A7LCJ2 · PA2_URTCR
- ProteinPhospholipase A2 A2-actitoxin-Ucs2a
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids155 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Miscellaneous
Lacks hemolytic activity on bovine red blood cells as well as neurotoxic activities.
mRNA is obtained from a single animal, whereas the protein is isolated from exudates of several specimens.
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 | |
Cellular Component | nematocyst | |
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 namePhospholipase A2 A2-actitoxin-Ucs2a
- EC number
- Short namesA2-AITX-Ucs2a
- Alternative names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Cnidaria > Anthozoa > Hexacorallia > Actiniaria > Actiniidae > Urticina
Accessions
- Primary accessionA7LCJ2
Subcellular Location
PTM/Processing
Features
Showing features for signal, propeptide, chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-19 | |||||
Sequence: MKNNIILVILLGISVFVDC | ||||||
Propeptide | PRO_0000413798 | 20-42 | ||||
Sequence: LPLNDQEEDKSLNAQESEVSAVQ | ||||||
Chain | PRO_0000413799 | 45-155 | Phospholipase A2 A2-actitoxin-Ucs2a | |||
Sequence: DILQFSGMIRCATGRSAWKYFNYGNWCGWGGSGTAVDGVDSCCRSHDWCYKRHDSCYPKIIPYIASTSGSHPSCSITCHSANNRCQRDVCNCDKVAAECFARNTYHPNNKH | ||||||
Disulfide bond | 55↔118 | |||||
Sequence: CATGRSAWKYFNYGNWCGWGGSGTAVDGVDSCCRSHDWCYKRHDSCYPKIIPYIASTSGSHPSC | ||||||
Disulfide bond | 71↔87 | |||||
Sequence: CGWGGSGTAVDGVDSCC | ||||||
Disulfide bond | 86↔143 | |||||
Sequence: CCRSHDWCYKRHDSCYPKIIPYIASTSGSHPSCSITCHSANNRCQRDVCNCDKVAAEC | ||||||
Disulfide bond | 93↔136 | |||||
Sequence: CYKRHDSCYPKIIPYIASTSGSHPSCSITCHSANNRCQRDVCNC | ||||||
Disulfide bond | 100↔129 | |||||
Sequence: CYPKIIPYIASTSGSHPSCSITCHSANNRC | ||||||
Disulfide bond | 122↔134 | |||||
Sequence: CHSANNRCQRDVC |
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length155
- Mass (Da)17,319
- Last updated2007-09-11 v1
- ChecksumD4C567640BA93626
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 45-46 | in Ref. 1; AA sequence | ||||
Sequence: DI → NL | ||||||
Sequence conflict | 51 | in Ref. 1; AA sequence | ||||
Sequence: G → S | ||||||
Sequence conflict | 54 | in Ref. 1; AA sequence | ||||
Sequence: R → K | ||||||
Sequence conflict | 65 | in Ref. 1; AA sequence | ||||
Sequence: F → D |
Keywords
- Technical term