Any feedback?
Literature summary extracted from
- Lipins, lipids and nuclear envelope structure (2009), Traffic, 10, 1181-1187.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.3.4 | Pah1p/Smp2p | Saccharomyces cerevisiae |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | G84R | causes lipodystrophy. Mutated residue is a conserved glycine in the N-LIP domain required for enzymatic activity | Mus musculus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.3.4 | Insulin | phosphorylation inhibits activity, lipin 1 is phosphorylated in response to insulin treatment in adipocytes in an mTOR-dependent manner | Rattus norvegicus | |
| 3.1.3.4 | additional information | phosphorylation inhibits activity, phosphorylation of lipin 1 on multiple sites correlates with a decrease of its microsomal-bound pool | Mus musculus | |
| 3.1.3.4 | additional information | phosphorylation of Pah1p inhibits its PAP1 activity. Pah1p is phosphorylated in vivo on at least 12 sites, including seven Ser/Thr-Pro (S/T-P) motifs. Pah1p is phosphorylated in mitotic cells in a Cdk1/Cdc28p-dependent manner. Mutations in the Nem1p-Spo7p complex result in hyperphosphorylation of Pah1p | Saccharomyces cerevisiae |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.1.3.4 | cytoplasm | translocates onto the cytosolic side of intracellular membranes | Saccharomyces cerevisiae | 5737 | - |
| 3.1.3.4 | soluble | - |
Saccharomyces cerevisiae | - |
- |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.3.4 | Mus musculus | - |
- |
- |
| 3.1.3.4 | Rattus norvegicus | - |
- |
- |
| 3.1.3.4 | Saccharomyces cerevisiae | - |
- |
- |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.1.3.4 | adipocyte | - |
Mus musculus | - |
| 3.1.3.4 | adipocyte | - |
Rattus norvegicus | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.3.4 | phosphatidic acid + H2O | - |
Mus musculus | 1,2-diacyl-sn-glycerol + phosphate | - |
? |  |
| 3.1.3.4 | phosphatidic acid + H2O | - |
Rattus norvegicus | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
| 3.1.3.4 | phosphatidic acid + H2O | Pah1p also uses phosphatidic acid to produce phosphatidylethanolamine and phosphatidylcholine through a second parallel route, the cytidine diphosphate diacylglycerol pathway | Saccharomyces cerevisiae | 1,2-diacyl-sn-glycerol + phosphate | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | lipin | - |
Saccharomyces cerevisiae |
| 3.1.3.4 | lipin 1 | - |
Mus musculus |
| 3.1.3.4 | lipin 1 | - |
Rattus norvegicus |
| 3.1.3.4 | Mg2+-dependent phosphatidate phosphatase | - |
Saccharomyces cerevisiae |
| 3.1.3.4 | Pah1p | - |
Saccharomyces cerevisiae |
| 3.1.3.4 | Pah1p/Smp2p | - |
Saccharomyces cerevisiae |
| 3.1.3.4 | PAP1 | - |
Saccharomyces cerevisiae |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.1.3.4 | malfunction | deletion of PAH1 leads to the accumulation of phosphatidic acid but also the concomitant reduction of 1,2-diacyl-sn-glycerol and triacylglycerol levels and changes in phosphatidylethanolamine and phosphatidylcholine amounts. Mammalian lipins can rescue the yeast pah1DELTA mutant. A septuple S/T-P Pah1p phosphorylation null mutant displays higher specific activity when compared to the wild-type enzyme. Mutations in Pah1p result in transcriptional derepression of UAS(INO)-containing genes. Overexpression of the more active septuple S/T-P Pah1p phosphorylation null mutant causes inositol auxotrophy, which can be rescued by the deletion of the Opi1p repressor. Pah1DELtAopi1DELTA double mutant exhibits a synergistic effect on the transcriptional derepression of two UAS(INO)-containing genes, INO1 and OPI3. PAH1 mutants display irregularly shaped nuclei with long stacks of membranes that contain nuclear pores and appear to be in contact with the nuclear envelope. Inactivation of the phosphatidic acid signals downstream of Pah1p by either deleting the transcriptional activator Ino2p or overexpressing the repressor Opi1p, can restore normal nuclear shape in nem1DELTA spo7DELTA or pah1DELTA deletion mutants | Saccharomyces cerevisiae |
| 3.1.3.4 | malfunction | lipin 1 gene is mutated in the fatty liver dystrophy mouse, which displays features of generalized lipodystrophy, characterized by significant reduction in the adipose tissue mass and in the cellular lipid droplet content | Mus musculus |
| 3.1.3.4 | physiological function | has essential roles in lipid droplet and phospholipid metabolism | Mus musculus |
| 3.1.3.4 | physiological function | has essential roles in lipid droplet and phospholipid metabolism. Pah1p and its regulators are required for the maintenance of a spherical nuclear shape. Pah1p carries an acidic stretch at the C-terminal end. PAH1/SMP2 are independently identified as a dosage suppressor of the spo7DELTA and nem1DELTA deletions. Pah1p has a key signalling function in the transcriptional regulation of genes encoding phospholipid biosynthetic enzymes. Pah1p may have roles in the biogenesis of membrane-bound organelles | Saccharomyces cerevisiae |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
