PLA2G6
entrez
8398
canonical
uniprot
O60733
canonical
ensembl
ENSG00000184381
resolver
ensp
ENSP00000333142
resolver
ensp
ENSP00000335149
resolver
ensp
ENSP00000386100
resolver
ensp
ENSP00000555203
resolver
ensp
ENSP00000555204
resolver
ensp
ENSP00000555205
resolver
genesymbol
PLA2G6
resolver
genesymbol_syn
PLPLA9
resolver
hgnc
HGNC:9039
resolver
uniprot
A8K597
resolver
uniprot
B0QYE8
resolver
uniprot
O75645
resolver
uniprot
Q8N452
resolver
uniprot
Q9UG29
resolver
uniprot
Q9UIT0
resolver
uniprot
Q9Y671
resolver
uniprot_entry
PLPL9_HUMAN
resolver
uniprot_sec
A8K597
resolver
uniprot_sec
B0QYE8
resolver
uniprot_sec
O75645
resolver
uniprot_sec
Q8N452
resolver
uniprot_sec
Q9UG29
resolver
uniprot_sec
Q9UIT0
resolver
uniprot_sec
Q9Y671
resolver
activity_regulation
ACTIVITY REGULATION: Activated by ATP (PubMed:10092647). Inhibited by calcium-activated calmodulin (By similarity). Inhibited by bromoenol lactone (BEL) (By similarity). {ECO:0000250|UniProtKB:P97570, ECO:0000269|PubMed:10092647}.
uniprot
proteins
amino_acid_sequence
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHGVPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLLLSP
uniprot
proteins
disease_involvement
DISEASE: Neurodegeneration with brain iron accumulation 2B (NBIA2B) [MIM:610217]: A neurodegenerative disorder associated with iron accumulation in the brain, primarily in the basal ganglia. It is characterized by progressive extrapyramidal dysfunction leading to rigidity, dystonia, dysarthria and sensorimotor impairment. {ECO:0000269|PubMed:16783378}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Neurodegeneration with brain iron accumulation 2A (NBIA2A) [MIM:256600]: A neurodegenerative disease characterized by pathologic axonal swelling and spheroid bodies in the central nervous system. Onset is within the first 2 years of life with death by age 10 years. {ECO:0000269|PubMed:16783378, ECO:0000269|PubMed:17033970, ECO:0000269|PubMed:23749988, ECO:0000269|PubMed:39796207}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Parkinson disease 14 (PARK14) [MIM:612953]: An adult-onset progressive neurodegenerative disorder characterized by parkinsonism, dystonia, severe cognitive decline, cerebral and cerebellar atrophy and absent iron in the basal ganglia on magnetic resonance imaging. {ECO:0000269|PubMed:18570303}. Note=The disease is caused by variants affecting the gene represented in this entry.
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:10092647, PubMed:10336645, PubMed:20886109, PubMed:9417066). 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 (PubMed:10092647, PubMed:10336645, PubMed:20886109). Can further hydrolyze lysophospholipids carrying saturated fatty acyl chains (lysophospholipase activity) (PubMed:20886109). Upon oxidative stress, contributes to remodeling of mitochondrial phospholipids in pancreatic beta cells, in a repair mechanism to reduce oxidized lipid content (PubMed:23533611). Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains from cardiolipins, yielding monolysocardiolipins that can be reacylated with unoxidized fatty acyls to regenerate native cardiolipin species (By similarity). Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic islets, releasing oxidized polyunsaturated fatty acids such as hydroxyeicosatetraenoates (HETEs) (By similarity). 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:20886109). 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 (PubMed:18208975). 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 (By similarity). 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:P97570, ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:10092647, ECO:0000269|PubMed:10336645, ECO:0000269|PubMed:18208975, ECO:0000269|PubMed:20886109, ECO:0000269|PubMed:23533611, ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-1]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.; FUNCTION: [Isoform Ankyrin-iPLA2-2]: Lacks the catalytic domain and may act as a negative regulator of the catalytically active isoforms. {ECO:0000269|PubMed:9417066}.
uniprot
proteins
mass_dalton
89903
uniprot
proteins
mutagenesis
MUTAGEN 519; /note="S->A: Abolishes phospholipase and lysophospholipase activities."; /evidence="ECO:0000269|PubMed:20886109
uniprot
proteins
pubmed
10092647
uniprot
proteins
pubmed
10336645
uniprot
proteins
pubmed
10591208
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15461802
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16783378
uniprot
proteins
pubmed
17033970
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
18208975
uniprot
proteins
pubmed
18570303
uniprot
proteins
pubmed
19029121
uniprot
proteins
pubmed
19164547
uniprot
proteins
pubmed
20886109
uniprot
proteins
pubmed
23533611
uniprot
proteins
pubmed
23749988
uniprot
proteins
pubmed
28887846
uniprot
proteins
pubmed
39796207
uniprot
proteins
pubmed
9417066
uniprot
proteins
sequence_length
806
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18208975}. Cell membrane {ECO:0000269|PubMed:18208975}. Mitochondrion {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium {ECO:0000269|PubMed:18208975}. Note=Recruited to the membrane-enriched pseudopods upon MCP1/CCL2 stimulation in monocytes. {ECO:0000269|PubMed:18208975}.
uniprot
proteins
transmembrane_region
TRANSMEM 480..500; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 511..531; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins