MGP Database

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MGP004603

UniProt Annotations

Entry Information
Gene Namelipin 1
Protein EntryLPIN1_HUMAN
UniProt IDQ14693
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=7; Name=1; Synonyms=Alpha; IsoId=Q14693-1; Sequence=Displayed; Name=2; IsoId=Q14693-2; Sequence=VSP_045533; Note=No experimental confirmation available.; Name=3; Synonyms=Beta; IsoId=Q14693-3; Sequence=VSP_053970; Name=4; Synonyms=Gamma; IsoId=Q14693-4; Sequence=VSP_053971; Name=5; IsoId=Q14693-5; Sequence=VSP_045533, VSP_053970; Note=No experimental confirmation available.; Name=6; IsoId=Q14693-6; Sequence=VSP_045533, VSP_053970, VSP_055361, VSP_055362; Note=No experimental confirmation available.; Name=7; IsoId=Q14693-7; Sequence=VSP_055384, VSP_053970; Note=No experimental confirmation available.;
Biophysicochemical PropertiesKinetic parameters: KM=0.35 mM for phosphatidate (isoform 1); KM=0.24 mM for phosphatidate (isoform 3); KM=0.11 mM for phosphatidate (isoform 4); Temperature dependence: Optimum temperature is 40 degrees Celsius. Thermolabile above 40 degrees Celsius and essentially inactive at 60 degrees Celsius.;
Catalytic ActivityA 1,2-diacylglycerol 3-phosphate + H(2)O = a 1,2-diacyl-sn-glycerol + phosphate.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:20231281}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:20231281}; Note=Mg(2+) and, at a lesser extent, Mn(2+). {ECO:0000269|PubMed:20231281};
DiseaseMyoglobinuria, acute recurrent, autosomal recessive (ARARM) [MIM:268200]: Recurrent myoglobinuria is characterized by recurrent attacks of rhabdomyolysis (necrosis or disintegration of skeletal muscle) associated with muscle pain and weakness and followed by excretion of myoglobin in the urine. Renal failure may occasionally occur. {ECO:0000269|PubMed:18817903}. Note=The disease is caused by mutations affecting the gene represented in this entry.
DomainContains 1 Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity. {ECO:0000250}.
DomainContains one Leu-Xaa-Xaa-Ile-Leu (LXXIL), a transcriptional binding motif, which mediates interaction with PPARA. {ECO:0000250}.
Enzyme RegulationPotently inhibited by sphingolipids, in particular, the sphingoid bases sphinganine and sphingosine and ceramide-1-phosphate. Inhibited by concentrations of Mg(2+) and Mn(2+) above their optimums and by Ca(2+), Zn(2+), N- ethylmaleimide and propranolol. {ECO:0000269|PubMed:20231281}.
FunctionPlays 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/PPARA to modulate lipid metabolism gene expression (By similarity). Is involved in adipocyte differentiation. May also be involved in mitochondrial fission by converting phosphatidic acid to diacylglycerol (By similarity). {ECO:0000250}.
MiscellaneousMay represent a candidate gene for human lipodysytropy syndromes.
PtmPhosphorylated at multiple sites in response to insulin. Phosphorylation is controlled by the mTOR signaling pathway. Phosphorylation is decreased by epinephrine. Phosphorylation may not directly affect the catalytic activity but may regulate the localization. Dephosphorylated by the CTDNEP1-CNEP1R1 complex (By similarity). {ECO:0000250}.
PtmSumoylated. {ECO:0000250}.
Sequence CautionSequence=BAA11505.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=BAG57200.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BAG57885.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; Sequence=BAG57957.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; Sequence=BC018071; Type=Frameshift; Positions=134; Evidence={ECO:0000305};
SimilarityBelongs to the lipin family. {ECO:0000305}.
Subcellular LocationNucleus membrane {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250}.
SubunitInteracts (via LXXIL motif) with PPARA. Interacts with PPARGC1A. Interaction with PPARA and PPARGC1A leads to the formation of a complex that modulates gene transcription. Interacts with MEF2C. {ECO:0000250}.
Tissue SpecificitySpecifically expressed in skeletal muscle. Also abundant in adipose tissue. Lower levels in some portions of the digestive tract. {ECO:0000269|PubMed:17158099, ECO:0000269|PubMed:22134922}.
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