PLPL8_RAT
ID PLPL8_RAT Reviewed; 776 AA.
AC D3ZRC4;
DT 17-JUN-2020, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=Intracellular membrane-associated calcium-independent phospholipase A2 gamma;
DE Short=iPLA2-gamma;
DE AltName: Full=Patatin-like phospholipase domain-containing protein 8;
GN Name=Pnpla8 {ECO:0000312|RGD:1311444};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Li P.W., Adams M.D., Amanatides P.G., Baden-Tillson H.,
RA Barnstead M., Chin S.H., Dew I., Evans C.A., Ferriera S., Flanigan M.,
RA Fosler C., Glodek A., Gu Z., Holt R.A., Jennings D., Kraft C.L., Lu F.,
RA Nguyen T., Nusskern D.R., Pfannkoch C.M., Sitter C., Sutton G.G.,
RA Venter J.C., Wang Z., Woodage T., Zheng X.H., Zhong F.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
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).
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:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NP80}. Microsome membrane
CC {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NP80}. Mitochondrion membrane
CC {ECO:0000250|UniProtKB:Q9NP80}; Single-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9NP80}. Peroxisome membrane
CC {ECO:0000305|PubMed:15908428}; Single-pass membrane protein
CC {ECO:0000305}.
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DR EMBL; AC133400; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473947; EDM03350.1; -; Genomic_DNA.
DR RefSeq; XP_003750198.1; XM_003750150.4.
DR RefSeq; XP_003754218.1; XM_003754170.4.
DR AlphaFoldDB; D3ZRC4; -.
DR SMR; D3ZRC4; -.
DR IntAct; D3ZRC4; 1.
DR STRING; 10116.ENSRNOP00000049214; -.
DR PhosphoSitePlus; D3ZRC4; -.
DR jPOST; D3ZRC4; -.
DR PaxDb; D3ZRC4; -.
DR PeptideAtlas; D3ZRC4; -.
DR PRIDE; D3ZRC4; -.
DR Ensembl; ENSRNOT00000047296; ENSRNOP00000049214; ENSRNOG00000039091.
DR GeneID; 314075; -.
DR CTD; 50640; -.
DR RGD; 1311444; Pnpla8.
DR eggNOG; KOG4231; Eukaryota.
DR GeneTree; ENSGT00940000154738; -.
DR HOGENOM; CLU_000288_144_7_1; -.
DR InParanoid; D3ZRC4; -.
DR OMA; YKLWQAI; -.
DR OrthoDB; 1209603at2759; -.
DR PhylomeDB; D3ZRC4; -.
DR TreeFam; TF319230; -.
DR Reactome; R-RNO-1482788; Acyl chain remodelling of PC.
DR Reactome; R-RNO-1482839; Acyl chain remodelling of PE.
DR PRO; PR:D3ZRC4; -.
DR Proteomes; UP000002494; Chromosome 6.
DR Proteomes; UP000234681; Chromosome 6.
DR Bgee; ENSRNOG00000039091; Expressed in quadriceps femoris and 19 other tissues.
DR ExpressionAtlas; D3ZRC4; baseline and differential.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; ISO:RGD.
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:0004620; F:phospholipase activity; IBA:GO_Central.
DR GO; GO:0019369; P:arachidonic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0050482; P:arachidonic acid secretion; ISO:RGD.
DR GO; GO:0032048; P:cardiolipin metabolic process; ISS:UniProtKB.
DR GO; GO:0008219; P:cell death; ISO:RGD.
DR GO; GO:0006631; P:fatty acid metabolic process; ISO:RGD.
DR GO; GO:0043651; P:linoleic acid metabolic process; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; ISS:UniProtKB.
DR GO; GO:0034638; P:phosphatidylcholine catabolic process; ISO:RGD.
DR GO; GO:0046338; P:phosphatidylethanolamine catabolic process; ISO:RGD.
DR GO; GO:0001516; P:prostaglandin biosynthetic process; ISO:RGD.
DR GO; GO:1900407; P:regulation of cellular response to oxidative stress; ISO:RGD.
DR GO; GO:0070328; P:triglyceride homeostasis; ISS:UniProtKB.
DR CDD; cd07211; Pat_PNPLA8; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR045217; PNPLA8-like.
DR InterPro; IPR002641; PNPLA_dom.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum; Hydrolase; Lipid degradation; Lipid metabolism;
KW Membrane; Microsome; Mitochondrion; Peroxisome; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..776
FT /note="Calcium-independent phospholipase A2-gamma"
FT /id="PRO_0000450242"
FT TRANSMEM 469..489
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 439..634
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 226..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 306..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 443..448
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 475..479
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 621..623
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT COMPBIAS 259..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 310..331
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 477
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 621
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 730
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8K1N1"
SQ SEQUENCE 776 AA; 87961 MW; 96808D538E5B8B27 CRC64;
MSINLTLDIY IYFLNNARSF CGKQRSKQLN FLCSKQYWRM NHVNVHREFH TSKKSCKWNR
SEAHCSKHWH SSSNHGVHIG IVKLSTSAPK GLTKVSIHMS RIKSTLNSVS KAIFGSQNEM
VSRLAQFKPS SRIFRKVSDR GWLKHKNVKQ AIESLKNYSD KSAEKNSFAE QKSYFADKEE
GSDKHSLYHY AYRITTRFGE SFYFLANHIN SYFKNKEKMS QIKEDRQLQD KPCLEESKSI
SPSPDILTDR PDSGPPLNVE DKLSSSTQLP EALPVSTKQS IANFLSRPTE GVQALVGGYI
GGLVPKLKSD PKSQPEEEEE PSKTDEPICK DKKAEEKKRV LLQREKIIAR VSIDNRTRAL
VQALRRTTDP KLCITRVEEL TFHLLEFPEG KGVAVKEKII PYLLRLRQIK DETLQAAVRE
ILALIGYVDP VKGRGIRILA IDGGGTRGVV ALQTLRKLVE LTQKPIHQLF DYICGVSTGA
ILAFMLGLFH MPLDECEELY RKLGSDVFTQ NVIVGTVKMS WSHAFYDSHT WEKILKDKVG
SALMIETARD PLCPKVAAVS TIVNRGQTPK AFVFRNYGHF PGTNSHYLGG CQYKMWQAIR
ASSAAPGYFA EYALGNDLHQ DGGLLLNNPS ALALHECKCI WPDTPLECIV SLGTGRYESD
VRNTTTYTSL KTKLSNVISS ATDTEEVHIM LDGLLPADTY FRFNPVICEN IPLDESRNEK
LDQLQLEGMK YLERNDEKMK KLAKILSREK TTLQKISDWI KLKSDMYEGL PFFSKL
