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Protein

Phosphatidate phosphatase LPIN2

Gene

Lpin2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays important roles in controlling the metabolism of fatty acids at differents levels. Acts as a magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis in the reticulum endoplasmic membrane. Acts also as a nuclear transcriptional coactivator for PPARGC1A to modulate lipid metabolism.2 Publications

Catalytic activityi

A 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate.1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by N-ethylmaleimide.1 Publication

GO - Molecular functioni

  • phosphatidate phosphatase activity Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • dephosphorylation Source: GOC
  • fatty acid metabolic process Source: UniProtKB-KW
  • lipid metabolic process Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1483191. Synthesis of PC.
R-MMU-1483213. Synthesis of PE.
R-MMU-75109. Triglyceride Biosynthesis.

Chemistry

SwissLipidsiSLP:000000602.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate phosphatase LPIN2 (EC:3.1.3.4)
Alternative name(s):
Lipin-2
Gene namesi
Name:Lpin2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:1891341. Lpin2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi731 – 7311S → D: Abolishes phosphatidate phosphatase activity but does not prevent membrane association. 1 Publication
Mutagenesisi731 – 7311S → L: Abolishes phosphatidate phosphatase activity but does not prevent membrane association nor coactivator activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893Phosphatidate phosphatase LPIN2PRO_0000209882Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei174 – 1741PhosphoserineCombined sources
Modified residuei186 – 1861PhosphoserineCombined sources
Modified residuei187 – 1871PhosphoserineCombined sources
Modified residuei563 – 5631PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99PI5.
MaxQBiQ99PI5.
PaxDbiQ99PI5.
PRIDEiQ99PI5.

PTM databases

iPTMnetiQ99PI5.
PhosphoSiteiQ99PI5.

Expressioni

Tissue specificityi

Expressed at high level in liver and to some extend in lung, kidney, placenta, spleen, thymus, lymph node, prostate, testes, small intestine, and colon. Expressed also in circulating red blood cells and site of lymphopoiesis.2 Publications

Inductioni

By fasting in hepatocytes. Up-regulated in fld/fld (defect in LPIN1) mice. Up-regulated at protein level but not at transcript level in ob/ob and db/db mice, two obese mice models.2 Publications

Gene expression databases

BgeeiQ99PI5.
CleanExiMM_LPIN2.
ExpressionAtlasiQ99PI5. baseline and differential.
GenevisibleiQ99PI5. MM.

Interactioni

Protein-protein interaction databases

BioGridi211110. 1 interaction.
STRINGi10090.ENSMUSP00000118610.

Structurei

3D structure databases

ProteinModelPortaliQ99PI5.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 108108N-LIPAdd
BLAST
Regioni632 – 834203C-LIPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi153 – 1586Nuclear localization signalSequence analysis
Motifi686 – 6905DXDXT motif
Motifi697 – 7015LXXIL motif

Domaini

Contains one Leu-Xaa-Xaa-Ile-Leu (LXXIL) motif, a motif known to be a transcriptional binding motif.By similarity

Sequence similaritiesi

Belongs to the lipin family.Curated

Phylogenomic databases

eggNOGiKOG2116. Eukaryota.
COG5083. LUCA.
GeneTreeiENSGT00390000011286.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ99PI5.
KOiK15728.
OrthoDBiEOG7QZG8X.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR031703. Lipin_mid.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
IPR026744. LPIN2.
[Graphical view]
PANTHERiPTHR12181:SF11. PTHR12181:SF11. 1 hit.
PfamiPF16876. Lipin_mid. 1 hit.
PF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99PI5-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MNYVGQLAGQ VLVTVKELYK GINQATLSGC IDVVVVRQQD GSYQCSPFHV
60 70 80 90 100
RFGKLGVLRS KEKVIDIEIN GSAVDLHMKL GDNGEAFFVE ETEEEYEKLP
110 120 130 140 150
AYLATSPIPT EDQFFKHIET PLVKSSGNER PAQSSDVSHT LESEAVFTQS
160 170 180 190 200
SVKKKKRRRK KCKQDNRKEE QAASPVAEDV GDVGVSSDDE KRAQAARGSS
210 220 230 240 250
NASLKEEDYK EPSLFHSGDN YPLSDGDWSP LETTYPQAVC PKSDSELEVK
260 270 280 290 300
PSESLLRSEP HMEWTWGGFP ESTKVTKRER YDYHPRTATI TPSENTHFRV
310 320 330 340 350
IPSEDSLIRE VEKDATVEDT TCTIVKPKPR ALCKQLSDAA STELPESPLE
360 370 380 390 400
APQISSLLDA DPVPSPSAEA PSEPKPAAKD SPTKKKGVHK RSQHQGPDDI
410 420 430 440 450
YLDDLKALEP EVAALYFPKS DTDPGSRQWP ESDTFSGSQS PQSVGSAAAD
460 470 480 490 500
SGTECLSDSA MDLPDVTLSL CGGLSENGEI SKEKFMEHII TYHEFAENPG
510 520 530 540 550
LIDNPNLVIR IYNRYYNWAL AAPMILSLQV FQKSLPKATV ESWVKDKMPK
560 570 580 590 600
KSGRWWFWRK KESMIKQLPE TKEGKSEVPP ANDLPSNAEE PTSARPAEND
610 620 630 640 650
TSSDEGSQEL EESIKVDPIT VETLSHCGTA SYKKSLRLSS DQIAKLKLHD
660 670 680 690 700
GPNDVVFSIT TQYQGTCRCA GTIYLWNWND KVIISDIDGT ITKSDALGQI
710 720 730 740 750
LPQLGKDWTH QGIARLYHSI NENGYKFLYC SARAIGMADM TRGYLHWVND
760 770 780 790 800
KGTILPRGPL MLSPSSLFSA FHREVIEKKP EKFKIECLND IKNLFAPSRQ
810 820 830 840 850
PFYAAFGNRP NDVYAYTQVG VPDCRIFTVN PKGELIQERT KGNKSSYHRL
860 870 880 890
SELVEHVFPL LSKEQNSAFP CPEFSSFCYW RDPIPDLDLD DLA
Length:893
Mass (Da):99,613
Last modified:May 24, 2004 - v2
Checksum:i8C7FD7881946F8EA
GO
Isoform 2 (identifier: Q99PI5-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     388-459: VHKRSQHQGP...DSGTECLSDS → LVWLKNNCLL...PKMNRNKNTF
     460-893: Missing.

Note: No experimental confirmation available.
Show »
Length:459
Mass (Da):50,997
Checksum:i69F763FB79AA0742
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti839 – 8391R → S in BAC34088 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei388 – 45972VHKRS…CLSDS → LVWLKNNCLLGDRCISGYDH GCVSRGPTWQLMTDSSARGP NALFWPLWAPGTQPYIRQNM HIPKMNRNKNTF in isoform 2. 1 PublicationVSP_010387Add
BLAST
Alternative sequencei460 – 893434Missing in isoform 2. 1 PublicationVSP_010388Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286723 mRNA. Translation: AAG52761.1.
AK033662 mRNA. Translation: BAC28415.1.
AK050138 mRNA. Translation: BAC34088.1.
AK086834 mRNA. Translation: BAC39754.1.
BC039698 mRNA. Translation: AAH39698.1.
CCDSiCCDS28956.1. [Q99PI5-1]
RefSeqiNP_075020.2. NM_022882.4. [Q99PI5-1]
XP_006524850.1. XM_006524787.2. [Q99PI5-1]
XP_006524851.1. XM_006524788.2. [Q99PI5-1]
UniGeneiMm.227924.

Genome annotation databases

EnsembliENSMUST00000129635; ENSMUSP00000119282; ENSMUSG00000024052. [Q99PI5-1]
ENSMUST00000156570; ENSMUSP00000120634; ENSMUSG00000024052. [Q99PI5-2]
GeneIDi64898.
KEGGimmu:64898.
UCSCiuc008dmc.1. mouse. [Q99PI5-2]
uc012awp.1. mouse. [Q99PI5-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286723 mRNA. Translation: AAG52761.1.
AK033662 mRNA. Translation: BAC28415.1.
AK050138 mRNA. Translation: BAC34088.1.
AK086834 mRNA. Translation: BAC39754.1.
BC039698 mRNA. Translation: AAH39698.1.
CCDSiCCDS28956.1. [Q99PI5-1]
RefSeqiNP_075020.2. NM_022882.4. [Q99PI5-1]
XP_006524850.1. XM_006524787.2. [Q99PI5-1]
XP_006524851.1. XM_006524788.2. [Q99PI5-1]
UniGeneiMm.227924.

3D structure databases

ProteinModelPortaliQ99PI5.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi211110. 1 interaction.
STRINGi10090.ENSMUSP00000118610.

Chemistry

SwissLipidsiSLP:000000602.

PTM databases

iPTMnetiQ99PI5.
PhosphoSiteiQ99PI5.

Proteomic databases

EPDiQ99PI5.
MaxQBiQ99PI5.
PaxDbiQ99PI5.
PRIDEiQ99PI5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000129635; ENSMUSP00000119282; ENSMUSG00000024052. [Q99PI5-1]
ENSMUST00000156570; ENSMUSP00000120634; ENSMUSG00000024052. [Q99PI5-2]
GeneIDi64898.
KEGGimmu:64898.
UCSCiuc008dmc.1. mouse. [Q99PI5-2]
uc012awp.1. mouse. [Q99PI5-1]

Organism-specific databases

CTDi9663.
MGIiMGI:1891341. Lpin2.

Phylogenomic databases

eggNOGiKOG2116. Eukaryota.
COG5083. LUCA.
GeneTreeiENSGT00390000011286.
HOGENOMiHOG000230954.
HOVERGENiHBG052338.
InParanoidiQ99PI5.
KOiK15728.
OrthoDBiEOG7QZG8X.

Enzyme and pathway databases

ReactomeiR-MMU-1483191. Synthesis of PC.
R-MMU-1483213. Synthesis of PE.
R-MMU-75109. Triglyceride Biosynthesis.

Miscellaneous databases

ChiTaRSiLpin2. mouse.
PROiQ99PI5.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PI5.
CleanExiMM_LPIN2.
ExpressionAtlasiQ99PI5. baseline and differential.
GenevisibleiQ99PI5. MM.

Family and domain databases

Gene3Di3.40.50.1000. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR031703. Lipin_mid.
IPR007651. Lipin_N.
IPR013209. LNS2.
IPR031315. LNS2/PITP.
IPR026744. LPIN2.
[Graphical view]
PANTHERiPTHR12181:SF11. PTHR12181:SF11. 1 hit.
PfamiPF16876. Lipin_mid. 1 hit.
PF04571. Lipin_N. 1 hit.
PF08235. LNS2. 1 hit.
[Graphical view]
SMARTiSM00775. LNS2. 1 hit.
[Graphical view]
SUPFAMiSSF56784. SSF56784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Lipodystrophy in the fld mouse results from mutation of a new gene encoding a nuclear protein, lipin."
    Peterfy M., Phan J., Xu P., Reue K.
    Nat. Genet. 27:121-124(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-276 AND 659-893 (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Cecum and Liver.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: FVB/N.
    Tissue: Liver.
  4. "Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns."
    Donkor J., Sariahmetoglu M., Dewald J., Brindley D.N., Reue K.
    J. Biol. Chem. 282:3450-3457(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-186 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. "Lipin 2 is a liver-enriched phosphatidate phosphohydrolase enzyme that is dynamically regulated by fasting and obesity in mice."
    Gropler M.C., Harris T.E., Hall A.M., Wolins N.E., Gross R.W., Han X., Chen Z., Finck B.N.
    J. Biol. Chem. 284:6763-6772(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, PHOSPHORYLATION AT SER-106, INDUCTION.
  7. "A conserved serine residue is required for the phosphatidate phosphatase activity but not the transcriptional coactivator functions of lipin-1 and lipin-2."
    Donkor J., Zhang P., Wong S., O'Loughlin L., Dewald J., Kok B.P., Brindley D.N., Reue K.
    J. Biol. Chem. 284:29968-29978(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, FUNCTION, TISSUE SPECIFICITY, INDUCTION, MUTAGENESIS OF SER-731.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-186 AND SER-187, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Kidney, Liver, Lung, Spleen and Testis.

Entry informationi

Entry nameiLPIN2_MOUSE
AccessioniPrimary (citable) accession number: Q99PI5
Secondary accession number(s): Q8C357
, Q8C7I8, Q8CC85, Q8CHR7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: May 24, 2004
Last modified: June 8, 2016
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.