P50393
uniprot
P50393
canonical
activity_regulation
ACTIVITY REGULATION: Activated by cytosolic calcium, which is necessary for binding to membrane lipids. Activated by phosphorylation in response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
uniprot
proteins
amino_acid_sequence
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRRQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSTTLSSLKEKVSAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEDAEREYQNDNQASWVHRMLMALVSDSALFNTREGRAGKEHNFMLGLNLNTSYPLSPLRDFSPQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQNPSRCSVSLSNVEARKFFNKEFLSKPTAESI
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
function
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 (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 lysophospholipids 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). {ECO:0000250|UniProtKB:P47712, ECO:0000250|UniProtKB:P47713}.
uniprot
proteins
mass_dalton
85707
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism. {ECO:0000250|UniProtKB:P47713}.; PATHWAY: Lipid metabolism; prostaglandin biosynthesis. {ECO:0000250|UniProtKB:P47712}.; PATHWAY: Lipid metabolism; leukotriene B4 biosynthesis. {ECO:0000250|UniProtKB:P47712}.
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at both Ser-505 and Ser-727 in response to mitogenic stimuli. {ECO:0000250|UniProtKB:P47712}.
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
7808237
uniprot
proteins
pubmed
7898324
uniprot
proteins
pubmed
9555100
uniprot
proteins
sequence_length
752
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
uniprot
proteins