true2008-07-222023-11-0899PA24A_RABITMolecular cloning of cDNA coding for phospholipase A2.Al-Khalili O.K.Eaton D.C.1999-11EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [MRNA]New Zealand whiteHeartEukaryotaEukaryotaC2_cPLA2cPLA2_Grp-IVAC2 domainCytosolic phospholipase A2 catalytic domainAcyl_Trfase/lysoPLipaseC2_cPLA2C2_domC2_domain_sfLysoPLipase_cat_domCYTOSOLIC PHOSPHOLIPASE A2CYTOSOLIC PHOSPHOLIPASE A2C2PLA2_BC2PLAcC2 domain (Calcium/lipid-binding domain, CaLB)FabD/lysophospholipase-likeC2PLA2CCytosolic phospholipase A2cPLA2Phospholipase A2 group IVAPhospholipase A23.1.1.4Phosphatidylcholine 2-acylhydrolaseLysophospholipase3.1.1.5PLA2G4ACPLA2PLA2G4Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).Activated by cytosolic calcium, which is necessary for binding to membrane lipids. Activated by phosphorylation in response to mitogenic stimuli.Interacts with KAT5.Translocates to intracellular membranes in a calcium-dependent way.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 calcium. In the presence of phosphoinositides, regulates phospholipase A2 and lysophospholipase activities in a calcium-independent way.Phosphorylated at both Ser-505 and Ser-726 in response to mitogenic stimuli.Cytosolic phospholipase A2852351748C26122PLA2c138739Phospholipid binding178Disordered428458Nucleophile228Proton acceptor54840414365939495Phosphoserine2Phosphothreonine268Phosphoserine434Phosphoserine435Phosphoserine437Phosphoserine; by MAPK505Phosphoserine514Phosphoserine726Phosphoserine728Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)540Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)605122000-05-011852351ad3ff906374e32677302eff0775b5f7MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFIATTPDSRKRTRHFNNDINPVWNEAFEFILDPNQGNVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSSPDLRFSMALCDQEKAFRQQRKENIKENMRKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYIAGLSGSTWYMSTLYSHPDFPEKGPQEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIHNRMHTTLSSLKEKVSSAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSHNKGSTMEEELENITAKHIVSNDSSDSDDESQEPKGTEGEDAEREYQNDHQASWVHRMLMALVSDSALFNTREGRAGKVHNFMLGLNLNTSYPLSPLRDFTQESFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPIIIHFVLANINFRKYKSPGVPRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAMVESIEYRRQNPSRCSVSLSNVEARRFFNKEFLSKPTAtruetruetruetruetruetruetrue