PLPL9_CRIGR
ID PLPL9_CRIGR Reviewed; 807 AA.
AC A0A3L7I2I8; A0A384E119;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=85/88 kDa calcium-independent phospholipase A2;
DE Short=CaI-PLA2;
DE EC=3.1.1.4;
DE AltName: Full=2-lysophosphatidylcholine acylhydrolase;
DE EC=3.1.1.5;
DE AltName: Full=Group VI phospholipase A2;
DE Short=GVI PLA2;
DE AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 beta;
DE Short=iPLA2-beta;
DE AltName: Full=PLA2G6;
DE AltName: Full=Palmitoyl-CoA hydrolase;
DE EC=3.1.2.2;
DE AltName: Full=Patatin-like phospholipase domain-containing protein 9;
DE Short=PNPLA9;
GN Name=PLA2G6; Synonyms=PLPLA9;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17A/GY; TISSUE=Liver;
RX PubMed=29704459; DOI=10.1002/bit.26722;
RA Rupp O., MacDonald M.L., Li S., Dhiman H., Polson S., Griep S., Heffner K.,
RA Hernandez I., Brinkrolf K., Jadhav V., Samoudi M., Hao H., Kingham B.,
RA Goesmann A., Betenbaugh M.J., Lewis N.E., Borth N., Lee K.H.;
RT "A reference genome of the Chinese hamster based on a hybrid assembly
RT strategy.";
RL Biotechnol. Bioeng. 115:2087-2100(2018).
RN [2]
RP IDENTIFICATION (ISOFORM SHORT), FUNCTION, CATALYTIC ACTIVITY, AND
RP MUTAGENESIS OF SER-520.
RX PubMed=9079687; DOI=10.1074/jbc.272.13.8567;
RA Tang J., Kriz R.W., Wolfman N., Shaffer M., Seehra J., Jones S.S.;
RT "A novel cytosolic calcium-independent phospholipase A2 contains eight
RT ankyrin motifs.";
RL J. Biol. Chem. 272:8567-8575(1997).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=15908428; DOI=10.1074/jbc.m502358200;
RA Yan W., Jenkins C.M., Han X., Mancuso D.J., Sims H.F., Yang K., Gross R.W.;
RT "The highly selective production of 2-arachidonoyl lysophosphatidylcholine
RT catalyzed by purified calcium-independent phospholipase A2gamma:
RT identification of a novel enzymatic mediator for the generation of a key
RT branch point intermediate in eicosanoid signaling.";
RL J. Biol. Chem. 280:26669-26679(2005).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.95 ANGSTROMS) (ISOFORM SHORT), REPEAT, SUBUNIT,
RP MUTAGENESIS OF TRP-750, ACTIVITY REGULATION, AND DOMAIN.
RX PubMed=29472584; DOI=10.1038/s41467-018-03193-0;
RA Malley K.R., Koroleva O., Miller I., Sanishvili R., Jenkins C.M.,
RA Gross R.W., Korolev S.;
RT "The structure of iPLA2beta reveals dimeric active sites and suggests
RT mechanisms of regulation and localization.";
RL Nat. Commun. 9:765-765(2018).
CC -!- FUNCTION: Calcium-independent phospholipase involved in phospholipid
CC remodeling with implications in cellular membrane homeostasis,
CC mitochondrial integrity and signal transduction. Hydrolyzes the ester
CC bond of the fatty acyl group attached at sn-1 or sn-2 position of
CC phospholipids (phospholipase A1 and A2 activity respectively),
CC producing lysophospholipids that are used in deacylation-reacylation
CC cycles. Hydrolyzes both saturated and unsaturated long fatty acyl
CC chains in various glycerophospholipid classes such as
CC phosphatidylcholines, phosphatidylethanolamines and phosphatidates,
CC with a preference for hydrolysis at sn-2 position (PubMed:9079687,
CC PubMed:15908428). Can further hydrolyze lysophospholipids carrying
CC saturated fatty acyl chains (lysophospholipase activity)
CC (PubMed:9079687). Upon oxidative stress, contributes to remodeling of
CC mitochondrial phospholipids in pancreatic beta cells, in a repair
CC mechanism to reduce oxidized lipid content (By similarity).
CC Preferentially hydrolyzes oxidized polyunsaturated fatty acyl chains
CC from cardiolipins, yielding monolysocardiolipins that can be reacylated
CC with unoxidized fatty acyls to regenerate native cardiolipin species.
CC Hydrolyzes oxidized glycerophosphoethanolamines present in pancreatic
CC islets, releasing oxidized polyunsaturated fatty acids such as
CC hydroxyeicosatetraenoates (HETEs) (By similarity). Has thioesterase
CC activity toward fatty-acyl CoA releasing CoA-SH known to facilitate
CC fatty acid transport and beta-oxidation in mitochondria particularly in
CC skeletal muscle (By similarity). Plays a role in regulation of membrane
CC dynamics and homeostasis. Selectively hydrolyzes sn-2 arachidonoyl
CC group in plasmalogen phospholipids, structural components of lipid
CC rafts and myelin (PubMed:9079687). Regulates F-actin polymerization at
CC the pseudopods, which is required for both speed and directionality of
CC MCP1/CCL2-induced monocyte chemotaxis (By similarity). Targets membrane
CC phospholipids to produce potent lipid signaling messengers. Generates
CC lysophosphatidate (LPA, 1-acyl-glycerol-3-phosphate), which acts via G-
CC protein receptors in various cell types (PubMed:9079687). Has
CC phospholipase A2 activity toward platelet-activating factor (PAF, 1-O-
CC alkyl-2-acetyl-sn-glycero-3-phosphocholine), likely playing a role in
CC inactivation of this potent pro-inflammatory signaling lipid
CC (PubMed:9079687). In response to glucose, amplifies calcium influx in
CC pancreatic beta cells to promote INS secretion (By similarity).
CC {ECO:0000250|UniProtKB:O60733, ECO:0000250|UniProtKB:P97570,
CC ECO:0000250|UniProtKB:P97819, ECO:0000269|PubMed:15908428,
CC ECO:0000269|PubMed:9079687}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-
CC glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:41223, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:72998, ChEBI:CHEBI:72999;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41224;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (9Z)-octadecenoate + 1-hexadecanoyl-sn-glycero-3-
CC phosphocholine + H(+); Xref=Rhea:RHEA:38779, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:72998,
CC ChEBI:CHEBI:73001; Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphocholine + H2O = (9Z,12Z)-octadecadienoate + 1-hexadecanoyl-sn-
CC glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40811,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC ChEBI:CHEBI:72998, ChEBI:CHEBI:73002;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40427, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:72998, ChEBI:CHEBI:73003;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC octadecanoyl-sn-glycero-3-phosphocholine + H(+);
CC Xref=Rhea:RHEA:40519, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73858, ChEBI:CHEBI:74965;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40520;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-
CC hexadecanoyl-sn-glycero-3-phosphoethanolamine + H(+);
CC Xref=Rhea:RHEA:40431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:32395, ChEBI:CHEBI:73004, ChEBI:CHEBI:73009;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1-
CC hexadecanoyl-sn-glycero-3-phosphate + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:63304, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57518, ChEBI:CHEBI:72859;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63305;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid +
CC H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870,
CC ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5;
CC Evidence={ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC Evidence={ECO:0000305|PubMed:15908428, ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-sn-glycero-3-phosphocholine + H2O = H(+) +
CC hexadecanoate + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:40435,
CC ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16870, ChEBI:CHEBI:72998;
CC Evidence={ECO:0000269|PubMed:15908428, ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC Evidence={ECO:0000305|PubMed:15908428, ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine
CC + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40831, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:74344; Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40832;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphocholine
CC + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + sn-glycerol 3-
CC phosphocholine; Xref=Rhea:RHEA:40827, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:76079; Evidence={ECO:0000269|PubMed:15908428};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40828;
CC Evidence={ECO:0000305|PubMed:15908428};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + 1-O-
CC hexadecyl-sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:41067,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC ChEBI:CHEBI:55430, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41068;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-O-hexadecyl-2-acetyl-sn-glycero-3-phosphocholine + H2O = 1-
CC O-hexadecyl-sn-glycero-3-phosphocholine + acetate + H(+);
CC Xref=Rhea:RHEA:40479, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30089, ChEBI:CHEBI:44811, ChEBI:CHEBI:64496;
CC Evidence={ECO:0000269|PubMed:9079687};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40480;
CC Evidence={ECO:0000305|PubMed:9079687};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + hexadecanoyl-CoA = CoA + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:16645, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57379; EC=3.1.2.2;
CC Evidence={ECO:0000250|UniProtKB:O60733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16646;
CC Evidence={ECO:0000250|UniProtKB:O60733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H2O = (9Z)-octadecenoate + 1'-[1,2-di-(9Z-octadecenoyl)-
CC sn-glycero-3-phospho]-3'-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40463, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77253,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:O60733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40464;
CC Evidence={ECO:0000250|UniProtKB:O60733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1'-[1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho]-3'-[1-(9Z-
CC octadecenoyl)-sn-glycero-3-phospho]-glycerol + H2O = (9Z)-
CC octadecenoate + 1',3'-bis-[1-(9Z-octadecenoyl)-sn-glycero-3-phospho]-
CC glycerol + H(+); Xref=Rhea:RHEA:40467, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:77256,
CC ChEBI:CHEBI:77259; Evidence={ECO:0000250|UniProtKB:O60733};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40468;
CC Evidence={ECO:0000250|UniProtKB:O60733};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1',3'-bis-[1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phospho]-glycerol + H2O = (9Z,12Z)-octadecadienoate + 1'-[1,2-di-
CC (9Z,12Z-octadecadienoyl)-sn-glycero-3-phospho]-3'-[1-(9Z,12Z-
CC octadecadienoyl)-sn-glycero-3-phospho]-glycerol + H(+);
CC Xref=Rhea:RHEA:52812, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:83580, ChEBI:CHEBI:83581;
CC Evidence={ECO:0000250|UniProtKB:P97819};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:52814;
CC Evidence={ECO:0000250|UniProtKB:P97819};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-octadecanoyl-2-(15-hydroxy-(5Z,8Z,11Z,13E)-
CC eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine + H2O = 1-
CC octadecanoyl-sn-glycero-3-phosphoethanolamine + 15-hydroxy-
CC (5Z,8Z,11Z,13E)-eicosatetraenoate + H(+); Xref=Rhea:RHEA:63256,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:75036,
CC ChEBI:CHEBI:78832, ChEBI:CHEBI:146277;
CC Evidence={ECO:0000250|UniProtKB:P97570};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:63257;
CC Evidence={ECO:0000250|UniProtKB:P97570};
CC -!- ACTIVITY REGULATION: Activated by ATP (By similarity). Inhibited by
CC calcium-activated calmodulin (PubMed:29472584). Inhibited by bromoenol
CC lactone (BEL) (By similarity). {ECO:0000250|UniProtKB:P97570,
CC ECO:0000269|PubMed:29472584}.
CC -!- SUBUNIT: Homodimer formed by catalytic domains tightly interacting
CC through a large hydrophobic interface. The contact area involves 3
CC alpha helices, several loops and a part of the beta sheet from each
CC monomer. Both active sites of the dimer are in close proximity adopting
CC an open conformation that provide sufficient space for phospholipid
CC access while favoring cooperativity in deacylation-reacylation
CC reactions. Each monomer has 9 ankyrin repeats stacked side-by-side in
CC an elongated structure oriented outwards from the catalytic core.
CC {ECO:0000269|PubMed:29472584}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O60733}. Cell
CC membrane {ECO:0000250|UniProtKB:O60733}. Mitochondrion
CC {ECO:0000250|UniProtKB:P97819}. Cell projection, pseudopodium
CC {ECO:0000250|UniProtKB:O60733}. Note=Recruited to the membrane-enriched
CC pseudopods upon MCP1/CCL2 stimulation in monocytes.
CC {ECO:0000250|UniProtKB:O60733}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Long;
CC IsoId=A0A3L7I2I8-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=A0A3L7I2I8-2; Sequence=VSP_060590;
CC -!- DOMAIN: Has two putative calmodulin binding domains, the 1-9-14 and IQ
CC motifs. One calmodulin molecule interacts with PLA2G6 dimer, likely
CC through 1-9-14 motif on each monomer (PubMed:29472584). Binds
CC calmodulin in a calcium-dependent way (By similarity).
CC {ECO:0000250|UniProtKB:P97570, ECO:0000269|PubMed:29472584}.
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DR EMBL; RAZU01000104; RLQ72369.1; -; Genomic_DNA.
DR PDB; 6AUN; X-ray; 3.95 A; A/B=1-752.
DR PDBsum; 6AUN; -.
DR AlphaFoldDB; A0A3L7I2I8; -.
DR SMR; A0A3L7I2I8; -.
DR Ensembl; ENSCGRT00001020680; ENSCGRP00001016436; ENSCGRG00001016761. [A0A3L7I2I8-2]
DR Ensembl; ENSCGRT00001020695; ENSCGRP00001016451; ENSCGRG00001016761. [A0A3L7I2I8-1]
DR Ensembl; ENSCGRT00015004249; ENSCGRP00015003438; ENSCGRG00015002664.
DR Ensembl; ENSCGRT00015004287; ENSCGRP00015003466; ENSCGRG00015002664.
DR Ensembl; ENSCGRT00015004370; ENSCGRP00015003537; ENSCGRG00015002664.
DR GeneTree; ENSGT00940000158756; -.
DR Proteomes; UP000273346; Unassembled WGS sequence.
DR GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0003847; F:1-alkyl-2-acetylglycerophosphocholine esterase activity; IDA:UniProtKB.
DR GO; GO:0047499; F:calcium-independent phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0004622; F:lysophospholipase activity; IDA:UniProtKB.
DR GO; GO:0102991; F:myristoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0016290; F:palmitoyl-CoA hydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR GO; GO:0017171; F:serine hydrolase activity; IEA:Ensembl.
DR GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl.
DR GO; GO:0035965; P:cardiolipin acyl-chain remodeling; IEA:Ensembl.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:Ensembl.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; IDA:UniProtKB.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; IDA:UniProtKB.
DR GO; GO:0046469; P:platelet activating factor metabolic process; IDA:UniProtKB.
DR GO; GO:0035774; P:positive regulation of insulin secretion involved in cellular response to glucose stimulus; ISS:UniProtKB.
DR Gene3D; 1.25.40.20; -; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF13606; Ank_3; 1.
DR Pfam; PF01734; Patatin; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 4.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ANK repeat; Cell membrane;
KW Cell projection; Cytoplasm; Hydrolase; Lipid metabolism; Membrane;
KW Mitochondrion; Phospholipid metabolism; Repeat; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..807
FT /note="85/88 kDa calcium-independent phospholipase A2"
FT /id="PRO_0000450229"
FT TRANSMEM 481..501
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 512..532
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 120..147
FT /note="ANK 1"
FT /evidence="ECO:0000269|PubMed:29472584,
FT ECO:0007744|PDB:6AUN"
FT REPEAT 151..181
FT /note="ANK 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 185..215
FT /note="ANK 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 219..248
FT /note="ANK 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 251..281
FT /note="ANK 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 286..312
FT /note="ANK 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 316..345
FT /note="ANK 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 349..378
FT /note="ANK 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00023,
FT ECO:0000269|PubMed:29472584, ECO:0007744|PDB:6AUN"
FT REPEAT 382..403
FT /note="ANK 9"
FT /evidence="ECO:0000269|PubMed:29472584,
FT ECO:0007744|PDB:6AUN"
FT DOMAIN 482..666
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 678..687
FT /note="Calmodulin-binding (1-9-14 motif)"
FT /evidence="ECO:0000269|PubMed:29472584"
FT REGION 749..760
FT /note="Calmodulin-binding (IQ motif)"
FT /evidence="ECO:0000269|PubMed:29472584"
FT MOTIF 486..491
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 518..522
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 653..655
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 520
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 653
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT VAR_SEQ 396..451
FT /note="LITRKALLSLLRTVGADHRFPLIQGVPTDQSSAATPHPIFSLDKTQPPAISL
FT NNLE -> Q (in isoform Short)"
FT /id="VSP_060590"
FT MUTAGEN 520
FT /note="S->A: Complete loss of phospholipase A2 activity."
FT /evidence="ECO:0000269|PubMed:9079687"
FT MUTAGEN 750
FT /note="W->E: Impaired dimer formation. Complete loss of
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:29472584"
SQ SEQUENCE 807 AA; 89776 MW; B573E942A5C86F8D CRC64;
MQFFGRLVNT LSSVTNLFSN PFRVKEISVA DYTSHERVRE EGQLILFQNA SNRTWDCILV
SPRNPHSGFR LFQLESEADA LVNFQQFSSQ LPPFYESSVQ VLHVEVLQHL SDLIRSHPSW
TVTHLAVELG IRECFHHSRI ISCANSTENE EGCTPLHLAC RKGDSEILVE LVQYCHAQMD
VTDNKGETAF HYAVQGDNSQ VLQLLGKNAS AGLNQVNKQG LTPLHLACQM GKQEMVRVLL
LCNARCNVMG PSGFPIHTAM KFSQKGCAEM IISMDSSQIH SKDPRYGASP LHWAKNAEMA
RMLLKRGCDV DSTSAAGNTA LHVAVMRNRF DCVMVLLTYG ANAGTPGEHG NTPLHLAISK
DNMEMIKALI VFGAEVDTPN DFGETPAFMA SKISKLITRK ALLSLLRTVG ADHRFPLIQG
VPTDQSSAAT PHPIFSLDKT QPPAISLNNL ELQDLMPISR ARKPAFILSS MRDEKRIHDH
LLCLDGGGVK GLVIIQLLIA IEKASGVATK DLFDWVAGTS TGGILALAIL HSKSMAYMRG
VYFRMKDEVF RGSRPYESGP LEEFLKREFG EHTKMTDVKK PKVMLTGTLS DRQPAELHLF
RNYDAPEVIR EPRFNQNINL KPPTQPADQL VWRAARSSGA APTYFRPNGR FLDGGLLANN
PTLDAMTEIH EYNQDMIRKG QGNKVKKLSI VVSLGTGRSP QVPVTCVDVF RPSNPWELAK
TVFGAKELGK MVVDCCTDPD GRAVDRARAW SEMVGIQYFR LNPQLGSDIM LDEVNDAVLV
NALWETEVYI YEHREEFQKL VQMLLSP
