LPIN3_MOUSE
ID LPIN3_MOUSE Reviewed; 848 AA.
AC Q99PI4; Q3TQ75; Q8C7R9;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Phosphatidate phosphatase LPIN3 {ECO:0000305};
DE EC=3.1.3.4 {ECO:0000269|PubMed:17158099};
DE AltName: Full=Lipin-3;
GN Name=Lpin3 {ECO:0000312|MGI:MGI:1891342};
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Head;
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 [3]
RP TISSUE SPECIFICITY, CATALYTIC ACTIVITY, 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Pancreas, 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).
CC -!- FUNCTION: Magnesium-dependent phosphatidate phosphatase enzyme which
CC catalyzes the conversion of phosphatidic acid to diacylglycerol during
CC triglyceride, phosphatidylcholine and phosphatidylethanolamine
CC biosynthesis therefore regulates fatty acid metabolism.
CC {ECO:0000269|PubMed:17158099}.
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:0000269|PubMed:17158099};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17158099};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide.
CC {ECO:0000269|PubMed:17158099}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Significant expression in intestine and other
CC regions of the gastrointestinal tract. {ECO:0000269|PubMed:17158099}.
CC -!- DOMAIN: Contains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif
CC known to be essential for phosphatidate phosphatase activity.
CC {ECO:0000250}.
CC -!- DOMAIN: Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known
CC to be a transcriptional binding motif. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the lipin family. {ECO:0000305}.
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DR EMBL; AF286724; AAG52762.1; -; mRNA.
DR EMBL; AK049363; BAC33710.1; -; mRNA.
DR EMBL; AK163833; BAE37510.1; -; mRNA.
DR CCDS; CCDS16998.1; -.
DR RefSeq; NP_001186047.1; NM_001199118.1.
DR RefSeq; NP_075021.1; NM_022883.3.
DR AlphaFoldDB; Q99PI4; -.
DR SMR; Q99PI4; -.
DR BioGRID; 211111; 1.
DR STRING; 10090.ENSMUSP00000105082; -.
DR SwissLipids; SLP:000000603; -.
DR iPTMnet; Q99PI4; -.
DR PhosphoSitePlus; Q99PI4; -.
DR MaxQB; Q99PI4; -.
DR PaxDb; Q99PI4; -.
DR PRIDE; Q99PI4; -.
DR ProteomicsDB; 290144; -.
DR Antibodypedia; 27036; 166 antibodies from 26 providers.
DR DNASU; 64899; -.
DR Ensembl; ENSMUST00000040872; ENSMUSP00000043053; ENSMUSG00000027412.
DR Ensembl; ENSMUST00000109456; ENSMUSP00000105082; ENSMUSG00000027412.
DR GeneID; 64899; -.
DR KEGG; mmu:64899; -.
DR UCSC; uc008nrh.2; mouse.
DR CTD; 64900; -.
DR MGI; MGI:1891342; Lpin3.
DR VEuPathDB; HostDB:ENSMUSG00000027412; -.
DR eggNOG; KOG2116; Eukaryota.
DR GeneTree; ENSGT00940000160046; -.
DR HOGENOM; CLU_002546_0_1_1; -.
DR InParanoid; Q99PI4; -.
DR OMA; TWSSINP; -.
DR OrthoDB; 866929at2759; -.
DR TreeFam; TF314095; -.
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; 64899; 2 hits in 76 CRISPR screens.
DR PRO; PR:Q99PI4; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q99PI4; protein.
DR Bgee; ENSMUSG00000027412; Expressed in dorsal pancreas and 77 other tissues.
DR ExpressionAtlas; Q99PI4; baseline and differential.
DR Genevisible; Q99PI4; MM.
DR GO; GO:0005634; C:nucleus; ISA:MGI.
DR GO; GO:0008195; F:phosphatidate phosphatase activity; IDA:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0044255; P:cellular lipid metabolic process; IBA:GO_Central.
DR GO; GO:0032869; P:cellular response to insulin stimulus; IBA:GO_Central.
DR GO; GO:0009062; P:fatty acid catabolic process; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0019432; P:triglyceride biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_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 PANTHER; PTHR12181; PTHR12181; 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 Fatty acid metabolism; Hydrolase; Lipid metabolism; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..848
FT /note="Phosphatidate phosphatase LPIN3"
FT /id="PRO_0000209884"
FT REGION 1..108
FT /note="N-LIP"
FT /evidence="ECO:0000250"
FT REGION 97..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 314..373
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..568
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..789
FT /note="C-LIP"
FT /evidence="ECO:0000250"
FT MOTIF 135..144
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT MOTIF 641..645
FT /note="DXDXT motif"
FT MOTIF 652..656
FT /note="LXXIL motif"
FT COMPBIAS 173..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 323..366
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 155
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQK8"
FT CONFLICT 833
FT /note="S -> G (in Ref. 2; BAC33710)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 848 AA; 94316 MW; ABD92B98EF0D71B2 CRC64;
MNYVGQLAET VFGTVKELYR GLNPATLSGG IDVLVVRQRD GSFRCSPFHV RFGKLGVLRS
REKVVDIEIN GEPVDLHMKL GDSGEAFFVQ ELDSDEEDVP PRLCTSPIPW GGLSGFPSDS
QIGTASEPEG LVITGRRKRR RRRKPRRREE DAVDSSSEEL EAGAESELTL LEKPTPESPS
AQEAEEPSSQ PKDIHPYSDG ECTPQANLSS GDLMSPKSDS ELELRSLEPS PLRAESHMQW
VWGRLPKVAK AERPEFSLIL ESMAEAICAL PEEPSPSSSP SEAGVDTLSP PVLHPGVRAD
TFHPAVEAHC EETAVDSPLA APESKETKTQ NSRGAGHPPA TKSWSWTTPE SHTPSGHPQV
SRGKGSLKRN QHLGPSDIYL DDLPSLDSEN VALYFPKSEY GMGARRWSEP SNQKLLESPN
PEHIAECTLD SVDKIELSLC GGLADNRDIS LEKFTQHMVS YEDLTKNPGL LDDPNLVVKI
NEKHYNWAVA APMILSLQAF QKNLPESTVD KLEKEKMPRK GGRWWFSWRR RDFPAEEHSS
QREKAATRKQ QGEKTEVLSS DDDVPDSPVI LEVPPLPSST PGYVPTYKKS LRLSSDQIRC
LNLNEGANDV VFSVTTQYQG TCRCKATIYL WNWDDKVVIS DIDGTITKSD ALGHILPQLG
KDWTHQGITS LYHKIHLNGY KFLYCSARAI GMADLTKGYL QWVSEHGCGL PKGPILLSPS
SLFSALHREV IEKKPEVFKV ACLSDIQQLF LPQRQPFHAA FGNRPNDVFA YRQVGLPESR
IFTVNPRGEL IQELIKSHKS TYQRLGEVVE LLFPPVVRGP STDLASPEYS NLSYWRKPLP
YVDFEALA
