Pla2g6
entrez
360426
canonical
uniprot
P97570
canonical
ensembl
ENSRNOG00000012295
resolver
ensp
ENSRNOP00000016827
resolver
ensp
ENSRNOP00000017104
resolver
ensp
ENSRNOP00000072104
resolver
ensp
ENSRNOP00000100746
resolver
ensp
ENSRNOP00000108803
resolver
enst
ENSRNOT00000016827
resolver
enst
ENSRNOT00000017108
resolver
enst
ENSRNOT00000153317
resolver
genesymbol
Pla2g6
resolver
genesymbol_syn
Pnpla9
resolver
uniprot
A0A8L2Q8C9
resolver
uniprot
A0A8L2Q8G5
resolver
uniprot
A0ABK0LGY9
resolver
uniprot
G3V7M8
resolver
uniprot
Q66HD1
resolver
uniprot_entry
A0A8L2Q8C9_RAT
resolver
uniprot_entry
A0A8L2Q8G5_RAT
resolver
uniprot_entry
A0ABK0LGY9_RAT
resolver
uniprot_entry
PLPL9_RAT
resolver
uniprot_sec
G3V7M8
resolver
uniprot_sec
Q66HD1
resolver
activity_regulation
ACTIVITY REGULATION: Activated by ATP (PubMed:18937505, PubMed:9111008). Inhibited by calcium-activated calmodulin (PubMed:11118454, PubMed:18937505). Inhibited by bromoenol lactone (BEL) (PubMed:18937505). {ECO:0000269|PubMed:11118454, ECO:0000269|PubMed:18937505, ECO:0000269|PubMed:9111008}.
uniprot
proteins
amino_acid_sequence
MQFFGRLVNTLSSVTNLFSNPFRVKEVSLADYASSERVREEGQLILLQNASNRTWDCVLVSPRNPQSGFRLFQLESEADALVNFQQYSSQLPPFYESSVQVLHVEVLQHLTDLIRNHPSWTVTHLAVELGIRECFHHSRIISCANSTENEEGCTPLHLACRKGDSEILVELVQYCHAQMDVTDNKGETAFHYAVQGDNPQVLQLLGKNASAGLNQVNNQGLTPLHLACQMGKQEMVRVLLLCNARCNIMGPGGFPIHTAMKFSQKGCAEMIISMDSNQIHSKDPRYGASPLHWAKNAEMARMLLKRGCDVDSTSASGNTALHVAVTRNRFDCVMVLLTYGANAGARGEHGNTPLHLAMSKDNMEMVKALIVFGAEVDTPNDFGETPAFIASKISKLITRKALLTLLKTVGADYHFPFIQGVSTEQSSAAGPHPFFSLDRTQPPTISLNNLELQDLMPVSRARKPAFILSSMRDEKRSHDHLLCLDGGGVKGLVIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGVYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVKKPKVMLTGTLSDRQPAELHLFRNYDAPEAVREPRCTPNINLKPPTQPADQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDMIRKGQGNKVKKLSIVVSLGTGKSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGSDIMLDEVSDAVLVNALWETEVYIYEHREEFQKLVQLLLSP
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, PubMed:9111008). 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) (PubMed:18937505). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:24648512). 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 (By similarity). {ECO:0000250|UniProtKB:A0A3L7I2I8, ECO:0000250|UniProtKB:O60733, ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:18937505, ECO:0000269|PubMed:24648512, ECO:0000269|PubMed:9111008}.
uniprot
proteins
mass_dalton
89556
uniprot
proteins
pubmed
11118454
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18937505
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
24648512
uniprot
proteins
pubmed
9111008
uniprot
proteins
sequence_length
807
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60733}. Cell membrane {ECO:0000250|UniProtKB:O60733}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. 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