BRENDA - Enzyme Database

Lipins, lipids and nuclear envelope structure

Siniossoglou, S.; Traffic 10, 1181-1187 (2009)

Data extracted from this reference:

Cloned(Commentary)
EC Number
Commentary
Organism
3.1.3.4
Pah1p/Smp2p
Saccharomyces cerevisiae
Engineering
EC Number
Amino acid exchange
Commentary
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
Commentary
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
Commentary
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
Primary Accession No. (UniProt)
Commentary
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
Commentary
Organism
Textmining
3.1.3.4
adipocyte
-
Rattus norvegicus
-
3.1.3.4
adipocyte
-
Mus musculus
-
Substrates and Products (Substrate)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
phosphatidic acid + H2O
-
710639
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
710639
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
710639
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
Cloned(Commentary) (protein specific)
EC Number
Commentary
Organism
3.1.3.4
Pah1p/Smp2p
Saccharomyces cerevisiae
Engineering (protein specific)
EC Number
Amino acid exchange
Commentary
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 (protein specific)
EC Number
Inhibitors
Commentary
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 (protein specific)
EC Number
Localization
Commentary
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
-
-
Source Tissue (protein specific)
EC Number
Source Tissue
Commentary
Organism
Textmining
3.1.3.4
adipocyte
-
Rattus norvegicus
-
3.1.3.4
adipocyte
-
Mus musculus
-
Substrates and Products (Substrate) (protein specific)
EC Number
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
3.1.3.4
phosphatidic acid + H2O
-
710639
Mus musculus
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
3.1.3.4
phosphatidic acid + H2O
-
710639
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
710639
Saccharomyces cerevisiae
1,2-diacyl-sn-glycerol + phosphate
-
-
-
?
General Information
EC Number
General Information
Commentary
Organism
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
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
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
General Information (protein specific)
EC Number
General Information
Commentary
Organism
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
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
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