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Protein

Phosphatidate phosphatase LPIN3

Gene

Lpin3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Regulates fatty acid metabolism. Magnesium-dependent phosphatidate phosphatase enzyme which catalyzes the conversion of phosphatidic acid to diacylglycerol during triglyceride, phosphatidylcholine and phosphatidylethanolamine biosynthesis.

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: MGI
  • transcription coactivator activity Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Fatty acid metabolism, Lipid metabolism

Enzyme and pathway databases

ReactomeiR-MMU-1483191. Synthesis of PC.
R-MMU-1483213. Synthesis of PE.

Chemistry

SwissLipidsiSLP:000000603.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphatidate phosphatase LPIN3 (EC:3.1.3.4)
Alternative name(s):
Lipin-3
Gene namesi
Name:Lpin3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1891342. Lpin3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 848848Phosphatidate phosphatase LPIN3PRO_0000209884Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei155 – 1551PhosphoserineBy similarity
Modified residuei156 – 1561PhosphoserineBy similarity
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei460 – 4601PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ99PI4.
MaxQBiQ99PI4.
PaxDbiQ99PI4.
PRIDEiQ99PI4.

PTM databases

iPTMnetiQ99PI4.
PhosphoSiteiQ99PI4.

Expressioni

Tissue specificityi

Significant expression in intestine and other regions of the gastrointestinal tract.1 Publication

Gene expression databases

BgeeiQ99PI4.
CleanExiMM_LPIN3.
ExpressionAtlasiQ99PI4. baseline and differential.
GenevisibleiQ99PI4. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043053.

Structurei

3D structure databases

ProteinModelPortaliQ99PI4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 108108N-LIPBy similarityAdd
BLAST
Regioni587 – 789203C-LIPBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi135 – 14410Nuclear localization signalSequence analysis
Motifi641 – 6455DXDXT motif
Motifi652 – 6565LXXIL 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.
HOVERGENiHBG052338.
InParanoidiQ99PI4.
KOiK15728.
OrthoDBiEOG7QZG8X.
TreeFamiTF314095.

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.
[Graphical view]
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.

Sequencei

Sequence statusi: Complete.

Q99PI4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNYVGQLAET VFGTVKELYR GLNPATLSGG IDVLVVRQRD GSFRCSPFHV
60 70 80 90 100
RFGKLGVLRS REKVVDIEIN GEPVDLHMKL GDSGEAFFVQ ELDSDEEDVP
110 120 130 140 150
PRLCTSPIPW GGLSGFPSDS QIGTASEPEG LVITGRRKRR RRRKPRRREE
160 170 180 190 200
DAVDSSSEEL EAGAESELTL LEKPTPESPS AQEAEEPSSQ PKDIHPYSDG
210 220 230 240 250
ECTPQANLSS GDLMSPKSDS ELELRSLEPS PLRAESHMQW VWGRLPKVAK
260 270 280 290 300
AERPEFSLIL ESMAEAICAL PEEPSPSSSP SEAGVDTLSP PVLHPGVRAD
310 320 330 340 350
TFHPAVEAHC EETAVDSPLA APESKETKTQ NSRGAGHPPA TKSWSWTTPE
360 370 380 390 400
SHTPSGHPQV SRGKGSLKRN QHLGPSDIYL DDLPSLDSEN VALYFPKSEY
410 420 430 440 450
GMGARRWSEP SNQKLLESPN PEHIAECTLD SVDKIELSLC GGLADNRDIS
460 470 480 490 500
LEKFTQHMVS YEDLTKNPGL LDDPNLVVKI NEKHYNWAVA APMILSLQAF
510 520 530 540 550
QKNLPESTVD KLEKEKMPRK GGRWWFSWRR RDFPAEEHSS QREKAATRKQ
560 570 580 590 600
QGEKTEVLSS DDDVPDSPVI LEVPPLPSST PGYVPTYKKS LRLSSDQIRC
610 620 630 640 650
LNLNEGANDV VFSVTTQYQG TCRCKATIYL WNWDDKVVIS DIDGTITKSD
660 670 680 690 700
ALGHILPQLG KDWTHQGITS LYHKIHLNGY KFLYCSARAI GMADLTKGYL
710 720 730 740 750
QWVSEHGCGL PKGPILLSPS SLFSALHREV IEKKPEVFKV ACLSDIQQLF
760 770 780 790 800
LPQRQPFHAA FGNRPNDVFA YRQVGLPESR IFTVNPRGEL IQELIKSHKS
810 820 830 840
TYQRLGEVVE LLFPPVVRGP STDLASPEYS NLSYWRKPLP YVDFEALA
Length:848
Mass (Da):94,316
Last modified:June 1, 2001 - v1
Checksum:iABD92B98EF0D71B2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti833 – 8331S → G in BAC33710 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286724 mRNA. Translation: AAG52762.1.
AK049363 mRNA. Translation: BAC33710.1.
AK163833 mRNA. Translation: BAE37510.1.
CCDSiCCDS16998.1.
RefSeqiNP_001186047.1. NM_001199118.1.
NP_075021.1. NM_022883.3.
UniGeneiMm.292111.

Genome annotation databases

EnsembliENSMUST00000040872; ENSMUSP00000043053; ENSMUSG00000027412.
ENSMUST00000109456; ENSMUSP00000105082; ENSMUSG00000027412.
GeneIDi64899.
KEGGimmu:64899.
UCSCiuc008nrh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF286724 mRNA. Translation: AAG52762.1.
AK049363 mRNA. Translation: BAC33710.1.
AK163833 mRNA. Translation: BAE37510.1.
CCDSiCCDS16998.1.
RefSeqiNP_001186047.1. NM_001199118.1.
NP_075021.1. NM_022883.3.
UniGeneiMm.292111.

3D structure databases

ProteinModelPortaliQ99PI4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000043053.

Chemistry

SwissLipidsiSLP:000000603.

PTM databases

iPTMnetiQ99PI4.
PhosphoSiteiQ99PI4.

Proteomic databases

EPDiQ99PI4.
MaxQBiQ99PI4.
PaxDbiQ99PI4.
PRIDEiQ99PI4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000040872; ENSMUSP00000043053; ENSMUSG00000027412.
ENSMUST00000109456; ENSMUSP00000105082; ENSMUSG00000027412.
GeneIDi64899.
KEGGimmu:64899.
UCSCiuc008nrh.2. mouse.

Organism-specific databases

CTDi64900.
MGIiMGI:1891342. Lpin3.

Phylogenomic databases

eggNOGiKOG2116. Eukaryota.
COG5083. LUCA.
GeneTreeiENSGT00390000011286.
HOVERGENiHBG052338.
InParanoidiQ99PI4.
KOiK15728.
OrthoDBiEOG7QZG8X.
TreeFamiTF314095.

Enzyme and pathway databases

ReactomeiR-MMU-1483191. Synthesis of PC.
R-MMU-1483213. Synthesis of PE.

Miscellaneous databases

ChiTaRSiLpin3. mouse.
PROiQ99PI4.
SOURCEiSearch...

Gene expression databases

BgeeiQ99PI4.
CleanExiMM_LPIN3.
ExpressionAtlasiQ99PI4. baseline and differential.
GenevisibleiQ99PI4. 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.
[Graphical view]
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].
  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].
    Strain: C57BL/6J.
    Tissue: Head.
  3. "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.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Kidney, Pancreas and Testis.

Entry informationi

Entry nameiLPIN3_MOUSE
AccessioniPrimary (citable) accession number: Q99PI4
Secondary accession number(s): Q3TQ75, Q8C7R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 10, 2002
Last sequence update: June 1, 2001
Last modified: July 6, 2016
This is version 101 of the entry and version 1 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.