC | ||||||
Disulfide bond | 49↔122 | |||||
Sequence: CCYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPKSRCRRPSETC | ||||||
Disulfide bond | 50↔88 | |||||
Sequence: CYGKLTKCNTKWDIYRYSLKSGYITCGKGTWCKEQICEC | ||||||
Disulfide bond | 57↔81 | |||||
Sequence: CNTKWDIYRYSLKSGYITCGKGTWC | ||||||
Disulfide bond | 75↔86 | |||||
Sequence: CGKGTWCKEQIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
When this protein is associated with crotapotin (F5 or F7), it forms the crotoxin protein.