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Literature summary extracted from

  • Brindley, D.N.
    Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer (2004), J. Cell. Biochem., 92, 900-912.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.1.3.4 additional information treatment of HeLa cells with the epidermal growth factor leads to 3fold increased LPP-3 expression, while LPP-1 expression is unaffected, LPP-1 expression is increased in prostate adenocarcinoma cells treated with androgens Homo sapiens

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.3.4 overexpression of LPP-3 in HEK293 cells and in Xenopus laevis dorsal blastomeres of embryos causing a mild ventralizing effect Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
3.1.3.4 additional information construction of several mouse models overexpressing or lacking LPP isozymes, e.g. overexpression of LPP-1 leads to defects in fertility in female mice and to increased accumulation of diacylglycerol, LPP-2 knockout mice are fertile and viable, whereas LPP-3 knockout mice show a severe phenotype failing to form a chorio-allantoic placenta and yolk sac vasculature, in addition, mutant embryos show a shortening of the anterior-posterior axis, overview, introduction of LPP-1 into Drosophila melanogaster germ cells has no effect on the germ-cell-specific factor in vivo Mus musculus
3.1.3.4 additional information introduction of LPP-3 into Drosophila melanogaster germ cells causes aberrant migration and germ cell death Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.3.4 additional information the enzymes act intra- and extracellularly Drosophila melanogaster
-
-
3.1.3.4 additional information the enzymes act intra- and extracellularly Mus musculus
-
-
3.1.3.4 additional information the enzymes act intra- and extracellularly Rattus norvegicus
-
-
3.1.3.4 additional information the enzymes act intra- and extracellularly Homo sapiens
-
-
3.1.3.4 plasma membrane
-
 Mus musculus 5886
-
3.1.3.4 plasma membrane
-
 Rattus norvegicus 5886
-
3.1.3.4 plasma membrane isozyme LPP-1, containing the apical sorting signal FDKTRL, is mainly located at the apical surface membrane, while isozyme LPP-3 is located at the basolateral membrane being targeted by the dityrosine motif in the second cytoplasmic portion Homo sapiens 5886
-
3.1.3.4 plasma membrane the isozyme LPP-1 is partly expressed in the plama membrane with its C-terminal end located on the cell surface Drosophila melanogaster 5886
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.1.3.4 lysophosphatidic acid + H2O Drosophila melanogaster
-
 monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O Mus musculus
-
 monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O Rattus norvegicus
-
 monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O Homo sapiens
-
 monoacylglycerol + phosphate
-
 ?
3.1.3.4 additional information Homo sapiens LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview ?
-
 ?
3.1.3.4 additional information Mus musculus LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview ?
-
 ?
3.1.3.4 additional information Rattus norvegicus LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview ?
-
 ?
3.1.3.4 additional information Homo sapiens LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview ?
-
 ?
3.1.3.4 additional information Drosophila melanogaster LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, Wunen and Wunen2 are essential for germ cell development, overview ?
-
 ?
3.1.3.4 additional information Homo sapiens LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview ?
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O Drosophila melanogaster
-
 sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O Mus musculus
-
 sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O Rattus norvegicus
-
 sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O Homo sapiens
-
 sphingosine + phosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.4 Drosophila melanogaster
-
 genes Wun and Wun2
-
3.1.3.4 Homo sapiens Q6T4P5 LPR-3; LPR-3
-
3.1.3.4 Homo sapiens Q7Z2D5 PRG-1 or LPR-4; PRG-1 or LPR-4
-
3.1.3.4 Homo sapiens Q8TBJ4 PRG-3 or LPR-1; isozyme PRG-3 or LPR-1
-
3.1.3.4 Homo sapiens Q96GM1 LPR-2 or PRG-4; PRG-4 or LPR-2
-
3.1.3.4 Mus musculus
-
 several isozymes, e.g. isozyme PAP2A, i.e. LPP-1
-
3.1.3.4 Rattus norvegicus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.3.4 glycoprotein N-glycosylation Drosophila melanogaster
3.1.3.4 glycoprotein N-glycosylation Mus musculus
3.1.3.4 glycoprotein N-glycosylation Rattus norvegicus
3.1.3.4 glycoprotein N-glycosylation Homo sapiens

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.3.4 a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate the active site of plasma membrane LPP-1, LPP-2, and LPP-3 is outside the cell, the conserved phosphatase family amino acids are essential for catalytic activity Drosophila melanogaster
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.4 aorta
-
 Homo sapiens
-
3.1.3.4 bladder
-
 Homo sapiens
-
3.1.3.4 brain
-
 Homo sapiens
-
3.1.3.4 brain LPP-2 predominantly Homo sapiens
-
3.1.3.4 heart
-
 Homo sapiens
-
3.1.3.4 heart LPP-1a predominantly Homo sapiens
-
3.1.3.4 HeLa cell
-
 Homo sapiens
-
3.1.3.4 intestinal mucosa epithelial differentiation of intestinal mucosa leads to increased Dri-42/LPP-3 expression Rattus norvegicus
-
3.1.3.4 kidney
-
 Homo sapiens
-
3.1.3.4 kidney LPP-1 predominantly Homo sapiens
-
3.1.3.4 liver
-
 Homo sapiens
-
3.1.3.4 liver LPP-1 predominantly Homo sapiens
-
3.1.3.4 lung
-
 Homo sapiens
-
3.1.3.4 lung LPP-1 predominantly Homo sapiens
-
3.1.3.4 additional information tissue distribution Homo sapiens
-
3.1.3.4 neuron expression of PRG-1 Homo sapiens
-
3.1.3.4 pancreas
-
 Homo sapiens
-
3.1.3.4 pancreas LPP-2 predominantly Homo sapiens
-
3.1.3.4 placenta
-
 Homo sapiens
-
3.1.3.4 placenta LPP-1 predominantly Homo sapiens
-
3.1.3.4 placenta LPP-2 predominantly Homo sapiens
-
3.1.3.4 prostate adenocarcinoma cell LPP-1 Homo sapiens
-
3.1.3.4 prostate gland
-
 Homo sapiens
-
3.1.3.4 uterus
-
 Homo sapiens
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.4 ceramide 1-phosphate + H2O
-
 Drosophila melanogaster ceramide + phosphate
-
 ?
3.1.3.4 ceramide 1-phosphate + H2O
-
 Mus musculus ceramide + phosphate
-
 ?
3.1.3.4 ceramide 1-phosphate + H2O
-
 Rattus norvegicus ceramide + phosphate
-
 ?
3.1.3.4 ceramide 1-phosphate + H2O
-
 Homo sapiens ceramide + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O
-
 Drosophila melanogaster monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O
-
 Mus musculus monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O
-
 Rattus norvegicus monoacylglycerol + phosphate
-
 ?
3.1.3.4 lysophosphatidic acid + H2O
-
 Homo sapiens monoacylglycerol + phosphate
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, LPP-3 is involved in embryonal axis patterning, overview Homo sapiens ?
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview Mus musculus ?
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview Rattus norvegicus ?
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview Homo sapiens ?
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, Wunen and Wunen2 are essential for germ cell development, overview Drosophila melanogaster ?
-
 ?
3.1.3.4 additional information LPP is involved in regulation of bioactive lipids acting in signalling pathways, thus the enzyme is involved in cell division, cytoskeletal rearrangement, Ca2+ transients, and membrane movement, the enzyme is also able to hydrolyze extracellular substrates, lysophosphatidic acid and sphingosine 1-phosphate, involved in wound repair and tumor growth, overview, expression of PRG-1 in neurons increases extracellular lysophosphatidic acid breakdown and attenuates LPA-induced axonal retraction, metabolism of lysophosphatidic acid and sphingosine 1-phosphate, intra- and extracellular function, overview Homo sapiens ?
-
 ?
3.1.3.4 additional information Wunen does not interact with Wunen2 Drosophila melanogaster ?
-
 ?
3.1.3.4 phosphatidic acid + H2O
-
 Drosophila melanogaster diacylglycerol + phosphate
-
 ?
3.1.3.4 phosphatidic acid + H2O
-
 Mus musculus diacylglycerol + phosphate
-
 ?
3.1.3.4 phosphatidic acid + H2O
-
 Rattus norvegicus diacylglycerol + phosphate
-
 ?
3.1.3.4 phosphatidic acid + H2O
-
 Homo sapiens diacylglycerol + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O
-
 Drosophila melanogaster sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O
-
 Mus musculus sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O
-
 Rattus norvegicus sphingosine + phosphate
-
 ?
3.1.3.4 sphingosine 1-phosphate + H2O
-
 Homo sapiens sphingosine + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.4 More the LPPs contain three conserved active site domains and six conserved transmembrane domains Drosophila melanogaster

Synonyms

EC Number Synonyms Comment Organism
3.1.3.4 Dri-42 i.e. LPP-3 Rattus norvegicus
3.1.3.4 lipid phosphate phosphatase
-
 Drosophila melanogaster
3.1.3.4 lipid phosphate phosphatase
-
 Mus musculus
3.1.3.4 lipid phosphate phosphatase
-
 Rattus norvegicus
3.1.3.4 lipid phosphate phosphatase
-
 Homo sapiens
3.1.3.4 lipid phosphate phosphatase-related protein
-
 Drosophila melanogaster
3.1.3.4 lipid phosphate phosphatase-related protein
-
 Mus musculus
3.1.3.4 lipid phosphate phosphatase-related protein
-
 Rattus norvegicus
3.1.3.4 lipid phosphate phosphatase-related protein type 1
-
 Homo sapiens
3.1.3.4 lipid phosphate phosphatase-related protein type 2
-
 Homo sapiens
3.1.3.4 lipid phosphate phosphatase-related protein type 3
-
 Homo sapiens
3.1.3.4 lipid phosphate phosphatase-related protein type 4
-
 Homo sapiens
3.1.3.4 LPP
-
 Drosophila melanogaster
3.1.3.4 LPP
-
 Mus musculus
3.1.3.4 LPP
-
 Rattus norvegicus
3.1.3.4 LPP
-
 Homo sapiens
3.1.3.4 LPPR2
-
 Homo sapiens
3.1.3.4 LPR
-
 Drosophila melanogaster
3.1.3.4 LPR
-
 Mus musculus
3.1.3.4 LPR
-
 Rattus norvegicus
3.1.3.4 LPR-1
-
 Homo sapiens
3.1.3.4 LPR-2
-
 Homo sapiens
3.1.3.4 LPR-3
-
 Homo sapiens
3.1.3.4 LPR-4
-
 Homo sapiens
3.1.3.4 PAP
-
 Mus musculus
3.1.3.4 plasticity related gene 1
-
 Homo sapiens
3.1.3.4 plasticity related gene 3
-
 Homo sapiens
3.1.3.4 plasticity related gene 4
-
 Homo sapiens
3.1.3.4 PRG-1
-
 Homo sapiens
3.1.3.4 PRG-3
-
 Homo sapiens
3.1.3.4 Wunen
-
 Drosophila melanogaster
3.1.3.4 Wunen2
-
 Drosophila melanogaster