PLPL2_RAT
ID PLPL2_RAT Reviewed; 478 AA.
AC P0C548;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 2 {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000250|UniProtKB:Q96AD5};
DE AltName: Full=Adipose triglyceride lipase;
DE AltName: Full=Calcium-independent phospholipase A2-zeta;
DE Short=iPLA2-zeta;
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q96AD5};
GN Name=Pnpla2 {ECO:0000312|RGD:1309044}; Synonyms=Atgl;
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 INDUCTION.
RX PubMed=16906479; DOI=10.1007/s00125-006-0336-y;
RA Festuccia W.T., Laplante M., Berthiaume M., Gelinas Y., Deshaies Y.;
RT "PPARgamma agonism increases rat adipose tissue lipolysis, expression of
RT glyceride lipases, and the response of lipolysis to hormonal control.";
RL Diabetologia 49:2427-2436(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-398 AND SER-422, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [4]
RP INTERACTION WITH PLIN5.
RX PubMed=23408028; DOI=10.1152/ajpregu.00418.2012;
RA MacPherson R.E., Ramos S.V., Vandenboom R., Roy B.D., Peters S.J.;
RT "Skeletal muscle PLIN proteins, ATGL and CGI-58, interactions at rest and
RT following stimulated contraction.";
RL Am. J. Physiol. 304:R644-R650(2013).
RN [5]
RP INTERACTION WITH PLIN5.
RX PubMed=24303154; DOI=10.1002/phy2.84;
RA Macpherson R.E., Vandenboom R., Roy B.D., Peters S.J.;
RT "Skeletal muscle PLIN3 and PLIN5 are serine phosphorylated at rest and
RT following lipolysis during adrenergic or contractile stimulation.";
RL Physiol. Rep. 1:E00084-E00084(2013).
CC -!- FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in
CC adipocyte and non-adipocyte lipid droplets (By similarity). Exhibits a
CC strong preference for the hydrolysis of long-chain fatty acid esters at
CC the sn-2 position of the glycerol backbone and acts coordinately with
CC LIPE/HLS and DGAT2 within the lipolytic cascade (By similarity). Also
CC possesses acylglycerol transacylase and phospholipase A2 activities (By
CC similarity). Transfers fatty acid from triglyceride to retinol,
CC hydrolyzes retinylesters, and generates 1,3-diacylglycerol from
CC triglycerides (By similarity). Regulates adiposome size and may be
CC involved in the degradation of adiposomes (By similarity). May play an
CC important role in energy homeostasis (By similarity). May play a role
CC in the response of the organism to starvation, enhancing hydrolysis of
CC triglycerides and providing free fatty acids to other tissues to be
CC oxidized in situations of energy depletion (By similarity).
CC {ECO:0000250|UniProtKB:Q8BJ56, ECO:0000250|UniProtKB:Q96AD5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid +
CC H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol + H2O = a 1,2-diacylglycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:44864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:49172,
CC ChEBI:CHEBI:64615; Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44865;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol + H2O = 1,3-diacyl-sn-glycerol + a fatty
CC acid + H(+); Xref=Rhea:RHEA:43732, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64615,
CC ChEBI:CHEBI:77272; Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43733;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol + H2O = a 2,3-diacyl-sn-glycerol + a
CC fatty acid + H(+); Xref=Rhea:RHEA:38499, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:64615,
CC ChEBI:CHEBI:75524; Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38500;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,3-diacylglycerol + a 1-acylglycerol = a triacylglycerol +
CC glycerol; Xref=Rhea:RHEA:44440, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855,
CC ChEBI:CHEBI:35759, ChEBI:CHEBI:47777;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44441;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacylglycerol + a 1-acylglycerol = a triacylglycerol +
CC glycerol; Xref=Rhea:RHEA:44436, ChEBI:CHEBI:17754, ChEBI:CHEBI:17855,
CC ChEBI:CHEBI:35759, ChEBI:CHEBI:49172;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44437;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 a 1-acylglycerol = a 1,2-diacylglycerol + glycerol;
CC Xref=Rhea:RHEA:44432, ChEBI:CHEBI:17754, ChEBI:CHEBI:35759,
CC ChEBI:CHEBI:49172; Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44433;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a triacyl-sn-glycerol + all-trans-retinol = a diacylglycerol +
CC an all-trans-retinyl ester; Xref=Rhea:RHEA:44676, ChEBI:CHEBI:17336,
CC ChEBI:CHEBI:18035, ChEBI:CHEBI:63410, ChEBI:CHEBI:64615;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44677;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(9Z)-octadecenoate + 1,2-di-(9Z-octadecenoyl)-glycerol + H(+)
CC = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O; Xref=Rhea:RHEA:38379,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:53753;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 1,3-di-(9Z-octadecenoyl)-glycerol + H(+);
CC Xref=Rhea:RHEA:38387, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75735;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-
CC glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol;
CC Xref=Rhea:RHEA:38331, ChEBI:CHEBI:17754, ChEBI:CHEBI:53753,
CC ChEBI:CHEBI:75342, ChEBI:CHEBI:75735;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z-octadecenoyl)-glycerol + 1-(9Z-octadecenoyl)-
CC glycerol = 1,2,3-tri-(9Z-octadecenoyl)-glycerol + glycerol;
CC Xref=Rhea:RHEA:38327, ChEBI:CHEBI:17754, ChEBI:CHEBI:52323,
CC ChEBI:CHEBI:53753, ChEBI:CHEBI:75342;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1-(9Z-octadecenoyl)-glycerol = 1,2-di-(9Z-octadecenoyl)-
CC glycerol + glycerol; Xref=Rhea:RHEA:38323, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:52323, ChEBI:CHEBI:75342;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + all-trans-retinol =
CC all-trans-retinyl 9Z-octadecenoate + di-(9Z)-octadecenoylglycerol;
CC Xref=Rhea:RHEA:39987, ChEBI:CHEBI:17336, ChEBI:CHEBI:53753,
CC ChEBI:CHEBI:70760, ChEBI:CHEBI:75945;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39988;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z)-hexadecenoylglycerol + H2O = (9Z)-hexadecenoate
CC + 1,3-di-(9Z)-hexadecenoylglycerol + H(+); Xref=Rhea:RHEA:38395,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:75841, ChEBI:CHEBI:75849;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38396;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + H2O = (9Z,12Z)-
CC octadecadienoate + 1,3-di-(9Z,12Z)-octadecadienoylglycerol + H(+);
CC Xref=Rhea:RHEA:38403, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75844, ChEBI:CHEBI:75850;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38404;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z,12Z,15Z)-octadecatrienoylglycerol + H2O =
CC (9Z,12Z,15Z)-octadecatrienoate + 1,3-di-(9Z,12Z,15Z)-
CC octadecatrienoylglycerol + H(+); Xref=Rhea:RHEA:38411,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387,
CC ChEBI:CHEBI:75845, ChEBI:CHEBI:75852;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38412;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z)-octadecenoyl-2-hexadecanoylglycerol + H2O = 1,3-
CC di-(9Z-octadecenoyl)-glycerol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:38419, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75735, ChEBI:CHEBI:75846;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38420;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + H2O =
CC (9Z)-octadecenoate + 1-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol +
CC H(+); Xref=Rhea:RHEA:38423, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75583, ChEBI:CHEBI:75867;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38424;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O =
CC (9Z)-octadecenoate + 1-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol +
CC H(+); Xref=Rhea:RHEA:38647, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75847, ChEBI:CHEBI:75868;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38648;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z-octadecenoyl)-glycerol + H2O = (9Z)-
CC octadecenoate + 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+);
CC Xref=Rhea:RHEA:38391, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:53753, ChEBI:CHEBI:75824;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z)-hexadecenoylglycerol + H2O = (9Z)-hexadecenoate
CC + 2,3-di-(9Z)-hexadecenoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38399,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32372,
CC ChEBI:CHEBI:75841, ChEBI:CHEBI:75853;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38400;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z,12Z)-octadecadienoylglycerol + H2O = (9Z,12Z)-
CC octadecadienoate + 2,3-di-(9Z,12Z)-octadecadienoyl-sn-glycerol +
CC H(+); Xref=Rhea:RHEA:38407, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30245, ChEBI:CHEBI:75844, ChEBI:CHEBI:75854;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38408;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2,3-tri-(9Z,12Z,15Z)-octadecatrienoylglycerol + H2O =
CC (9Z,12Z,15Z)-octadecatrienoate + 2,3-di-(9Z,12Z,15Z)-
CC octadecatrienoyl-sn-glycerol + H(+); Xref=Rhea:RHEA:38415,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:32387,
CC ChEBI:CHEBI:75845, ChEBI:CHEBI:75855;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38416;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,3-di-(9Z)-octadecenoyl-2-hexadecanoylglycerol + H2O = (9Z)-
CC octadecenoate + 2-hexadecanoyl-3-(9Z)-octadecenoyl-sn-glycerol +
CC H(+); Xref=Rhea:RHEA:38431, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75846, ChEBI:CHEBI:75870;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38432;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-hexadecanoyl-2,3-di-(9Z)-octadecenoyl-sn-glycerol + H2O =
CC 2,3-di-(9Z)-octadecenoyl-sn-glycerol + H(+) + hexadecanoate;
CC Xref=Rhea:RHEA:38427, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:75824, ChEBI:CHEBI:75847;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38428;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,2-di-(9Z)-octadecenoyl-3-hexadecanoyl-sn-glycerol + H2O =
CC (9Z)-octadecenoate + 2-(9Z-octadecenoyl)-3-hexadecanoyl-sn-glycerol +
CC H(+); Xref=Rhea:RHEA:38643, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30823, ChEBI:CHEBI:75546, ChEBI:CHEBI:75583;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38644;
CC Evidence={ECO:0000250|UniProtKB:Q8BJ56};
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:0000250|UniProtKB:Q96AD5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000250|UniProtKB:Q96AD5};
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC -!- SUBUNIT: Interacts with ABHD5; this association stimulates PNPLA2
CC triglyceride hydrolase activity (By similarity). Interacts with
CC SERPINF1; this interaction stimulates the phospholipase A2 activity of
CC PNPLA2 (By similarity). Despite a colocalization in lipid droplets, it
CC probably does not interact with PLIN (By similarity). Interacts with
CC PLIN5; prevents interaction with ABHD5 (PubMed:23408028,
CC PubMed:24303154). Interacts with FAF2 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BJ56, ECO:0000250|UniProtKB:Q96AD5,
CC ECO:0000269|PubMed:23408028, ECO:0000269|PubMed:24303154}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000250|UniProtKB:Q96AD5}.
CC Cell membrane {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane
CC protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BJ56}.
CC -!- INDUCTION: Increased by rosiglitazone in subcutaneous and visceral
CC white adipose tissue. {ECO:0000269|PubMed:16906479}.
CC -!- PTM: Phosphorylation at Ser-398 by PKA is increased during fasting and
CC moderate intensity exercise, and moderately increases lipolytic
CC activity. {ECO:0000250|UniProtKB:Q8BJ56}.
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DR EMBL; AC109542; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001101979.2; NM_001108509.2.
DR RefSeq; XP_003749062.1; XM_003749014.3.
DR RefSeq; XP_017459687.1; XM_017604198.1.
DR AlphaFoldDB; P0C548; -.
DR BioGRID; 262869; 1.
DR STRING; 10116.ENSRNOP00000025319; -.
DR GlyGen; P0C548; 1 site.
DR iPTMnet; P0C548; -.
DR PhosphoSitePlus; P0C548; -.
DR PaxDb; P0C548; -.
DR PRIDE; P0C548; -.
DR Ensembl; ENSRNOT00000025319; ENSRNOP00000025319; ENSRNOG00000069673.
DR GeneID; 361676; -.
DR KEGG; rno:361676; -.
DR CTD; 57104; -.
DR RGD; 1309044; Pnpla2.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000160155; -.
DR HOGENOM; CLU_018371_0_1_1; -.
DR InParanoid; P0C548; -.
DR OMA; AFIPVYC; -.
DR OrthoDB; 1204225at2759; -.
DR PhylomeDB; P0C548; -.
DR TreeFam; TF314272; -.
DR Reactome; R-RNO-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-RNO-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-RNO-8957275; Post-translational protein phosphorylation.
DR UniPathway; UPA00256; -.
DR PRO; PR:P0C548; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000018736; Expressed in heart and 18 other tissues.
DR Genevisible; P0C548; RN.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051265; F:diolein transacylation activity; ISS:UniProtKB.
DR GO; GO:0051264; F:mono-olein transacylation activity; ISS:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; ISS:UniProtKB.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; ISS:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; ISS:UniProtKB.
DR GO; GO:0044242; P:cellular lipid catabolic process; ISO:RGD.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; IEA:Ensembl.
DR GO; GO:0034389; P:lipid droplet organization; ISO:RGD.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; ISO:RGD.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; ISS:UniProtKB.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; ISS:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; ISS:UniProtKB.
DR CDD; cd07220; Pat_PNPLA2; 1.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR033562; PLPL.
DR InterPro; IPR033903; PNPLA2.
DR InterPro; IPR002641; PNPLA_dom.
DR PANTHER; PTHR12406; PTHR12406; 1.
DR Pfam; PF01734; Patatin; 1.
DR SUPFAM; SSF52151; SSF52151; 1.
DR PROSITE; PS51635; PNPLA; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Glycoprotein; Hydrolase; Lipid degradation;
KW Lipid droplet; Lipid metabolism; Membrane; Phosphoprotein;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..478
FT /note="Patatin-like phospholipase domain-containing protein
FT 2"
FT /id="PRO_0000292529"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..42
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..323
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT TRANSMEM 324..344
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 345..478
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT DOMAIN 10..179
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 456..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 14..19
FT /note="GXGXXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 45..49
FT /note="GXSXG"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOTIF 166..168
FT /note="DGA/G"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 47
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT MOD_RES 366
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ56"
FT MOD_RES 388
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ56"
FT MOD_RES 398
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 460
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ56"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 478 AA; 52567 MW; E6B8294E47631410 CRC64;
MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGA
CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK TLPADCHTRA SGRLGISLTR
VSDGENVIIS HFSSKDELIQ ANVCSTFIPV YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRITNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ
GYRDGLRFLR RNGLLNQPNP LLALPPVVPQ EEDAEEAAVT EERTGGEDRI LEHLPARLNE
ALLEACVEPK DLMTTLSNML PVRLATAMMV PYTLPLESAV SFTIRLLEWL PDVPEDIRWM
KEQTGSICQY LVMRAKRKLG DHLPSRLSEQ VELRRAQSLP SVPLSCATYS EALPNWVRNN
LSLGDALAKW EECQRQLLLG LFCTNVAFPP DALRMRAPAS PTATDPATPQ DPSGLPPC
