PLPL2_MOUSE
ID PLPL2_MOUSE Reviewed; 486 AA.
AC Q8BJ56; O89080; Q05BJ0; Q3UD97; Q643S0; Q6P234; Q9D1Q9; Q9DCF6;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 2 {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698, ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:23066022};
DE AltName: Full=Adipose triglyceride lipase;
DE AltName: Full=Calcium-independent phospholipase A2-zeta {ECO:0000250|UniProtKB:Q96AD5};
DE Short=iPLA2-zeta {ECO:0000250|UniProtKB:Q96AD5};
DE EC=3.1.1.4 {ECO:0000250|UniProtKB:Q96AD5};
DE AltName: Full=Desnutrin;
GN Name=Pnpla2 {ECO:0000312|MGI:MGI:1914103}; Synonyms=Atgl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, INDUCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6J; TISSUE=White adipose tissue;
RX PubMed=15337759; DOI=10.1074/jbc.m403855200;
RA Villena J.A., Roy S., Sarkadi-Nagy E., Kim K.-H., Sul H.S.;
RT "Desnutrin, an adipocyte gene encoding a novel patatin domain-containing
RT protein, is induced by fasting and glucocorticoids: ectopic expression of
RT desnutrin increases triglyceride hydrolysis.";
RL J. Biol. Chem. 279:47066-47075(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ACTIVITY REGULATION,
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP PHOSPHORYLATION, AND CATALYTIC ACTIVITY.
RC STRAIN=C57BL/6J;
RX PubMed=15550674; DOI=10.1126/science.1100747;
RA Zimmermann R., Strauss J.G., Haemmerle G., Schoiswohl G.,
RA Birner-Gruenberger R., Riederer M., Lass A., Neuberger G., Eisenhaber F.,
RA Hermetter A., Zechner R.;
RT "Fat mobilization in adipose tissue is promoted by adipose triglyceride
RT lipase.";
RL Science 306:1383-1386(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=C57BL/6J;
RX PubMed=16705060; DOI=10.1152/ajpendo.00317.2005;
RA Kim J.Y., Tillison K., Lee J.-H., Rearick D.A., Smas C.M.;
RT "The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by
RT insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for
RT transactivation by PPARgamma.";
RL Am. J. Physiol. 291:E115-E127(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, Kidney, and Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=FVB/N; TISSUE=Trophoblast stem cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 296-473.
RC STRAIN=BALB/cJ; TISSUE=Spleen;
RX PubMed=9798653; DOI=10.1016/s0161-5890(98)00031-5;
RA Chu C.C., Paul W.E.;
RT "Expressed genes in interleukin-4 treated B cells identified by cDNA
RT representational difference analysis.";
RL Mol. Immunol. 35:487-502(1998).
RN [7]
RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RX PubMed=16150821; DOI=10.1194/jlr.m500290-jlr200;
RA Lake A.C., Sun Y., Li J.-L., Kim J.E., Johnson J.W., Li D., Revett T.,
RA Shih H.H., Liu W., Paulsen J.E., Gimeno R.E.;
RT "Expression, regulation, and triglyceride hydrolase activity of Adiponutrin
RT family members.";
RL J. Lipid Res. 46:2477-2487(2005).
RN [8]
RP INDUCTION.
RX PubMed=16009485; DOI=10.1016/j.mce.2005.06.002;
RA Kralisch S., Klein J., Lossner U., Bluher M., Paschke R., Stumvoll M.,
RA Fasshauer M.;
RT "Isoproterenol, TNFalpha, and insulin downregulate adipose triglyceride
RT lipase in 3T3-L1 adipocytes.";
RL Mol. Cell. Endocrinol. 240:43-49(2005).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, INTERACTION WITH ABHD5, AND MUTAGENESIS OF
RP SER-47.
RX PubMed=16679289; DOI=10.1016/j.cmet.2006.03.005;
RA Lass A., Zimmermann R., Haemmerle G., Riederer M., Schoiswohl G.,
RA Schweiger M., Kienesberger P., Strauss J.G., Gorkiewicz G., Zechner R.;
RT "Adipose triglyceride lipase-mediated lipolysis of cellular fat stores is
RT activated by CGI-58 and defective in Chanarin-Dorfman Syndrome.";
RL Cell Metab. 3:309-319(2006).
RN [10]
RP INDUCTION.
RX PubMed=16380488; DOI=10.2337/diabetes.55.01.06.db05-0982;
RA Kershaw E.E., Hamm J.K., Verhagen L.A.W., Peroni O., Katic M., Flier J.S.;
RT "Adipose triglyceride lipase: function, regulation by insulin, and
RT comparison with adiponutrin.";
RL Diabetes 55:148-157(2006).
RN [11]
RP FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=17074755; DOI=10.1074/jbc.m608048200;
RA Schweiger M., Schreiber R., Haemmerle G., Lass A., Fledelius C.,
RA Jacobsen P., Tornqvist H., Zechner R., Zimmermann R.;
RT "Adipose triglyceride lipase and hormone-sensitive lipase are the major
RT enzymes in adipose tissue triacylglycerol catabolism.";
RL J. Biol. Chem. 281:40236-40241(2006).
RN [12]
RP FUNCTION, DISRUPTION PHENOTYPE, AND CATALYTIC ACTIVITY.
RX PubMed=16675698; DOI=10.1126/science.1123965;
RA Haemmerle G., Lass A., Zimmermann R., Gorkiewicz G., Meyer C., Rozman J.,
RA Heldmaier G., Maier R., Theussl C., Eder S., Kratky D., Wagner E.F.,
RA Klingenspor M., Hoefler G., Zechner R.;
RT "Defective lipolysis and altered energy metabolism in mice lacking adipose
RT triglyceride lipase.";
RL Science 312:734-737(2006).
RN [13]
RP ACTIVITY REGULATION, FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=17114792; DOI=10.1074/jbc.m605770200;
RA Miyoshi H., Perfield J.W. II, Souza S.C., Shen W.-J., Zhang H.-H.,
RA Stancheva Z.S., Kraemer F.B., Obin M.S., Greenberg A.S.;
RT "Control of adipose triglyceride lipase action by serine 517 of perilipin A
RT globally regulates protein kinase A-stimulated lipolysis in adipocytes.";
RL J. Biol. Chem. 282:996-1002(2007).
RN [14]
RP INTERACTION WITH ABHD5, AND LACK OF INTERACTION WITH PLIN.
RX PubMed=17189257; DOI=10.1074/jbc.m610580200;
RA Granneman J.G., Moore H.-P.H., Granneman R.L., Greenberg A.S., Obin M.S.,
RA Zhu Z.;
RT "Analysis of lipolytic protein trafficking and interactions in
RT adipocytes.";
RL J. Biol. Chem. 282:5726-5735(2007).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-406 AND SER-430, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [16]
RP INTERACTION WITH PLIN5, AND EXCLUSION OF INTERACTION WITH ABHD5.
RX PubMed=21148142; DOI=10.1074/jbc.m110.180711;
RA Granneman J.G., Moore H.P., Mottillo E.P., Zhu Z., Zhou L.;
RT "Interactions of perilipin-5 (Plin5) with adipose triglyceride lipase.";
RL J. Biol. Chem. 286:5126-5135(2011).
RN [17]
RP INTERACTION WITH PLIN5.
RX PubMed=21393244; DOI=10.1074/jbc.m110.207779;
RA Wang H., Bell M., Sreenivasan U., Sreenevasan U., Hu H., Liu J., Dalen K.,
RA Londos C., Yamaguchi T., Rizzo M.A., Coleman R., Gong D., Brasaemle D.,
RA Sztalryd C.;
RT "Unique regulation of adipose triglyceride lipase (ATGL) by perilipin 5, a
RT lipid droplet-associated protein.";
RL J. Biol. Chem. 286:15707-15715(2011).
RN [18]
RP PHOSPHORYLATION AT SER-374; SER-396; SER-406; SER-430 AND SER-468, AND
RP MUTAGENESIS OF SER-396 AND SER-406.
RX PubMed=22733971; DOI=10.1210/en.2012-1127;
RA Pagnon J., Matzaris M., Stark R., Meex R.C., Macaulay S.L., Brown W.,
RA O'Brien P.E., Tiganis T., Watt M.J.;
RT "Identification and functional characterization of protein kinase A
RT phosphorylation sites in the major lipolytic protein, adipose triglyceride
RT lipase.";
RL Endocrinology 153:4278-4289(2012).
RN [19]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=23066022; DOI=10.1074/jbc.m112.400416;
RA Eichmann T.O., Kumari M., Haas J.T., Farese R.V. Jr., Zimmermann R.,
RA Lass A., Zechner R.;
RT "Studies on the substrate and stereo/regioselectivity of adipose
RT triglyceride lipase, hormone-sensitive lipase, and diacylglycerol-O-
RT acyltransferases.";
RL J. Biol. Chem. 287:41446-41457(2012).
CC -!- FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in
CC adipocyte and non-adipocyte lipid droplets (PubMed:15550674,
CC PubMed:23066022, PubMed:15337759, PubMed:16150821, PubMed:16679289,
CC PubMed:17074755, PubMed:16675698, PubMed:17114792). Exhibits a strong
CC preference for the hydrolysis of long-chain fatty acid esters at the
CC sn-2 position of the glycerol backbone and acts coordinately with
CC LIPE/HLS and DGAT2 within the lipolytic cascade (PubMed:23066022). 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 (PubMed:16675698). 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 (PubMed:15337759).
CC {ECO:0000250|UniProtKB:Q96AD5, ECO:0000269|PubMed:15337759,
CC ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821,
CC ECO:0000269|PubMed:16675698, ECO:0000269|PubMed:16679289,
CC ECO:0000269|PubMed:17074755, ECO:0000269|PubMed:17114792,
CC ECO:0000269|PubMed:23066022}.
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:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674,
CC ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16675698,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17074755,
CC ECO:0000269|PubMed:17114792, ECO:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:23066022};
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 = 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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38500;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43733;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38396;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38404;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38412;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38420;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38424;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38648;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38392;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38400;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38408;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38416;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38432;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38428;
CC Evidence={ECO:0000305|PubMed:23066022};
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:0000269|PubMed:23066022};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38644;
CC Evidence={ECO:0000305|PubMed:23066022};
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=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=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=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 -!- ACTIVITY REGULATION: Stimulated by PKA-dependent PLIN phosphorylation.
CC {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:17074755,
CC ECO:0000269|PubMed:17114792}.
CC -!- PATHWAY: Glycerolipid metabolism; triacylglycerol degradation.
CC -!- SUBUNIT: Interacts with ABHD5; this association stimulates PNPLA2
CC triglyceride hydrolase activity (PubMed:16679289, PubMed:17189257).
CC Interacts with SERPINF1; this interaction stimulates the phospholipase
CC A2 activity of PNPLA2 (By similarity). Despite a colocalization in
CC lipid droplets, it probably does not interact with PLIN
CC (PubMed:17189257). Interacts with PLIN5; prevents interaction with
CC ABHD5 (PubMed:21148142, PubMed:21393244). Interacts with FAF2 (By
CC similarity). {ECO:0000250|UniProtKB:Q96AD5,
CC ECO:0000269|PubMed:16679289, ECO:0000269|PubMed:17189257,
CC ECO:0000269|PubMed:21148142, ECO:0000269|PubMed:21393244}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:15550674,
CC ECO:0000269|PubMed:16705060}. Cell membrane
CC {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15337759}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8BJ56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BJ56-2; Sequence=VSP_026424;
CC Name=3;
CC IsoId=Q8BJ56-3; Sequence=VSP_026422, VSP_026423;
CC -!- TISSUE SPECIFICITY: Expressed at high levels in white and brown adipose
CC tissue, and to a lesser degree in testis and cardiac muscle. Barely
CC detected in liver, spleen, thymus, kidney, skeletal muscle, and brain.
CC Among the white adipose depots, gonadal fat showed the highest level of
CC expression compared with inguinal and renal white adipose tissues.
CC {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:15550674,
CC ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16705060}.
CC -!- DEVELOPMENTAL STAGE: Increased expression when preadipocytes are
CC induced to differentiate to adipocytes. Not detected in proliferating
CC or confluent preadipocytes. {ECO:0000269|PubMed:15337759,
CC ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821,
CC ECO:0000269|PubMed:16705060}.
CC -!- INDUCTION: Transiently induced during fasting. cAMP and glucagon may
CC not be involved in the induction during fasting. Induced by
CC dexamethasone. Down-regulated by insulin, isoprotenerol and TNF-alfa.
CC Expression is not affected by glucose and by growth hormone. Expression
CC is reduced in fasted leptin deficient mouse (ob/ob), an obese mouse
CC model. Expression is not affected in fed ob/ob mouse.
CC {ECO:0000269|PubMed:15337759, ECO:0000269|PubMed:16009485,
CC ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16380488,
CC ECO:0000269|PubMed:16705060}.
CC -!- PTM: Phosphorylation at Ser-406 by PKA is increased during fasting and
CC moderate intensity exercise, and moderately increases lipolytic
CC activity. {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:22733971}.
CC -!- DISRUPTION PHENOTYPE: Mice show increased adipose mass and
CC triacylglycerol deposition in multiple tissues. They accumulate large
CC amounts of lipid in the heart, causing cardiac dysfunction and
CC premature death. {ECO:0000269|PubMed:16675698}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB22643.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY731699; AAU33824.1; -; mRNA.
DR EMBL; AY894805; AAW81963.1; -; mRNA.
DR EMBL; AY510273; AAS48458.1; -; mRNA.
DR EMBL; AK002826; BAB22387.1; -; mRNA.
DR EMBL; AK003207; BAB22643.1; ALT_FRAME; mRNA.
DR EMBL; AK031609; BAC27476.1; -; mRNA.
DR EMBL; AK150184; BAE29364.1; -; mRNA.
DR EMBL; BC019188; AAH19188.1; -; mRNA.
DR EMBL; BC044781; AAH44781.1; -; mRNA.
DR EMBL; BC064747; AAH64747.1; -; mRNA.
DR EMBL; U89431; AAC36536.1; -; mRNA.
DR CCDS; CCDS22015.1; -. [Q8BJ56-2]
DR CCDS; CCDS52445.1; -. [Q8BJ56-1]
DR RefSeq; NP_001157161.1; NM_001163689.1. [Q8BJ56-1]
DR RefSeq; NP_080078.2; NM_025802.3. [Q8BJ56-2]
DR AlphaFoldDB; Q8BJ56; -.
DR SMR; Q8BJ56; -.
DR BioGRID; 211763; 5.
DR DIP; DIP-61641N; -.
DR IntAct; Q8BJ56; 2.
DR STRING; 10090.ENSMUSP00000127149; -.
DR BindingDB; Q8BJ56; -.
DR ChEMBL; CHEMBL3425391; -.
DR SwissLipids; SLP:000000317; -.
DR GlyGen; Q8BJ56; 1 site.
DR iPTMnet; Q8BJ56; -.
DR PhosphoSitePlus; Q8BJ56; -.
DR SwissPalm; Q8BJ56; -.
DR EPD; Q8BJ56; -.
DR jPOST; Q8BJ56; -.
DR MaxQB; Q8BJ56; -.
DR PaxDb; Q8BJ56; -.
DR PeptideAtlas; Q8BJ56; -.
DR PRIDE; Q8BJ56; -.
DR ProteomicsDB; 289932; -. [Q8BJ56-1]
DR ProteomicsDB; 289933; -. [Q8BJ56-2]
DR ProteomicsDB; 289934; -. [Q8BJ56-3]
DR Antibodypedia; 22689; 532 antibodies from 38 providers.
DR Ensembl; ENSMUST00000064151; ENSMUSP00000065116; ENSMUSG00000025509. [Q8BJ56-2]
DR Ensembl; ENSMUST00000164016; ENSMUSP00000127149; ENSMUSG00000025509. [Q8BJ56-1]
DR GeneID; 66853; -.
DR KEGG; mmu:66853; -.
DR UCSC; uc009klg.2; mouse. [Q8BJ56-2]
DR UCSC; uc009klh.2; mouse. [Q8BJ56-3]
DR UCSC; uc009kli.2; mouse. [Q8BJ56-1]
DR CTD; 57104; -.
DR MGI; MGI:1914103; Pnpla2.
DR VEuPathDB; HostDB:ENSMUSG00000025509; -.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000160155; -.
DR HOGENOM; CLU_018371_0_1_1; -.
DR InParanoid; Q8BJ56; -.
DR OMA; AFIPVYC; -.
DR OrthoDB; 1204225at2759; -.
DR PhylomeDB; Q8BJ56; -.
DR TreeFam; TF314272; -.
DR BRENDA; 3.1.1.3; 3474.
DR Reactome; R-MMU-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
DR UniPathway; UPA00256; -.
DR BioGRID-ORCS; 66853; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Pnpla2; mouse.
DR PRO; PR:Q8BJ56; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8BJ56; protein.
DR Bgee; ENSMUSG00000025509; Expressed in thoracic mammary gland and 241 other tissues.
DR ExpressionAtlas; Q8BJ56; baseline and differential.
DR Genevisible; Q8BJ56; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; ISO:MGI.
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; IDA:UniProtKB.
DR GO; GO:0044242; P:cellular lipid catabolic process; IMP:MGI.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; IDA:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; ISO:MGI.
DR GO; GO:0034389; P:lipid droplet organization; IMP:MGI.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IMP:UniProtKB.
DR GO; GO:0010891; P:negative regulation of sequestering of triglyceride; IDA:UniProtKB.
DR GO; GO:0010898; P:positive regulation of triglyceride catabolic process; IDA:UniProtKB.
DR GO; GO:0019433; P:triglyceride catabolic process; IDA: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 Alternative splicing; Cell membrane; Cytoplasm; Glycoprotein; Hydrolase;
KW Lipid degradation; Lipid droplet; Lipid metabolism; Membrane;
KW Phosphoprotein; Reference proteome; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..486
FT /note="Patatin-like phospholipase domain-containing protein
FT 2"
FT /id="PRO_0000292528"
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..331
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q96AD5"
FT TRANSMEM 332..352
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..486
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 465..486
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 374
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000269|PubMed:22733971"
FT MOD_RES 396
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:22733971"
FT MOD_RES 406
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:22733971,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000269|PubMed:22733971,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 468
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000269|PubMed:22733971"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..56
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026422"
FT VAR_SEQ 57..62
FT /note="VTGACL -> MSHACQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_026423"
FT VAR_SEQ 253..308
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_026424"
FT MUTAGEN 47
FT /note="S->A: Loss of triacylglycerol hydrolysis activity."
FT /evidence="ECO:0000269|PubMed:16679289"
FT MUTAGEN 396
FT /note="S->A: Slightly reduced TG hydrolase activity."
FT /evidence="ECO:0000269|PubMed:22733971"
FT MUTAGEN 406
FT /note="S->A: Reduced TG hydrolase activity."
FT /evidence="ECO:0000269|PubMed:22733971"
FT CONFLICT 3
FT /note="P -> T (in Ref. 4; BAB22387)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="R -> H (in Ref. 1; AAU33824)"
FT /evidence="ECO:0000305"
FT CONFLICT 193
FT /note="I -> V (in Ref. 4; BAE29364)"
FT /evidence="ECO:0000305"
FT CONFLICT 319..320
FT /note="DL -> VG (in Ref. 4; BAB22643)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="P -> T (in Ref. 4; BAE29364)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="R -> G (in Ref. 6; AAC36536)"
FT /evidence="ECO:0000305"
FT CONFLICT 389
FT /note="D -> G (in Ref. 5; AAH64747)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="L -> P (in Ref. 6; AAC36536)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 53657 MW; 512FE1931B72FC9C CRC64;
MFPRETKWNI SFAGCGFLGV YHIGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGA
CLGEAGANII EVSKEARKRF LGPLHPSFNL VKTIRGCLLK TLPADCHERA NGRLGISLTR
VSDGENVIIS HFSSKDELIQ ANVCSTFIPV YCGLIPPTLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PMVLREMCKQ
GYRDGLRFLR RNGLLNQPNP LLALPPVVPQ EEDAEEAAVV EERAGEEDQL QPYRKDRILE
HLPARLNEAL LEACVEPKDL MTTLSNMLPV RLATAMMVPY TLPLESAVSF TIRLLEWLPD
VPEDIRWMKE QTGSICQYLV MRAKRKLGDH LPSRLSEQVE LRRAQSLPSV PLSCATYSEA
LPNWVRNNLS LGDALAKWEE CQRQLLLGLF CTNVAFPPDA LRMRAPASPT AADPATPQDP
PGLPPC
