UniProt ID: B3DFL0 |
CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000256|RuleBase:RU362102}; DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. {ECO:0000256|RuleBase:RU362102}. |
UniProt ID: P50392 |
FUNCTION: Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response. CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn- glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; ACTIVITY REGULATION: Stimulated by agonists such as ATP, EGF, thrombin and bradykinin as well as by cytosolic Ca(2+). SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Translocates to membrane vesicles in a calcium- dependent fashion. {ECO:0000250}. DOMAIN: The N-terminal C2 domain associates with lipid membranes upon calcium binding. It modulates enzyme activity by presenting the active site to its substrate in response to elevations of cytosolic Ca(2+) (By similarity). {ECO:0000250}. PTM: Activated by phosphorylation on a serine residue. {ECO:0000250}. |
This information was provided by UniProt through a collaboration with ZFIN. (1) |