LMPD Database

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LMP006918

UniProt Annotations

Entry Information
Gene Namephosphatidate phosphatase PAH1
Protein EntryPAH1_YEAST
UniProt IDP32567
SpeciesYeast (S288c)
Comments
Comment typeDescription
Catalytic ActivityA 1,2-diacylglycerol 3-phosphate + H(2)O = a 1,2-diacyl-sn-glycerol + phosphate. {ECO:0000269|PubMed:16467296, ECO:0000269|PubMed:17910939, ECO:0000269|PubMed:17971454}.
CofactorName=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16467296};
DomainContains one Asp-Xaa-Asp-Xaa-Thr (DXDXT) motif, a catalytic motif essential for phosphatidate phosphatase activity. {ECO:0000269|PubMed:20876142}.
DomainThe N-terminal amphipathic helix (residues 1 to 18) is involved in the membrane recruitment. {ECO:0000269|PubMed:20876142}.
Enzyme RegulationPhenylglyoxal and propranolol inhibit activity in dose-dependent manners with IC(50) values of 1.3 mM and 0.2 mM, respectively. {ECO:0000269|PubMed:17910939}.
FunctionMg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controles transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation. {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16467296, ECO:0000269|PubMed:16968695, ECO:0000269|PubMed:17910939, ECO:0000269|PubMed:17971454, ECO:0000269|PubMed:20876142, ECO:0000269|PubMed:21081492, ECO:0000269|PubMed:21422231, ECO:0000269|PubMed:8437575}.
MiscellaneousPresent with 3910 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
PtmPhosphorylated by CDC28 at the onset of mitosis, and dephosphorylated by the NEM1-SPO7 complex. Phosphorylation regulates recruitment on promoters of lipid biosynthetic enzymes. {ECO:0000269|PubMed:15889145, ECO:0000269|PubMed:16968695, ECO:0000269|PubMed:17330950, ECO:0000269|PubMed:18407956, ECO:0000269|PubMed:19779198, ECO:0000269|PubMed:20876142, ECO:0000269|PubMed:21081492}.
SimilarityBelongs to the lipin family. {ECO:0000305}.
Subcellular LocationCytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.