P80966 · PA2A1_OPHHA
- ProteinAcidic phospholipase A2 1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids151 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that may exhibit cardiotoxicity, myotoxicity, antiplatelet activity, and edema-inducing activity. 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.
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 | signaling receptor binding | |
Molecular Function | toxin activity | |
Biological Process | arachidonic acid secretion | |
Biological Process | fatty acid biosynthetic process | |
Biological Process | lipid catabolic process | |
Biological Process | phospholipid metabolic process | |
Biological Process | positive regulation of fibroblast proliferation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameAcidic phospholipase A2 1
- EC number
- Short namessvPLA2
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Elapidae > Elapinae > Ophiophagus
Accessions
- Primary accessionP80966
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MNPAHLLVLSAVCVSLLGASS | ||||||
Propeptide | PRO_0000022942 | 22-27 | ||||
Sequence: IPPQPL | ||||||
Chain | PRO_0000022943 | 28-151 | Acidic phospholipase A2 1 | |||
Sequence: HLIQFGNMIQCTVPGFLSWIKYADYGCYCGAGGSGTPVDKLDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSERTVTCKADNDECAAFICNCDRVAAHCFAASPYNNNNYNIDTTTRC | ||||||
Disulfide bond | 38↔104 | |||||
Sequence: CTVPGFLSWIKYADYGCYCGAGGSGTPVDKLDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDC | ||||||
Disulfide bond | 54↔151 | |||||
Sequence: CYCGAGGSGTPVDKLDRCCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSERTVTCKADNDECAAFICNCDRVAAHCFAASPYNNNNYNIDTTTRC | ||||||
Disulfide bond | 56↔72 | |||||
Sequence: CGAGGSGTPVDKLDRCC | ||||||
Disulfide bond | 71↔132 | |||||
Sequence: CCQVHDNCYTQAQKLPACSSIMDSPYVKIYSYDCSERTVTCKADNDECAAFICNCDRVAAHC | ||||||
Disulfide bond | 78↔125 | |||||
Sequence: CYTQAQKLPACSSIMDSPYVKIYSYDCSERTVTCKADNDECAAFICNC | ||||||
Disulfide bond | 88↔118 | |||||
Sequence: CSSIMDSPYVKIYSYDCSERTVTCKADNDEC | ||||||
Disulfide bond | 111↔123 | |||||
Sequence: CKADNDECAAFIC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
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.
- Length151
- Mass (Da)16,444
- Last updated2002-08-30 v2
- ChecksumF1E021B886BC4BEB
Mass Spectrometry
Keywords
- Technical term