Protein Name:
Cytosolic phospholipase A2
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UniprotKB/SwissProt ID: P47713 (P47713)
Gene Name:
Pla2g4a
Organism: Mus musculus (Mouse)
Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (PubMed:1904318, PubMed:9403692, PubMed:9403693). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (PubMed:9403692, PubMed:9403693). 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)
Other Modifications: View all modification sites in dbPTM
Protein Subcellular Localization: Cytoplasm. Golgi apparatus membrane. Nucleus envelope
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Graphical Visualization of S-nitrosylation Sites:
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The S-nitrosylation sites of P47713
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| No. |
Position |
S-nitrosylated Peptide |
Secondary Structure of S-nitrosylated Peptide |
Solvent Accessibility of nitrosylated Site |
PubMed ID |
| 1 |
151 |
CPDLRFSMAL C DQEKTFRQQR |
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| 2 |
725 |
IEYRRQNPSR C SVSLSNVEAR |
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