P00598 · PA2A1_NAJAT
- ProteinAcidic phospholipase A2 1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids146 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Snake venom phospholipase A2 (PLA2) that has high affinity for muscarinic acetylcholine receptors mAChRs (CHRM) and has the ability to activate them. In guinea-pig ileum, produces an onset and dose-dependent contraction. Has also weak anticoagulant 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 per subunit.
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 1
- EC number
- Short namessvPLA2
- Alternative names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Lepidosauria > Squamata > Bifurcata > Unidentata > Episquamata > Toxicofera > Serpentes > Colubroidea > Elapidae > Elapinae > Naja
Accessions
- Primary accessionP00598
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-21 | |||||
Sequence: MTPAHLLILAAVCVSPLGASS | ||||||
Propeptide | PRO_0000022916 | 22-27 | ||||
Sequence: NRPMPL | ||||||
Chain | PRO_0000022917 | 28-146 | Acidic phospholipase A2 1 | |||
Sequence: NLYQFKNMIQCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARCQ | ||||||
Disulfide bond | 38↔98 | |||||
Sequence: CTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYEC | ||||||
Disulfide bond | 53↔145 | |||||
Sequence: CYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAICFAGAPYNNNNYNIDLKARC | ||||||
Disulfide bond | 55↔71 | |||||
Sequence: CGRGGSGTPVDDLDRCC | ||||||
Disulfide bond | 70↔126 | |||||
Sequence: CCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDCDRLAAIC | ||||||
Disulfide bond | 77↔119 | |||||
Sequence: CYNEAEKISGCWPYFKTYSYECSQGTLTCKGGNNACAAAVCDC | ||||||
Disulfide bond | 87↔112 | |||||
Sequence: CWPYFKTYSYECSQGTLTCKGGNNAC | ||||||
Disulfide bond | 105↔117 | |||||
Sequence: CKGGNNACAAAVC |
Keywords
- PTM
Expression
Tissue specificity
Expressed by the venom gland.
Interaction
Subunit
Homodimer.
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.
- Length146
- Mass (Da)16,013
- Last updated1994-02-01 v2
- Checksum862EDF47654BFF93
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 111-112 | in Ref. 2; AA sequence | ||||
Sequence: AC → CA | ||||||
Sequence conflict | 134-136 | in Ref. 2; AA sequence | ||||
Sequence: NNN → DND | ||||||
Sequence conflict | 140 | in Ref. 2; AA sequence | ||||
Sequence: D → N | ||||||
Sequence conflict | 146 | in Ref. 2; AA sequence | ||||
Sequence: Q → QE |
Mass Spectrometry
Keywords
- Technical term