Q8AXY1 · PA2A_BOTJR
- ProteinAcidic phospholipase A2 BthA-1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids138 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that displays edema-inducing activities (activity that is inhibited by EDTA and dexamethasone), inhibits phospholipid-dependent collagen/ADP-induced platelet aggregation, possess hypotensive as well as anticoagulant activities. In addition, this enzyme shows bactericidal activity against E.coli and S.aureus. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Miscellaneous
This enzyme has been found to be not myotoxic, not cytotoxic, not hemorrhagic and not lethal.
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 per subunit.
Activity regulation
Inhibited by EDTA and bromophenacyl bromide (BPB).
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 | phospholipid metabolic process | |
Biological Process | regulation of blood pressure |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcidic phospholipase A2 BthA-1
- 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 > Bothrops
Accessions
- Primary accessionQ8AXY1
Subcellular Location
Phenotypes & Variants
Toxic dose
LD50 is 25 mg/kg by intraperitoneal injection into mice.
LD50 is 7.5 mg/kg by intravenous injection into mice.
LD50 is 0.5 mg/kg by intracerebroventricular injection.
PTM/Processing
Features
Showing features for signal, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-16 | |||||
Sequence: MRTLWIMAVLLVGVEG | ||||||
Chain | PRO_0000413804 | 17-138 | Acidic phospholipase A2 BthA-1 | |||
Sequence: SLWQFGKMINYVMGESGVLQYLSYGCYCGLGGQGQPTDATDRCCFVHDCCYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTCFRDNKDTYDIKYWFYGAKNCQEKSEPC | ||||||
Disulfide bond | 42↔131 | |||||
Sequence: CYCGLGGQGQPTDATDRCCFVHDCCYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTCFRDNKDTYDIKYWFYGAKNC | ||||||
Disulfide bond | 44↔60 | |||||
Sequence: CGLGGQGQPTDATDRCC | ||||||
Disulfide bond | 59↔111 | |||||
Sequence: CCFVHDCCYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTC | ||||||
Disulfide bond | 65↔138 | |||||
Sequence: CCYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICECDRVATTCFRDNKDTYDIKYWFYGAKNCQEKSEPC | ||||||
Disulfide bond | 66↔104 | |||||
Sequence: CYGKVTGCDPKIDSYTYSKKNGDVVCGGDDPCKKQICEC | ||||||
Disulfide bond | 73↔97 | |||||
Sequence: CDPKIDSYTYSKKNGDVVCGGDDPC | ||||||
Disulfide bond | 91↔102 | |||||
Sequence: CGGDDPCKKQIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Homodimer; non-covalently linked.
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)15,456
- Last updated2003-03-01 v1
- Checksum513647907BFD0F4E
Keywords
- Technical term