PLPL2_HUMAN
ID PLPL2_HUMAN Reviewed; 504 AA.
AC Q96AD5; O60643; Q5EFF5; Q6XYE5; Q96ET6; Q9NQ61; Q9NQ62;
DT 26-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Patatin-like phospholipase domain-containing protein 2 {ECO:0000305};
DE EC=3.1.1.3 {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16239926, ECO:0000269|PubMed:17603008};
DE AltName: Full=Adipose triglyceride lipase {ECO:0000303|PubMed:15550674};
DE AltName: Full=Calcium-independent phospholipase A2-zeta {ECO:0000303|PubMed:15364929};
DE Short=iPLA2-zeta {ECO:0000303|PubMed:15364929};
DE EC=3.1.1.4 {ECO:0000269|PubMed:15364929, ECO:0000269|PubMed:17032652};
DE AltName: Full=Desnutrin;
DE AltName: Full=Pigment epithelium-derived factor receptor {ECO:0000303|PubMed:17032652};
DE Short=PEDF-R {ECO:0000303|PubMed:17032652};
DE AltName: Full=TTS2.2 {ECO:0000303|PubMed:17603008};
DE AltName: Full=Transport-secretion protein 2;
DE Short=TTS2;
GN Name=PNPLA2 {ECO:0000312|HGNC:HGNC:30802};
GN Synonyms=ATGL {ECO:0000303|PubMed:15550674}; ORFNames=FP17548;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP CATALYTIC ACTIVITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT PRO-481.
RA Strahl T., Shingler W.H., Lammiman M., Gregory C.D., Leach L., Matthias P.,
RA Nielsen P.J., Shaw P.E.;
RT "TTS-2, a novel protein implicated in vesicular transport of the cell
RT surface receptor ICAM-3.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT PRO-481.
RC TISSUE=Brain, and Eye;
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 94-504 (ISOFORM 1).
RC TISSUE=Brain;
RA Yu W., Gibbs R.A.;
RL Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP FUNCTION, ACTIVITY REGULATION, AND CATALYTIC ACTIVITY.
RX PubMed=15364929; DOI=10.1074/jbc.m407841200;
RA Jenkins C.M., Mancuso D.J., Yan W., Sims H.F., Gibson B., Gross R.W.;
RT "Identification, cloning, expression, and purification of three novel human
RT calcium-independent phospholipase A2 family members possessing
RT triacylglycerol lipase and acylglycerol transacylase activities.";
RL J. Biol. Chem. 279:48968-48975(2004).
RN [8]
RP DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RX PubMed=16249444; DOI=10.2337/diabetes.54.11.3190;
RA Langin D., Dicker A., Tavernier G., Hoffstedt J., Mairal A., Ryden M.,
RA Arner E., Sicard A., Jenkins C.M., Viguerie N., van Harmelen V.,
RA Gross R.W., Holm C., Arner P.;
RT "Adipocyte lipases and defect of lipolysis in human obesity.";
RL Diabetes 54:3190-3197(2005).
RN [9]
RP TISSUE SPECIFICITY, MUTAGENESIS OF SER-47, CATALYTIC ACTIVITY, AND
RP FUNCTION.
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 [10]
RP DEVELOPMENTAL STAGE.
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 [11]
RP FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-47, AND CATALYTIC
RP ACTIVITY.
RX PubMed=16239926; DOI=10.1038/sj.embor.7400559;
RA Smirnova E., Goldberg E.B., Makarova K.S., Lin L., Brown W.J.,
RA Jackson C.L.;
RT "ATGL has a key role in lipid droplet/adiposome degradation in mammalian
RT cells.";
RL EMBO Rep. 7:106-113(2006).
RN [12]
RP ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH
RP SERPINF1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP FUNCTION, CATALYTIC ACTIVITY, AND TOPOLOGY.
RX PubMed=17032652; DOI=10.1074/jbc.m600353200;
RA Notari L., Baladron V., Aroca-Aguilar J.D., Balko N., Heredia R., Meyer C.,
RA Notario P.M., Saravanamuthu S., Nueda M.-L., Sanchez-Sanchez F.,
RA Escribano J., Laborda J., Becerra S.P.;
RT "Identification of a lipase-linked cell membrane receptor for pigment
RT epithelium-derived factor.";
RL J. Biol. Chem. 281:38022-38037(2006).
RN [13]
RP CATALYTIC ACTIVITY, AND FUNCTION.
RX PubMed=17603008; DOI=10.1016/j.bbrc.2007.06.089;
RA Gao J.G., Simon M.;
RT "A comparative study of human GS2, its paralogues, and its rat
RT orthologue.";
RL Biochem. Biophys. Res. Commun. 360:501-506(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP PHOSPHORYLATION AT SER-404.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-404 AND SER-428, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [18]
RP INTERACTION WITH FAF2.
RX PubMed=23297223; DOI=10.1073/pnas.1213738110;
RA Olzmann J.A., Richter C.M., Kopito R.R.;
RT "Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid
RT droplet turnover.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1345-1350(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-428, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP PHOSPHORYLATION AT SER-404.
RX PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
RA Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
RA Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
RA Pinna L.A., Pagliarini D.J., Dixon J.E.;
RT "A single kinase generates the majority of the secreted phosphoproteome.";
RL Cell 161:1619-1632(2015).
RN [21]
RP VARIANTS PHE-219; LYS-252 AND PRO-481, POLYMORPHISM, AND ASSOCIATION WITH
RP DIABETES MELLITUS TYPE 2.
RX PubMed=16644682; DOI=10.2337/db05-1498;
RA Schoenborn V., Heid I.M., Vollmert C., Lingenhel A., Adams T.D.,
RA Hopkins P.N., Illig T., Zimmermann R., Zechner R., Hunt S.C.,
RA Kronenberg F.;
RT "The ATGL gene is associated with free fatty acids, triglycerides, and type
RT 2 diabetes.";
RL Diabetes 55:1270-1275(2006).
RN [22]
RP VARIANT NLSDM LEU-195.
RX PubMed=17187067; DOI=10.1038/ng1951;
RA Fischer J., Lefevre C., Morava E., Mussini J.-M., Laforet P.,
RA Negre-Salvayre A., Lathrop M., Salvayre R.;
RT "The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in
RT neutral lipid storage disease with myopathy.";
RL Nat. Genet. 39:28-30(2007).
CC -!- FUNCTION: Catalyzes the initial step in triglyceride hydrolysis in
CC adipocyte and non-adipocyte lipid droplets (PubMed:15550674,
CC PubMed:15364929, PubMed:16150821, PubMed:17603008, PubMed:16239926).
CC Exhibits a strong preference for the hydrolysis of long-chain fatty
CC acid esters at the sn-2 position of the glycerol backbone and acts
CC coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (By
CC similarity). Also possesses acylglycerol transacylase and phospholipase
CC A2 activities (PubMed:15364929, PubMed:17032652, PubMed:17603008).
CC Transfers fatty acid from triglyceride to retinol, hydrolyzes
CC retinylesters, and generates 1,3-diacylglycerol from triglycerides
CC (PubMed:17603008). Regulates adiposome size and may be involved in the
CC degradation of adiposomes (PubMed:16239926). May play an important role
CC in energy homeostasis (By similarity). May play a role in the response
CC of the organism to starvation, enhancing hydrolysis of triglycerides
CC and providing free fatty acids to other tissues to be oxidized in
CC situations of energy depletion (By similarity).
CC {ECO:0000250|UniProtKB:Q8BJ56, ECO:0000269|PubMed:15364929,
CC ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16150821,
CC ECO:0000269|PubMed:16239926, ECO:0000269|PubMed:17032652,
CC ECO:0000269|PubMed:17603008}.
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:15364929, ECO:0000269|PubMed:15550674,
CC ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16239926,
CC ECO:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12045;
CC Evidence={ECO:0000305|PubMed:15550674, ECO:0000305|PubMed:16150821,
CC ECO:0000305|PubMed:17603008};
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:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44865;
CC Evidence={ECO:0000305|PubMed:17603008};
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:17603008,
CC ECO:0000305|PubMed:15550674};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43733;
CC Evidence={ECO:0000305|PubMed:15550674, ECO:0000305|PubMed:17603008};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44441;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44437;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44433;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:44677;
CC Evidence={ECO:0000305|PubMed:17603008};
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:0000269|PubMed:17603008, ECO:0000305|PubMed:15550674};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38381;
CC Evidence={ECO:0000305|PubMed:15550674, ECO:0000305|PubMed:17603008};
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:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38388;
CC Evidence={ECO:0000305|PubMed:17603008};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38332;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38328;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:15364929};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38324;
CC Evidence={ECO:0000305|PubMed:15364929};
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:0000269|PubMed:17603008};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:39988;
CC Evidence={ECO:0000305|PubMed:17603008};
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:0000269|PubMed:15364929, ECO:0000269|PubMed:17032652};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15802;
CC Evidence={ECO:0000305|PubMed:17032652};
CC -!- ACTIVITY REGULATION: The triglyceride lipase activity is inhibited by
CC BEL ((E)-6-(bromomethylene)-3-(1-naphthalenyl)-2H-tetrahydropyran-2-
CC one), a suicide substrate inhibitor (PubMed:17032652). No differences
CC in the acylglycerol transacylase was detected in the presence or
CC absence of ATP (PubMed:15364929). {ECO:0000269|PubMed:15364929,
CC ECO:0000269|PubMed:17032652}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5 with (1,2-dilinoleoyl)-phosphatidylcholine as
CC substrate. {ECO:0000269|PubMed:17032652};
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 (PubMed:17032652). Despite a colocalization in lipid droplets,
CC it probably does not interact with PLIN (By similarity). Interacts with
CC PLIN5; prevents interaction with ABHD5 (By similarity). Interacts with
CC FAF2 (PubMed:23297223). {ECO:0000250|UniProtKB:Q8BJ56,
CC ECO:0000269|PubMed:17032652, ECO:0000269|PubMed:23297223}.
CC -!- SUBCELLULAR LOCATION: Lipid droplet {ECO:0000269|PubMed:16239926}. Cell
CC membrane {ECO:0000269|PubMed:17032652}; Multi-pass membrane protein
CC {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BJ56}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96AD5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96AD5-2; Sequence=VSP_026421;
CC -!- TISSUE SPECIFICITY: Highest expression in adipose tissue. Also detected
CC in heart, skeletal muscle, and portions of the gastrointestinal tract.
CC Detected in normal retina and retinoblastoma cells. Detected in retinal
CC pigment epithelium and, at lower intensity, in the inner segments of
CC photoreceptors and in the ganglion cell layer of the neural retina (at
CC protein level). {ECO:0000269|PubMed:15550674,
CC ECO:0000269|PubMed:16150821, ECO:0000269|PubMed:16249444,
CC ECO:0000269|PubMed:17032652}.
CC -!- DEVELOPMENTAL STAGE: Induced during differentiation of primary
CC preadipocytes to adipocytes. Expression increased from fetal to adult
CC in retinal pigment epithelium. {ECO:0000269|PubMed:16249444,
CC ECO:0000269|PubMed:16705060, ECO:0000269|PubMed:17032652}.
CC -!- PTM: Phosphorylation at Ser-404 by PKA is increased during fasting and
CC moderate intensity exercise, and moderately increases lipolytic
CC activity (By similarity). Phosphorylation at Ser-404 is increased upon
CC beta-adrenergic stimulation (PubMed:22733971).
CC {ECO:0000250|UniProtKB:Q8BJ56, ECO:0000269|PubMed:22733971}.
CC -!- POLYMORPHISM: Genetic variations in PNPLA2 may influence plasma free
CC fatty acids and triglycerides levels, and fasting glucose
CC concentrations. {ECO:0000269|PubMed:16644682}.
CC -!- DISEASE: Note=Genetic variations in PNPLA2 may be associated with risk
CC of diabetes mellitus type 2. {ECO:0000269|PubMed:16644682}.
CC -!- DISEASE: Neutral lipid storage disease with myopathy (NLSDM)
CC [MIM:610717]: Neutral lipid storage disorder (NLSD) with myopathy but
CC without ichthyosis. NLSDs are characterized by the presence of
CC triglyceride-containing cytoplasmic droplets in leukocytes and in other
CC tissues, including bone marrow, skin, and muscle. Individuals with
CC NLSDM did not show obesity, in spite of a defect in triglyceride
CC degradation in fibroblasts and in marked triglyceride storage in liver,
CC muscles, and other visceral cells. {ECO:0000269|PubMed:17187067}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAP34448.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAC01131.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAC01132.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY894804; AAW81962.1; -; mRNA.
DR EMBL; AJ278475; CAC01131.1; ALT_INIT; mRNA.
DR EMBL; AJ278476; CAC01132.1; ALT_INIT; mRNA.
DR EMBL; AY203925; AAP34448.1; ALT_FRAME; mRNA.
DR EMBL; AP006621; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC011958; AAH11958.1; -; mRNA.
DR EMBL; BC017280; AAH17280.1; -; mRNA.
DR EMBL; AF055000; AAC09354.1; -; mRNA.
DR CCDS; CCDS7718.1; -. [Q96AD5-1]
DR RefSeq; NP_065109.1; NM_020376.3. [Q96AD5-1]
DR RefSeq; XP_016873517.1; XM_017018028.1. [Q96AD5-1]
DR AlphaFoldDB; Q96AD5; -.
DR SMR; Q96AD5; -.
DR BioGRID; 121370; 47.
DR IntAct; Q96AD5; 12.
DR MINT; Q96AD5; -.
DR STRING; 9606.ENSP00000337701; -.
DR BindingDB; Q96AD5; -.
DR ChEMBL; CHEMBL3822353; -.
DR SwissLipids; SLP:000000311; -.
DR GlyGen; Q96AD5; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q96AD5; -.
DR PhosphoSitePlus; Q96AD5; -.
DR BioMuta; PNPLA2; -.
DR DMDM; 74731110; -.
DR EPD; Q96AD5; -.
DR jPOST; Q96AD5; -.
DR MassIVE; Q96AD5; -.
DR MaxQB; Q96AD5; -.
DR PaxDb; Q96AD5; -.
DR PeptideAtlas; Q96AD5; -.
DR PRIDE; Q96AD5; -.
DR ProteomicsDB; 75955; -. [Q96AD5-1]
DR ProteomicsDB; 75956; -. [Q96AD5-2]
DR Antibodypedia; 22689; 532 antibodies from 38 providers.
DR DNASU; 57104; -.
DR Ensembl; ENST00000336615.9; ENSP00000337701.4; ENSG00000177666.17. [Q96AD5-1]
DR GeneID; 57104; -.
DR KEGG; hsa:57104; -.
DR MANE-Select; ENST00000336615.9; ENSP00000337701.4; NM_020376.4; NP_065109.1.
DR UCSC; uc001lrt.4; human. [Q96AD5-1]
DR CTD; 57104; -.
DR DisGeNET; 57104; -.
DR GeneCards; PNPLA2; -.
DR HGNC; HGNC:30802; PNPLA2.
DR HPA; ENSG00000177666; Tissue enhanced (adipose tissue, breast).
DR MalaCards; PNPLA2; -.
DR MIM; 609059; gene.
DR MIM; 610717; phenotype.
DR neXtProt; NX_Q96AD5; -.
DR OpenTargets; ENSG00000177666; -.
DR Orphanet; 98908; Neutral lipid storage myopathy.
DR Orphanet; 565612; Triglyceride deposit cardiomyovasculopathy.
DR PharmGKB; PA134903083; -.
DR VEuPathDB; HostDB:ENSG00000177666; -.
DR eggNOG; KOG3773; Eukaryota.
DR GeneTree; ENSGT00940000160155; -.
DR HOGENOM; CLU_018371_0_1_1; -.
DR InParanoid; Q96AD5; -.
DR OMA; AFIPVYC; -.
DR OrthoDB; 1204225at2759; -.
DR PhylomeDB; Q96AD5; -.
DR TreeFam; TF314272; -.
DR PathwayCommons; Q96AD5; -.
DR Reactome; R-HSA-1482883; Acyl chain remodeling of DAG and TAG.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; Q96AD5; -.
DR UniPathway; UPA00256; -.
DR BioGRID-ORCS; 57104; 12 hits in 1077 CRISPR screens.
DR ChiTaRS; PNPLA2; human.
DR GeneWiki; PNPLA2; -.
DR GenomeRNAi; 57104; -.
DR Pharos; Q96AD5; Tchem.
DR PRO; PR:Q96AD5; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q96AD5; protein.
DR Bgee; ENSG00000177666; Expressed in omental fat pad and 185 other tissues.
DR Genevisible; Q96AD5; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
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; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0016411; F:acylglycerol O-acyltransferase activity; IDA:UniProtKB.
DR GO; GO:0051265; F:diolein transacylation activity; IDA:UniProtKB.
DR GO; GO:0004465; F:lipoprotein lipase activity; TAS:Reactome.
DR GO; GO:0051264; F:mono-olein transacylation activity; IDA:UniProtKB.
DR GO; GO:0004623; F:phospholipase A2 activity; IDA:UniProtKB.
DR GO; GO:0050253; F:retinyl-palmitate esterase activity; EXP:UniProtKB.
DR GO; GO:0004806; F:triglyceride lipase activity; IDA:UniProtKB.
DR GO; GO:0036155; P:acylglycerol acyl-chain remodeling; TAS:Reactome.
DR GO; GO:0006651; P:diacylglycerol biosynthetic process; ISS:UniProtKB.
DR GO; GO:1905691; P:lipid droplet disassembly; IMP:UniProtKB.
DR GO; GO:0055088; P:lipid homeostasis; IBA:GO_Central.
DR GO; GO:0019915; P:lipid storage; IEA:Ensembl.
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; 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 Alternative splicing; Cell membrane; Cytoplasm; Disease variant;
KW Glycoprotein; Hydrolase; Lipid degradation; Lipid droplet;
KW Lipid metabolism; Membrane; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..504
FT /note="Patatin-like phospholipase domain-containing protein
FT 2"
FT /id="PRO_0000292527"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17032652"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..42
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:17032652"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 64..137
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17032652"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 159..329
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:17032652"
FT TRANSMEM 330..350
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 351..504
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:17032652"
FT DOMAIN 10..179
FT /note="PNPLA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01161"
FT REGION 463..492
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 372
FT /note="Phosphoserine; in vitro"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ56"
FT MOD_RES 404
FT /note="Phosphoserine; by PKA and FAM20C"
FT /evidence="ECO:0000269|PubMed:22733971,
FT ECO:0000269|PubMed:26091039, ECO:0007744|PubMed:23186163"
FT MOD_RES 428
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT CARBOHYD 39
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..324
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_026421"
FT VARIANT 195
FT /note="P -> L (in NLSDM; dbSNP:rs121918259)"
FT /evidence="ECO:0000269|PubMed:17187067"
FT /id="VAR_032995"
FT VARIANT 219
FT /note="L -> F (in dbSNP:rs140612115)"
FT /evidence="ECO:0000269|PubMed:16644682"
FT /id="VAR_032996"
FT VARIANT 252
FT /note="N -> K (in dbSNP:rs140201358)"
FT /evidence="ECO:0000269|PubMed:16644682"
FT /id="VAR_032997"
FT VARIANT 481
FT /note="L -> P (in dbSNP:rs1138693)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16644682, ECO:0000269|Ref.2"
FT /id="VAR_032998"
FT MUTAGEN 47
FT /note="S->A: Reduces rate of lipid hydrolysis; does not
FT affect the localization around the rim of the adiposomes."
FT /evidence="ECO:0000269|PubMed:16150821,
FT ECO:0000269|PubMed:16239926"
FT CONFLICT 163
FT /note="R -> G (in Ref. 6; AAC09354)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="I -> V (in Ref. 1; AAW81962)"
FT /evidence="ECO:0000305"
FT CONFLICT 333
FT /note="A -> G (in Ref. 3; AAP34448)"
FT /evidence="ECO:0000305"
FT CONFLICT 351
FT /note="R -> C (in Ref. 1; AAW81962)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="V -> L (in Ref. 2; CAC01131/CAC01132)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="L -> P (in Ref. 1; AAW81962)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 55316 MW; D9C16F942AB0B3C7 CRC64;
MFPREKTWNI SFAGCGFLGV YYVGVASCLR EHAPFLVANA THIYGASAGA LTATALVTGV
CLGEAGAKFI EVSKEARKRF LGPLHPSFNL VKIIRSFLLK VLPADSHEHA SGRLGISLTR
VSDGENVIIS HFNSKDELIQ ANVCSGFIPV YCGLIPPSLQ GVRYVDGGIS DNLPLYELKN
TITVSPFSGE SDICPQDSST NIHELRVTNT SIQFNLRNLY RLSKALFPPE PLVLREMCKQ
GYRDGLRFLQ RNGLLNRPNP LLALPPARPH GPEDKDQAVE SAQAEDYSQL PGEDHILEHL
PARLNEALLE ACVEPTDLLT TLSNMLPVRL ATAMMVPYTL PLESALSFTI RLLEWLPDVP
EDIRWMKEQT GSICQYLVMR AKRKLGRHLP SRLPEQVELR RVQSLPSVPL SCAAYREALP
GWMRNNLSLG DALAKWEECQ RQLLLGLFCT NVAFPPEALR MRAPADPAPA PADPASPQHQ
LAGPAPLLST PAPEARPVIG ALGL
