P0DUN3 · PA2A1_BOTBZ
- ProteinAcidic phospholipase A2 braziliase-I
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids107 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that induces significant edematogenic activity. Shows mild cytotoxicity on Trypanosoma cruzi and Leishmania infantum. Also inhibits ADP- and collagen-induced platelet aggregation. Does not show myotoxic activity.
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.
pH Dependence
Optimum pH is 5.5-8.5.
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
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcidic phospholipase A2 braziliase-I
- 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 accessionP0DUN3
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000452894 | 1-107 | Acidic phospholipase A2 braziliase-I | |||
Sequence: NLWQFEMLIMKIALTSGFMFYSSYGCYCGWGGHGRPKDASDRCCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXCQEESDPC | ||||||
Disulfide bond | 26↔100 | |||||
Sequence: CYCGWGGHGRPKDASDRCCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXC | ||||||
Disulfide bond | 28↔44 | |||||
Sequence: CGWGGHGRPKDASDRCC | ||||||
Disulfide bond | 43↔86 | |||||
Sequence: CCFVHDCCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATC | ||||||
Disulfide bond | 49↔107 | |||||
Sequence: CCYGKVTTCNPKFGVVVCGGDDPCKKQICECDRVAATCFRDNKYWFYGAKXCQEESDPC | ||||||
Disulfide bond | 50↔79 | |||||
Sequence: CYGKVTTCNPKFGVVVCGGDDPCKKQICEC | ||||||
Disulfide bond | 57↔72 | |||||
Sequence: CNPKFGVVVCGGDDPC | ||||||
Disulfide bond | 66↔77 | |||||
Sequence: CGGDDPCKKQIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Monomer.
Structure
Family & Domains
Sequence similarities
Family and domain databases
Sequence
- Sequence statusFragments
- Length107
- Mass (Da)12,108
- Last updated2021-06-02 v1
- Checksum3E7FE7ECBD6A14A2
Features
Showing features for non-adjacent residues.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-adjacent residues | 61-62 | |||||
Sequence: FG | ||||||
Non-adjacent residues | 89-90 | |||||
Sequence: DN |
Mass Spectrometry
Keywords
- Technical term