ID   PLPL8_RABIT             Reviewed;         786 AA.
AC   Q5XTS1;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   08-NOV-2023, entry version 74.
DE   RecName: Full=Calcium-independent phospholipase A2-gamma {ECO:0000305};
DE            EC=3.1.1.- {ECO:0000250|UniProtKB:Q9NP80};
DE            EC=3.1.1.5 {ECO:0000250|UniProtKB:Q9NP80};
DE   AltName: Full=Group VIB calcium-independent phospholipase A2 {ECO:0000303|PubMed:15629460};
DE   AltName: Full=Intracellular membrane-associated calcium-independent phospholipase A2 gamma {ECO:0000303|PubMed:15629460};
DE            Short=iPLA2-gamma {ECO:0000303|PubMed:15629460};
DE   AltName: Full=Patatin-like phospholipase domain-containing protein 8;
GN   Name=PNPLA8 {ECO:0000250|UniProtKB:Q9NP80};
OS   Oryctolagus cuniculus (Rabbit).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX   NCBI_TaxID=9986;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TOPOLOGY, AND TISSUE
RP   SPECIFICITY.
RC   TISSUE=Heart;
RX   PubMed=15629460; DOI=10.1016/j.bbrc.2004.12.016;
RA   Kinsey G.R., Cummings B.S., Beckett C.S., Saavedra G., Zhang W.,
RA   McHowat J., Schnellmann R.G.;
RT   "Identification and distribution of endoplasmic reticulum iPLA2.";
RL   Biochem. Biophys. Res. Commun. 327:287-293(2005).
CC   -!- FUNCTION: Calcium-independent and membrane-bound phospholipase, that
CC       catalyzes the esterolytic cleavage of fatty acids from
CC       glycerophospholipids to yield free fatty acids and lysophospholipids,
CC       hence regulating membrane physical properties and the release of lipid
CC       second messengers and growth factors. Hydrolyzes
CC       phosphatidylethanolamine, phosphatidylcholine and probably
CC       phosphatidylinositol with a possible preference for the former. Has
CC       also a broad substrate specificity in terms of fatty acid moieties,
CC       hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal
CC       rates from either the sn-1 or sn-2 position in diacyl
CC       phosphatidylcholine. However, has a weak activity toward
CC       polyunsaturated fatty acids at the sn-2 position, and thereby favors
CC       the production of 2-arachidonoyl lysophosphatidylcholine, a key branch
CC       point metabolite in eicosanoid signaling. On the other hand, can
CC       produce arachidonic acid from the sn-1 position of diacyl phospholipid
CC       and from the sn-2 position of arachidonate-containing plasmalogen
CC       substrates. Therefore, plays an important role in the mobilization of
CC       arachidonic acid in response to cellular stimuli and the generation of
CC       lipid second messengers. Can also hydrolyze lysophosphatidylcholine. In
CC       the mitochondrial compartment, catalyzes the hydrolysis and release of
CC       oxidized aliphatic chains from cardiolipin and integrates mitochondrial
CC       bioenergetics and signaling. It is essential for maintaining efficient
CC       bioenergetic mitochondrial function through tailoring mitochondrial
CC       membrane lipid metabolism and composition.
CC       {ECO:0000250|UniProtKB:Q8K1N1, ECO:0000250|UniProtKB:Q9NP80}.
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;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-
CC         glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:18689,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868,
CC         ChEBI:CHEBI:57643, ChEBI:CHEBI:57875;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18690;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + H2O = a 1-
CC         acyl-sn-glycero-3-phosphoethanolamine + a fatty acid + H(+);
CC         Xref=Rhea:RHEA:44604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:64381, ChEBI:CHEBI:64612;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44605;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-alkenyl)-2-acyl-sn-glycero-3-phosphocholine + H2O = 1-
CC         O-(1Z-alkenyl)-sn-glycero-3-phosphocholine + a fatty acid + H(+);
CC         Xref=Rhea:RHEA:44068, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:28868, ChEBI:CHEBI:77286, ChEBI:CHEBI:77287;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44069;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15178;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-phosphocholine
CC         + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:40643, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30245, ChEBI:CHEBI:58168,
CC         ChEBI:CHEBI:60000; Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40644;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-acyl-
CC         sn-glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:40651,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:58168, ChEBI:CHEBI:75063;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40652;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40428;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = (9Z)-octadecenoate + 1-octadecanoyl-sn-glycero-3-
CC         phosphocholine + H(+); Xref=Rhea:RHEA:40819, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:73858,
CC         ChEBI:CHEBI:75034; Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40820;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38780;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40812;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(9Z,12Z)-octadecadienoyl-sn-glycero-3-
CC         phosphoethanolamine + H2O = (9Z,12Z)-octadecadienoate + a 1-acyl-sn-
CC         glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40639,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30245,
CC         ChEBI:CHEBI:64381, ChEBI:CHEBI:75069;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40640;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-acyl-2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-
CC         phosphoethanolamine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate + a 1-
CC         acyl-sn-glycero-3-phosphoethanolamine + H(+); Xref=Rhea:RHEA:40647,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32395,
CC         ChEBI:CHEBI:64381, ChEBI:CHEBI:75067;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40648;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40432;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC         3-phosphocholine + H2O = 2-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC         glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:40571, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:73003, ChEBI:CHEBI:76079;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40572;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine
CC         + H2O = 2-(9Z-octadecenoyl)-sn-glycero-3-phosphocholine + H(+) +
CC         octadecanoate; Xref=Rhea:RHEA:40823, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:25629, ChEBI:CHEBI:75034,
CC         ChEBI:CHEBI:76071; Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40824;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC         glycero-3-phosphocholine + H2O = 2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC         docosahexaenoyl)-sn-glycero-3-phosphocholine + H(+) + hexadecanoate;
CC         Xref=Rhea:RHEA:41063, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:74963, ChEBI:CHEBI:76085;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41064;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z)-hexadecenyl-2 (5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-
CC         glycero-3-phosphocholine + H2O = (5Z,8Z,11Z,14Z)-eicosatetraenoate +
CC         1-(1Z-hexadecenyl)-sn-glycero-3-phosphocholine + H(+);
CC         Xref=Rhea:RHEA:40579, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:32395, ChEBI:CHEBI:73850, ChEBI:CHEBI:77292;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40580;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1-O-(1Z-hexadecenyl)-2-(9Z-octadecenoyl)-sn-glycero-3-
CC         phosphocholine + H2O = (9Z)-octadecenoate + 1-(1Z-hexadecenyl)-sn-
CC         glycero-3-phosphocholine + H(+); Xref=Rhea:RHEA:67156,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC         ChEBI:CHEBI:73850, ChEBI:CHEBI:86232;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67157;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:40436;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
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:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:52813;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1'-[1-acyl-2-(9-hydroxy-(10E,12Z)-octadecadienoyl)-sn-glycero-
CC         3-phospho]-3'-[1,2-diacyl-sn-glycero-3-phospho]-glycerol + H2O = 1'-
CC         [1,2-diacyl-sn-glycero-3-phospho],3'-[1-acyl-sn-glycero-3-phospho]-
CC         glycerol + 9-hydroxy-(10E,12Z)-octadecadienoate + H(+);
CC         Xref=Rhea:RHEA:67272, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:64743, ChEBI:CHEBI:133820, ChEBI:CHEBI:167908;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67273;
CC         Evidence={ECO:0000250|UniProtKB:Q9NP80};
CC   -!- ACTIVITY REGULATION: Calcium-independent phospholipase.
CC       {ECO:0000250|UniProtKB:Q9NP80}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000250|UniProtKB:Q9NP80}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000269|PubMed:15629460}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:15629460}. Mitochondrion membrane
CC       {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:15629460}. Peroxisome membrane
CC       {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein
CC       {ECO:0000305|PubMed:15629460}.
CC   -!- TISSUE SPECIFICITY: Expressed in kidney, heart and brain.
CC       {ECO:0000269|PubMed:15629460}.
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DR   EMBL; AY738591; AAU85256.1; -; mRNA.
DR   RefSeq; NP_001164743.1; NM_001171272.1.
DR   AlphaFoldDB; Q5XTS1; -.
DR   SMR; Q5XTS1; -.
DR   STRING; 9986.ENSOCUP00000019643; -.
DR   GlyCosmos; Q5XTS1; 1 site, No reported glycans.
DR   PaxDb; 9986-ENSOCUP00000019643; -.
DR   GeneID; 100328577; -.
DR   KEGG; ocu:100328577; -.
DR   CTD; 50640; -.
DR   eggNOG; KOG4231; Eukaryota.
DR   InParanoid; Q5XTS1; -.
DR   OrthoDB; 5477952at2759; -.
DR   Proteomes; UP000001811; Unplaced.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; ISS:UniProtKB.
DR   GO; GO:0031966; C:mitochondrial membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR   GO; GO:0005778; C:peroxisomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
DR   GO; GO:0047499; F:calcium-independent phospholipase A2 activity; ISS:UniProtKB.
DR   GO; GO:0004622; F:lysophospholipase activity; IEA:UniProtKB-EC.
DR   GO; GO:0102545; F:phosphatidyl phospholipase B activity; IEA:UniProtKB-EC.
DR   GO; GO:0008970; F:phospholipase A1 activity; IEA:RHEA.
DR   GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR   GO; GO:0032048; P:cardiolipin metabolic process; ISS:UniProtKB.
DR   GO; GO:0016042; P:lipid catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR   GO; GO:0070328; P:triglyceride homeostasis; ISS:UniProtKB.
DR   CDD; cd07211; Pat_PNPLA8; 1.
DR   Gene3D; 3.40.1090.10; Cytosolic phospholipase A2 catalytic domain; 1.
DR   InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR   InterPro; IPR045217; PNPLA8-like.
DR   InterPro; IPR002641; PNPLA_dom.
DR   PANTHER; PTHR24185; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   PANTHER; PTHR24185:SF1; CALCIUM-INDEPENDENT PHOSPHOLIPASE A2-GAMMA; 1.
DR   Pfam; PF01734; Patatin; 1.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   PROSITE; PS51635; PNPLA; 1.
PE   1: Evidence at protein level;
KW   Endoplasmic reticulum; Glycoprotein; Hydrolase; Lipid degradation;
KW   Lipid metabolism; Membrane; Mitochondrion; Peroxisome; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..786
FT                   /note="Calcium-independent phospholipase A2-gamma"
FT                   /id="PRO_0000303216"
FT   TRANSMEM        483..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          449..644
FT                   /note="PNPLA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   REGION          158..180
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          225..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          321..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           453..458
FT                   /note="GXGXXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           485..489
FT                   /note="GXSXG"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOTIF           631..633
FT                   /note="DGA/G"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   COMPBIAS        225..246
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..285
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        487
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   ACT_SITE        631
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT   MOD_RES         740
FT                   /note="N6-succinyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K1N1"
FT   CARBOHYD        4
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   786 AA;  88177 MW;  AB130C143E718367 CRC64;
     MSINLTIDIC IYLLSNARNL CGKHRSKQLH LVCSPNHCWK IRHVSLQRGL HPHKVRCKWT
     KSETHSCSKH YYSPSNHGLH IGILKLSTSA PKGLTKVSIR MSRIKSTLNS VSKAVFGSQN
     EMISRLAQFK PSSRILRKVS DSGWLKQESI KQAIRSLKKY SDKSTEKSPV PEGRNHIIDK
     EDDIGKQSLF HYTGNITTKF GESFYFLSNH INSYFKRAEK MSQDKENSHF QEKSELEGKK
     VEEGKSSSLD PGILTSQADK PDPKSSAGTM DKATSPSGTP ESLPISTKQS IANFLSRPTE
     GVQALVGGYI GGLVPKLKYD SKSQAEEQEE PAKSEPAGSK DKTVEEKKHL SLQREKIIAR
     VSIDNRTRAL VQALRRTADP KLCITRVEEL TFHLLEFPEG KGVAVKERLI PCLLRLRQMK
     DETLQAAVRE ILALIGYVDP VKGRGIRILT IDGGGTRGVV ALQTLRKLVE LTQKPVHQLF
     DYICGVSTGA ILAFMLGLFH LPLDECEELY RKLGSDIFSQ NVIVGTVKMS WSHAFYDSQT
     WEKILKERMG SALMIETARN PMCPKVAAVS TIVNRGSTPK AFVFRNYGHF PGSQSHYLGG
     CQYKMWQAIR ASSAAPGYFA EYALGNDLHQ DGGLLLNNPS ALAMHECKCL WPDAPLECIV
     SLGTGRYESD VRNNTTYTSL KTKLSNVINS ATDTEEVHIM LDGLLPPDTY FRFNPVMCEN
     IPLDESRNEK LDQLQLEGSK YIERNEHKMK KVAKILSQEK TTLQKINDWI KLKTDMYEGL
     PFFSKL
//