Pla2g6
entrez
53357
canonical
uniprot
P97819
canonical
ensembl
ENSMUSG00000042632
resolver
ensp
ENSMUSP00000044234
resolver
ensp
ENSMUSP00000131081
resolver
ensp
ENSMUSP00000132071
resolver
ensp
ENSMUSP00000134456
resolver
ensp
ENSMUSP00000134672
resolver
ensp
ENSMUSP00000264216
resolver
ensp
ENSMUSP00000264218
resolver
ensp
ENSMUSP00000264219
resolver
ensp
ENSMUSP00000264220
resolver
ensp
ENSMUSP00000264241
resolver
ensp
ENSMUSP00000264245
resolver
ensp
ENSMUSP00000343637
resolver
genesymbol
Pla2g6
resolver
genesymbol_syn
Pnpla9
resolver
uniprot
Q3U613
resolver
uniprot
Q3UN31
resolver
uniprot
Q99LA9
resolver
uniprot
Q9JK61
resolver
uniprot_entry
PLPL9_MOUSE
resolver
uniprot_entry
Q3U613_MOUSE
resolver
uniprot_entry
Q3UN31_MOUSE
resolver
uniprot_sec
Q99LA9
resolver
uniprot_sec
Q9JK61
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by calcium-activated calmodulin (By similarity). Activated by ATP (PubMed:17895289, PubMed:18937505). Inhibited by bromoenol lactone (BEL) (PubMed:17895289, PubMed:18937505). {ECO:0000250|UniProtKB:P97570, ECO:0000269|PubMed:17895289, ECO:0000269|PubMed:18937505}.
uniprot
proteins
amino_acid_sequence
MQFFGRLVNTLSSVTNLFSNPFRVKEVSLTDYVSSERVREEGQLILLQNVSNRTWDCVLVSPRNPQSGFRLFQLESEADALVNFQQFSSQLPPFYESSVQVLHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACKMGKQEMVRVLLLCNARCNIMGPGGFPIHTAMKFSQKGCAEMIISMDSNQIHSKDPRYGASPLHWAKNAEMARMLLKRGCDVDSTSSSGNTALHVAVMRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPALIASKISKLITRKALLTLLKTVGADHHFPIIQGVSTEQGSAAATHPLFSLDRTQPPAISLNNLELQDLMPISRARKPAFILSSMRDEKRSHDHLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREPRCNQNINLKPPTQPADQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHREEFQKLVQLLLSP
uniprot
proteins
ec_number
3.1.1.4
uniprot
proteins
ec_number
3.1.1.5
uniprot
proteins
ec_number
3.1.2.2
uniprot
proteins
function
FUNCTION: Calcium-independent phospholipase involved in phospholipid remodeling with implications in cellular membrane homeostasis, mitochondrial integrity and signal transduction. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 or sn-2 position of phospholipids (phospholipase A1 and A2 activity respectively), producing lysophospholipids that are used in deacylation-reacylation cycles (PubMed:18937505). Hydrolyzes both saturated and unsaturated long fatty acyl chains in various glycerophospholipid classes such as phosphatidylcholines, phosphatidylethanolamines and phosphatidates, with a preference for hydrolysis at sn-2 position. Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (By similarity). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species. Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (PubMed:24648512). Has thioesterase activity toward fatty-acyl CoA releasing CoA-SH known to facilitate fatty acid transport and beta-oxidation in mitochondria particularly in skeletal muscle (PubMed:18937505). Plays a role in regulation of membrane dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl group in plasmalogen phospholipids, structural components of lipid rafts and myelin (By similarity). Regulates F-actin polymerization at the pseudopods, which is required for both speed and directionality of MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane phospholipids to produce potent lipid signaling messengers. Generates lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G protein receptors in various cell types. Has phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in inactivation of this potent pro-inflammatory signaling lipid (By similarity). In response to glucose, amplifies calcium influx in pancreatic beta cells to promote INS secretion (PubMed:17895289). {ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:O60733, ECO:0000269|PubMed:17895289, ECO:0000269|PubMed:18937505, ECO:0000269|PubMed:24648512}.
uniprot
proteins
mass_dalton
89560
uniprot
proteins
pubmed
11563837
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17895289
uniprot
proteins
pubmed
18305254
uniprot
proteins
pubmed
18937505
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21813701
uniprot
proteins
pubmed
24648512
uniprot
proteins
pubmed
9079688
uniprot
proteins
sequence_length
807
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11563837}. Cell membrane {ECO:0000269|PubMed:11563837}. Mitochondrion {ECO:0000269|PubMed:24648512}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:O60733}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:0000250|UniProtKB:O60733}.
uniprot
proteins
transmembrane_region
TRANSMEM 481..501; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 512..532; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins