LPIN1_MOUSE
ID LPIN1_MOUSE Reviewed; 924 AA.
AC Q91ZP3; Q9CQI2; Q9JLG6;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Phosphatidate phosphatase LPIN1 {ECO:0000305};
DE EC=3.1.3.4 {ECO:0000269|PubMed:17158099};
DE AltName: Full=Fatty liver dystrophy protein {ECO:0000303|PubMed:11138012};
DE AltName: Full=Lipin-1 {ECO:0000303|PubMed:19717560};
GN Name=Lpin1; Synonyms=Flde {ECO:0000303|PubMed:11138012};
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), AND PROTEIN SEQUENCE OF 38-50;
RP 301-317; 362-369; 425-459; 570-577; 676-693; 708-732; 769-777; 811-843;
RP 868-888 AND 890-908.
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=11792863; DOI=10.1073/pnas.022634399;
RA Huffman T.A., Mothe-Satney I., Lawrence J.C. Jr.;
RT "Insulin-stimulated phosphorylation of lipin mediated by the mammalian
RT target of rapamycin.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1047-1052(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND VARIANT
RP FLD2J ARG-84.
RC STRAIN=BALB/cJ;
RX PubMed=11138012; DOI=10.1038/83685;
RA Peterfy M., Phan J., Xu P., Reue K.;
RT "Lipodystrophy in the fld mouse results from mutation of a new gene
RT encoding a nuclear protein, lipin.";
RL Nat. Genet. 27:121-124(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Skin, 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 [4]
RP ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16049017; DOI=10.1074/jbc.m503885200;
RA Peterfy M., Phan J., Reue K.;
RT "Alternatively spliced lipin isoforms exhibit distinct expression pattern,
RT subcellular localization, and role in adipogenesis.";
RL J. Biol. Chem. 280:32883-32889(2005).
RN [5]
RP FUNCTION AS COACTIVATOR, MUTAGENESIS OF ASP-712; ILE-726 AND LEU-727,
RP INDUCTION, AND INTERACTION WITH PPARGC1A AND PPARA.
RX PubMed=16950137; DOI=10.1016/j.cmet.2006.08.005;
RA Finck B.N., Gropler M.C., Chen Z., Leone T.C., Croce M.A., Harris T.E.,
RA Lawrence J.C. Jr., Kelly D.P.;
RT "Lipin 1 is an inducible amplifier of the hepatic PGC-1alpha/PPARalpha
RT regulatory pathway.";
RL Cell Metab. 4:199-210(2006).
RN [6]
RP PROTEIN SEQUENCE OF 103-115, PHOSPHORYLATION AT SER-106; SER-150; SER-285;
RP SER-287; SER-293; THR-298; SER-328; SER-392; SER-468; SER-472; SER-483;
RP SER-634; SER-635; SER-921 AND SER-923, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17105729; DOI=10.1074/jbc.m609537200;
RA Harris T.E., Huffman T.A., Chi A., Shabanowitz J., Hunt D.F., Kumar A.,
RA Lawrence J.C. Jr.;
RT "Insulin controls subcellular localization and multisite phosphorylation of
RT the phosphatidic acid phosphatase, lipin 1.";
RL J. Biol. Chem. 282:277-286(2007).
RN [7]
RP CATALYTIC ACTIVITY, TISSUE SPECIFICITY, COFACTOR, ACTIVITY REGULATION, AND
RP FUNCTION.
RX PubMed=17158099; DOI=10.1074/jbc.m610745200;
RA Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.;
RT "Three mammalian lipins act as phosphatidate phosphatases with distinct
RT tissue expression patterns.";
RL J. Biol. Chem. 282:3450-3457(2007).
RN [8]
RP SUBCELLULAR LOCATION, MUTAGENESIS OF SER-106, AND MUTAGENESIS OF SER-724
RP (ISOFORM 2).
RX PubMed=19717560; DOI=10.1074/jbc.m109.023663;
RA Donkor J., Zhang P., Wong S., O'Loughlin L., Dewald J., Kok B.P.,
RA Brindley D.N., Reue K.;
RT "A conserved serine residue is required for the phosphatidate phosphatase
RT activity but not the transcriptional coactivator functions of lipin-1 and
RT lipin-2.";
RL J. Biol. Chem. 284:29968-29978(2009).
RN [9]
RP SUMOYLATION AT LYS-599 AND LYS-629, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP LYS-599 AND LYS-629, TISSUE SPECIFICITY, AND INTERACTION WITH MEF2C.
RX PubMed=19753306; DOI=10.1371/journal.pone.0007031;
RA Liu G.H., Gerace L.;
RT "Sumoylation regulates nuclear localization of lipin-1alpha in neuronal
RT cells.";
RL PLoS ONE 4:E7031-E7031(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, 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 [11]
RP FUNCTION (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1), AND MUTAGENESIS OF
RP ASP-712.
RX PubMed=21397848; DOI=10.1016/j.devcel.2011.01.004;
RA Huang H., Gao Q., Peng X., Choi S.Y., Sarma K., Ren H., Morris A.J.,
RA Frohman M.A.;
RT "piRNA-associated germline nuage formation and spermatogenesis require
RT MitoPLD profusogenic mitochondrial-surface lipid signaling.";
RL Dev. Cell 20:376-387(2011).
RN [12]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND DEPHOSPHORYLATION BY CTDNEP1.
RX PubMed=22134922; DOI=10.1074/jbc.m111.324350;
RA Han S., Bahmanyar S., Zhang P., Grishin N., Oegema K., Crooke R.,
RA Graham M., Reue K., Dixon J.E., Goodman J.M.;
RT "Nuclear envelope phosphatase-regulatory subunit 1 (formerly TMEM188) is
RT the metazoan SPO7 ortholog and functions in the lipin activation pathway.";
RL J. Biol. Chem. 287:3123-3137(2012).
CC -!- FUNCTION: Acts as a magnesium-dependent phosphatidate phosphatase
CC enzyme which catalyzes the conversion of phosphatidic acid to
CC diacylglycerol during triglyceride, phosphatidylcholine and
CC phosphatidylethanolamine biosynthesis and therefore controls the
CC metabolism of fatty acids at different levels (PubMed:17158099). Acts
CC also as nuclear transcriptional coactivator for PPARGC1A/PPARA
CC regulatory pathway to modulate lipid metabolism gene expression
CC (PubMed:16950137). Is involved in adipocyte differentiation
CC (PubMed:16049017). {ECO:0000269|PubMed:16049017,
CC ECO:0000269|PubMed:16950137, ECO:0000269|PubMed:17158099}.
CC -!- FUNCTION: [Isoform 1]: Recruited at the mitochondrion outer membrane
CC and is involved in mitochondrial fission by converting phosphatidic
CC acid to diacylglycerol. {ECO:0000269|PubMed:21397848}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphate + H2O = a 1,2-diacyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:27429, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:17815, ChEBI:CHEBI:43474, ChEBI:CHEBI:58608; EC=3.1.3.4;
CC Evidence={ECO:0000269|PubMed:17158099};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27430;
CC Evidence={ECO:0000305|PubMed:17158099};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + H2O = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43296,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:77129,
CC ChEBI:CHEBI:77130; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43297;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + H2O = 1-octadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43296,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:77129,
CC ChEBI:CHEBI:77130; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43297;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + H2O = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43292,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75728,
CC ChEBI:CHEBI:77091; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43293;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-octadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + H2O = 1-octadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43292,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:75728,
CC ChEBI:CHEBI:77091; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43293;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + H2O = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43288, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43289;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-octadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + H2O = 1-octadecanoyl-2-(9Z,12Z)-octadecadienoyl-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43288, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77097, ChEBI:CHEBI:77098;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43289;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:43284, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:75468;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43285;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = 1-octadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:43284, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:74560, ChEBI:CHEBI:75468;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43285;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43280,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:82928,
CC ChEBI:CHEBI:82949; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43281;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycero-3-phosphate + H2O = 1-hexadecanoyl-2-(4Z,7Z,10Z,13Z,16Z,19Z-
CC docosahexaenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43280,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:82928,
CC ChEBI:CHEBI:82949; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43281;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-dioctadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dioctadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:33335,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:41847, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:82921; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33336;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + H2O = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43260,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72864,
CC ChEBI:CHEBI:77096; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43261;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-
CC 3-phosphate + H2O = 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-
CC eicosatetraenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43260,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72864,
CC ChEBI:CHEBI:77096; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43261;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + H2O = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43256, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:72860, ChEBI:CHEBI:82927;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43257;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-glycero-3-
CC phosphate + H2O = 1-hexadecanoyl-2-(9Z,12Z-octadecadienoyl)-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43256, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:72860, ChEBI:CHEBI:82927;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43257;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycero-3-phosphate +
CC H2O = 1-hexadecanoyl-2-(9Z-octadecenoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:41255, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:64839, ChEBI:CHEBI:75466;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:41256;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1,2-di-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phosphate + H2O = 1,2-di-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43252, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:82924, ChEBI:CHEBI:82925;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43253;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-di-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-glycero-3-
CC phosphate + H2O = 1,2-di-(4Z,7Z,10Z,13Z,16Z,19Z-docosahexaenoyl)-sn-
CC glycerol + phosphate; Xref=Rhea:RHEA:43252, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:82924, ChEBI:CHEBI:82925;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43253;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate
CC + H2O = 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:43248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77125, ChEBI:CHEBI:77126;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43249;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycero-3-phosphate
CC + H2O = 1,2-di-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-sn-glycerol +
CC phosphate; Xref=Rhea:RHEA:43248, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:77125, ChEBI:CHEBI:77126;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43249;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H2O =
CC 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:43240, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:77127, ChEBI:CHEBI:77128;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43241;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycero-3-phosphate + H2O =
CC 1,2-di-(9Z,12Z-octadecadienoyl)-sn-glycerol + phosphate;
CC Xref=Rhea:RHEA:43240, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:77127, ChEBI:CHEBI:77128;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43241;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 1]:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1,2-
CC di-(9Z-octadecenoyl)-sn-glycerol + phosphate; Xref=Rhea:RHEA:43244,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:52333,
CC ChEBI:CHEBI:74546; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43245;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- CATALYTIC ACTIVITY: [Isoform 2]:
CC Reaction=1,2-dihexadecanoyl-sn-glycero-3-phosphate + H2O = 1,2-
CC dihexadecanoyl-sn-glycerol + phosphate; Xref=Rhea:RHEA:43236,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:72859,
CC ChEBI:CHEBI:82929; Evidence={ECO:0000250|UniProtKB:Q14693};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:43237;
CC Evidence={ECO:0000250|UniProtKB:Q14693};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17158099};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide treatment.
CC {ECO:0000269|PubMed:17158099}.
CC -!- SUBUNIT: Interacts (via LXXIL motif) with PPARA (PubMed:16950137).
CC Interacts with PPARGC1A (PubMed:16950137). Interaction with PPARA and
CC PPARGC1A leads to the formation of a complex that modulates gene
CC transcription (PubMed:16950137). Interacts with MEF2C
CC (PubMed:19753306). {ECO:0000269|PubMed:16950137,
CC ECO:0000269|PubMed:19753306}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion outer membrane
CC {ECO:0000269|PubMed:21397848}. Cytoplasm {ECO:0000269|PubMed:16049017,
CC ECO:0000269|PubMed:21397848}. Nucleus membrane
CC {ECO:0000269|PubMed:21397848}. Note=Recruited at the mitochondrion
CC outer membrane following phosphatidic acid formation mediated by PLD6.
CC In neuronals cells, isoform 1 is exclusively cytoplasmic
CC (PubMed:21397848). In 3T3-L1 pre-adipocytes, it primarily located in
CC the cytoplasm (PubMed:16049017). {ECO:0000269|PubMed:16049017,
CC ECO:0000269|PubMed:21397848}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:11138012, ECO:0000269|PubMed:16049017,
CC ECO:0000269|PubMed:17105729, ECO:0000269|PubMed:19753306,
CC ECO:0000269|PubMed:22134922}. Cytoplasm {ECO:0000269|PubMed:19753306}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q14693}.
CC Note=Nuclear localization requires both CNEP1R1 and CTDNEP1
CC (PubMed:22134922). In neuronals cells, localized in both the cytoplasm
CC and the nucleus (PubMed:19753306). In 3T3-L1 pre-adipocytes, it is
CC predominantly nuclear (PubMed:16049017). Translocates from the cytosol
CC to the endoplasmic reticulum following acetylation by KAT5 (By
CC similarity). {ECO:0000250|UniProtKB:Q14693,
CC ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:19753306,
CC ECO:0000269|PubMed:22134922}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Lipin-beta {ECO:0000303|PubMed:16049017};
CC IsoId=Q91ZP3-1; Sequence=Displayed;
CC Name=2; Synonyms=Lipin-alpha {ECO:0000303|PubMed:16049017};
CC IsoId=Q91ZP3-2; Sequence=VSP_003134;
CC -!- TISSUE SPECIFICITY: Specifically expressed in skeletal muscle. Also
CC expressed prominently in adipose tissue, and testis. Lower expression
CC also detected in kidney, lung, brain and liver.
CC {ECO:0000269|PubMed:16049017, ECO:0000269|PubMed:17158099,
CC ECO:0000269|PubMed:19753306, ECO:0000269|PubMed:22134922}.
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Predominant isoform in the liver.
CC {ECO:0000269|PubMed:16049017}.
CC -!- TISSUE SPECIFICITY: [Isoform 2]: Predominant isoform in the brain.
CC {ECO:0000269|PubMed:16049017}.
CC -!- INDUCTION: By fasting, glucocorticoids and diabetes in the liver in a
CC PPARGC1A-dependent manner. Up-regulated during differentiation of 3T3-
CC L1 pre-adipocytes. {ECO:0000269|PubMed:16950137}.
CC -!- DOMAIN: Contains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic
CC motif essential for phosphatidate phosphatase activity.
CC {ECO:0000269|PubMed:19717560}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional
CC binding motif, which mediates interaction with PPARA.
CC {ECO:0000269|PubMed:16950137}.
CC -!- PTM: Phosphorylated at multiple sites in response to insulin.
CC Phosphorylation is controlled by the mTOR signaling pathway.
CC Phosphorylation is decreased by epinephrine. Phosphorylation may not
CC directly affect the catalytic activity but may regulate the
CC localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex.
CC {ECO:0000269|PubMed:17105729}.
CC -!- PTM: Sumoylation is important in brain and is marginal in other
CC tissues. Sumoylation facilitates nuclear localization of isoform 2 in
CC neuronals cells and its transcriptional coactivator activity.
CC {ECO:0000269|PubMed:19753306}.
CC -!- PTM: Acetylation at Lys-459 and Lys-629 by KAT5 in response to fatty
CC acids promotes translocation to the endoplasmic reticulum and synthesis
CC of diacylglycerol. {ECO:0000250|UniProtKB:Q14693}.
CC -!- DISEASE: Note=Defects in Lpin1 are the cause of the fatty liver
CC dystrophy phenotype (fld). Fld mutant mice are characterized by
CC neonatal fatty liver and hypertriglyceridemia that resolve at weaning,
CC and neuropathy affecting peripheral nerve in adulthood. Adipose tissue
CC deficiency, glucose intolerance and increased susceptibility to
CC atherosclerosis are associated with this mutation too. Two independent
CC mutant alleles are characterized in this phenotype, fld and fld2j.
CC {ECO:0000269|PubMed:11138012}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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DR EMBL; AF412811; AAL07798.1; -; mRNA.
DR EMBL; AF180471; AAF44296.1; -; mRNA.
DR EMBL; AK019539; BAB31786.1; -; mRNA.
DR EMBL; AK014526; BAB29412.1; -; mRNA.
DR CCDS; CCDS25822.1; -. [Q91ZP3-1]
DR CCDS; CCDS25823.1; -. [Q91ZP3-2]
DR RefSeq; NP_001123884.1; NM_001130412.1.
DR RefSeq; NP_056578.2; NM_015763.4.
DR RefSeq; NP_766538.2; NM_172950.3.
DR RefSeq; XP_006515051.1; XM_006514988.3.
DR PDB; 7KIH; X-ray; 1.47 A; A=491-581.
DR PDB; 7KIL; X-ray; 1.90 A; A/B=491-581.
DR PDBsum; 7KIH; -.
DR PDBsum; 7KIL; -.
DR AlphaFoldDB; Q91ZP3; -.
DR SMR; Q91ZP3; -.
DR BioGRID; 199700; 1.
DR IntAct; Q91ZP3; 3.
DR MINT; Q91ZP3; -.
DR STRING; 10090.ENSMUSP00000070583; -.
DR SwissLipids; SLP:000000601; -.
DR iPTMnet; Q91ZP3; -.
DR PhosphoSitePlus; Q91ZP3; -.
DR SwissPalm; Q91ZP3; -.
DR EPD; Q91ZP3; -.
DR jPOST; Q91ZP3; -.
DR MaxQB; Q91ZP3; -.
DR PaxDb; Q91ZP3; -.
DR PRIDE; Q91ZP3; -.
DR ProteomicsDB; 287258; -. [Q91ZP3-1]
DR ProteomicsDB; 287259; -. [Q91ZP3-2]
DR DNASU; 14245; -.
DR GeneID; 14245; -.
DR KEGG; mmu:14245; -.
DR UCSC; uc007nbs.2; mouse. [Q91ZP3-1]
DR CTD; 23175; -.
DR MGI; MGI:1891340; Lpin1.
DR eggNOG; KOG2116; Eukaryota.
DR InParanoid; Q91ZP3; -.
DR OrthoDB; 866929at2759; -.
DR PhylomeDB; Q91ZP3; -.
DR TreeFam; TF314095; -.
DR BRENDA; 3.1.3.4; 3474.
DR Reactome; R-MMU-1483191; Synthesis of PC.
DR Reactome; R-MMU-1483213; Synthesis of PE.
DR Reactome; R-MMU-4419969; Depolymerisation of the Nuclear Lamina.
DR Reactome; R-MMU-75109; Triglyceride biosynthesis.
DR BioGRID-ORCS; 14245; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Lpin1; mouse.
DR PRO; PR:Q91ZP3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q91ZP3; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; IDA:MGI.
DR GO; GO:0042975; F:peroxisome proliferator activated receptor binding; IPI:UniProtKB.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:UniProtKB.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:MGI.
DR GO; GO:0044255; P:cellular lipid metabolic process; IMP:MGI.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IMP:MGI.
DR GO; GO:0045444; P:fat cell differentiation; NAS:UniProtKB.
DR GO; GO:0009062; P:fatty acid catabolic process; IDA:UniProtKB.
DR GO; GO:0006955; P:immune response; IMP:MGI.
DR GO; GO:0006629; P:lipid metabolic process; IMP:MGI.
DR GO; GO:0000266; P:mitochondrial fission; IDA:UniProtKB.
DR GO; GO:0031642; P:negative regulation of myelination; ISO:MGI.
DR GO; GO:1903741; P:negative regulation of phosphatidate phosphatase activity; ISO:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0046473; P:phosphatidic acid metabolic process; ISS:UniProtKB.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IMP:YuBioLab.
DR GO; GO:0045740; P:positive regulation of DNA replication; ISO:MGI.
DR GO; GO:0031065; P:positive regulation of histone deacetylation; IMP:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045598; P:regulation of fat cell differentiation; IMP:MGI.
DR GO; GO:0031529; P:ruffle organization; IMP:MGI.
DR GO; GO:0019432; P:triglyceride biosynthetic process; ISS:UniProtKB.
DR GO; GO:0006642; P:triglyceride mobilization; IDA:UniProtKB.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR026058; LIPIN.
DR InterPro; IPR031703; Lipin_mid.
DR InterPro; IPR007651; Lipin_N.
DR InterPro; IPR013209; LNS2.
DR InterPro; IPR031315; LNS2/PITP.
DR InterPro; IPR028794; LPIN1.
DR PANTHER; PTHR12181; PTHR12181; 1.
DR PANTHER; PTHR12181:SF10; PTHR12181:SF10; 1.
DR Pfam; PF16876; Lipin_mid; 1.
DR Pfam; PF04571; Lipin_N; 1.
DR Pfam; PF08235; LNS2; 1.
DR SMART; SM00775; LNS2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Direct protein sequencing; Disease variant; Endoplasmic reticulum;
KW Hydrolase; Isopeptide bond; Membrane; Mitochondrion;
KW Mitochondrion outer membrane; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..924
FT /note="Phosphatidate phosphatase LPIN1"
FT /id="PRO_0000209880"
FT REGION 1..108
FT /note="N-LIP"
FT REGION 133..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..649
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 658..864
FT /note="C-LIP"
FT MOTIF 153..158
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 712..716
FT /note="DXDXT motif"
FT /evidence="ECO:0000305|PubMed:19717560"
FT MOTIF 723..727
FT /note="LXXIL motif"
FT /evidence="ECO:0000305|PubMed:16950137"
FT COMPBIAS 215..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 463..490
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 106
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 298
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 459
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14693"
FT MOD_RES 468
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 483
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 629
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q14693"
FT MOD_RES 634
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 921
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT MOD_RES 923
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17105729"
FT CROSSLNK 599
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:19753306"
FT CROSSLNK 629
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:19753306"
FT VAR_SEQ 241..273
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11138012"
FT /id="VSP_003134"
FT VARIANT 84
FT /note="G -> R (in allele FLD2J; causes the fatty liver
FT dystrophy phenotype (fld), characterized by neonatal fatty
FT liver and hypertriglyceridemia that resolve at weaning and
FT neuropathy affecting peripheral nerve in adulthood)"
FT /evidence="ECO:0000269|PubMed:11138012"
FT MUTAGEN 106
FT /note="S->A: Abolishes phosphorylation in response to
FT insulin but has no effect on cellular location."
FT /evidence="ECO:0000269|PubMed:19717560"
FT MUTAGEN 599
FT /note="K->R: Reduces sumoylation. Abolishes sumoylation and
FT nuclear localization; when associated with R-629."
FT /evidence="ECO:0000269|PubMed:19753306"
FT MUTAGEN 629
FT /note="K->R: Reduces sumoylation. Abolishes sumoylation and
FT nuclear localization; when associated with R-599."
FT /evidence="ECO:0000269|PubMed:19753306"
FT MUTAGEN 712
FT /note="D->A,E: Abolishes phosphatidate phosphatase
FT activity. No effect on interaction or coactivation with
FT PPARA."
FT /evidence="ECO:0000269|PubMed:16950137,
FT ECO:0000269|PubMed:21397848"
FT MUTAGEN 726
FT /note="I->F: Diminishes significantly the interaction and
FT coactivation OF PPARA; when associated with F-727."
FT /evidence="ECO:0000269|PubMed:16950137"
FT MUTAGEN 727
FT /note="L->F: Diminishes significantly the interaction and
FT coactivation OF PPARA; when associated with F-726."
FT /evidence="ECO:0000269|PubMed:16950137"
FT CONFLICT 175
FT /note="S -> T (in Ref. 3; BAB31786/BAB29412)"
FT /evidence="ECO:0000305"
FT CONFLICT 223
FT /note="H -> Y (in Ref. 3; BAB31786/BAB29412)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="G -> V (in Ref. 2; AAF44296)"
FT /evidence="ECO:0000305"
FT STRAND 498..502
FT /evidence="ECO:0007829|PDB:7KIH"
FT TURN 506..509
FT /evidence="ECO:0007829|PDB:7KIH"
FT HELIX 514..519
FT /evidence="ECO:0007829|PDB:7KIH"
FT HELIX 524..529
FT /evidence="ECO:0007829|PDB:7KIH"
FT HELIX 531..535
FT /evidence="ECO:0007829|PDB:7KIH"
FT STRAND 540..543
FT /evidence="ECO:0007829|PDB:7KIH"
FT STRAND 546..548
FT /evidence="ECO:0007829|PDB:7KIH"
FT HELIX 550..563
FT /evidence="ECO:0007829|PDB:7KIH"
FT HELIX 569..579
FT /evidence="ECO:0007829|PDB:7KIH"
FT MUTAGEN Q91ZP3-2:724
FT /note="S->L: Abolishes phosphatidate phosphatase activity
FT but does not prevent membrane association."
FT /evidence="ECO:0000269|PubMed:19717560"
SQ SEQUENCE 924 AA; 102002 MW; 175F90E9159A216A CRC64;
MNYVGQLAGQ VFVTVKELYK GLNPATLSGC IDIIVIRQPN GSLQCSPFHV RFGKMGVLRS
REKVVDIEIN GESVDLHMKL GDNGEAFFVQ ETDNDQEIIP MYLATSPILS EGAARMESQL
KRNSVDRIRC LDPTTAAQGL PPSDTPSTGS LGKKRRKRRR KAQLDNLKRD DNVNSSEDED
MFPIEMSSDE DTAPMDGSRT LPNDVPPFQD DIPKENFPSI STHPQSASYP SSDREWSPSP
SSLVDCQRTP PHLAEGVLSS SCPLQSCHFH ASESPSGSRP STPKSDSELV SKSADRLTPK
NNLEMLWLWG ELPQAAKSSS PHKMKESSPL GSRKTPDKMN FQAIHSESSD TFSDQSPTMA
RGLLIHQSKA QTEMQFVNEE DLESLGAAAP PSPVAEELKA PYPNTAQSSS KTDSPSRKKD
KRSRHLGADG VYLDDLTDMD PEVAALYFPK NGDPGGLPKQ ASDNGARSAN QSPQSVGGSG
IDSGVESTSD SLRDLPSIAI SLCGGLSDHR EITKDAFLEQ AVSYQQFADN PAIIDDPNLV
VKVGNKYYNW TTAAPLLLAM QAFQKPLPKA TVESIMRDKM PKKGGRWWFS WRGRNATIKE
ESKPEQCLTG KGHNTGEQPA QLGLATRIKH ESSSSDEEHA AAKPSGSSHL SLLSNVSYKK
TLRLTSEQLK SLKLKNGPND VVFSVTTQYQ GTCRCEGTIY LWNWDDKVII SDIDGTITRS
DTLGHILPTL GKDWTHQGIA KLYHKVSQNG YKFLYCSARA IGMADMTRGY LHWVNERGTV
LPQGPLLLSP SSLFSALHRE VIEKKPEKFK VQCLTDIKNL FFPNTEPFYA AFGNRPADVY
SYKQVGVSLN RIFTVNPKGE LVQEHAKTNI SSYVRLCEVV DHVFPLLKRS HSCDFPCSDT
FSNFTFWREP LPPFENQDMH SASA
