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Information on EC 3.1.3.4 - phosphatidate phosphatase and Organism(s) Homo sapiens and UniProt Accession Q92539

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.4 phosphatidate phosphatase
IUBMB Comments
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
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UNIPROT: Q92539 not found.
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
phosphatidate phosphohydrolase, lipin-1, lpin1, pap-1, lipin1, phosphatidate phosphatase, lipin 1, prg-1, phosphatidic acid phosphohydrolase, pa phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3-sn-phosphatidate phosphohydrolase
-
-
acid phosphatidyl phosphatase
-
-
-
-
ecto-PAPase
-
-
-
-
ecto-phosphatidic acid phosphohydrolase
-
-
-
-
Germ cell guidance factor
-
-
-
-
lipid phosphate phosphatase
lipid phosphate phosphatase 1
-
-
lipid phosphate phosphatase 3
lipid phosphate phosphatase-1
-
-
lipid phosphate phosphatase-2
-
-
lipid phosphate phosphatase-3
-
-
lipid phosphate phosphatase-related protein type 1
-
lipid phosphate phosphatase-related protein type 2
-
lipid phosphate phosphatase-related protein type 3
-
lipid phosphate phosphatase-related protein type 4
-
lipid phosphate phosphohydrolase
-
-
lipidphosphatase-related protein 1
-
lipin 1
lipin 1beta
-
-
lipin-1
lipin-1alpha
-
isoform
lipin-1beta
-
isoform
lipin-1gamma
-
isoform
lipin-3
-
-
Lipin1
-
-
Mg2+-dependent phosphatidate phosphatase
-
-
PA phosphatase
PA-P
-
-
PA-PSP
-
-
PAP-2
-
-
PAP-2b
-
-
PAP2a
-
-
phosphatidate phosphatase
phosphatidate phosphatase-1
-
-
phosphatidate phosphohydrolase
-
-
-
-
phosphatidic acid phosphatase
phosphatidic acid phosphatase 2a
-
-
phosphatidic acid phosphatase type 2
-
phosphatidic acid phosphatase-1
-
-
phosphatidic acid phosphohydrolase
-
-
-
-
phosphatidic acid phosphohydrolase-1
-
-
plasticity related gene 1
-
plasticity related gene 3
-
plasticity related gene 4
-
presqualene diphosphate phosphatase
-
-
PRG-1
type 2b phosphatidic acid phosphatase
-
-
Wunen protein
-
-
-
-
additional information
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
diacylglycerol-3-phosphate phosphohydrolase
This enzyme catalyses the Mg2+-dependent dephosphorylation of a 1,2-diacylglycerol-3-phosphate, yielding a 1,2-diacyl-sn-glycerol (DAG), the substrate for de novo lipid synthesis via the Kennedy pathway and for the synthesis of triacylglycerol. In lipid signalling, the enzyme generates a pool of DAG to be used for protein kinase C activation. The mammalian enzymes are known as lipins.
CAS REGISTRY NUMBER
COMMENTARY hide
9025-77-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycero-3-phosphate + H2O
2-(4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-pentanoyl)-1-hexadecanoyl-sn-glycerol + phosphate
show the reaction diagram
-
fluorescent substrate deirvative
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
ceramide 1-phosphate + H2O
ceramide + phosphate
show the reaction diagram
ceramide-1-phosphate + H2O
?
show the reaction diagram
-
isoenzyme PAP-2a and PAP-2b
-
-
?
diacylglycerol diphosphate + H2O
?
show the reaction diagram
didecanoyl phosphatidic acid + H2O
1,2-didecanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dihexanoyl phosphatidic acid + H2O
1,2-dihexanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dihydro-sphingosine-1-phosphate + H2O
dihydro-sphingosine + phosphate
show the reaction diagram
-
all LPPs
-
-
?
dimyristoyl phosphatidic acid + H2O
1,2-dimyristoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dioctanoyl phosphatidic acid + H2O
1,2-dioctanoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dioleoyl phosphatidic acid + H2O
1,2-dioleoyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
dipalmitoyl phosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
FTY720-phosphate + H2O
FTY720 + phosphate
show the reaction diagram
-
LPP3
-
-
?
lyso-phosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
lysophosphatidate + H2O
?
show the reaction diagram
lysophosphatidic acid + H2O
?
show the reaction diagram
-
-
-
?
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
octanoyl lysophosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
oleoyl phosphatidic acid + H2O
?
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
phosphatidic acid + H2O
diacylglycerol + phosphate
show the reaction diagram
sphingosine 1-phosphate + H2O
?
show the reaction diagram
-
hydrolysis by isoenzyme PAP-2b, no hydrolysis by isoenzyme PAP-2a
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
sphingosine-1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-diacylglycerol 3-phosphate + H2O
1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
-
-
-
-
?
a 3-sn-phosphatidate + H2O
a 1,2-diacyl-sn-glycerol + phosphate
show the reaction diagram
lysophosphatidic acid + H2O
monoacylglycerol + phosphate
show the reaction diagram
phosphatidic acid + H2O
1,2-diacylglycerol + phosphate
show the reaction diagram
-
-
-
-
?
sphingosine 1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
sphingosine-1-phosphate + H2O
sphingosine + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
bromoenol lactone
dihydrosphingosine
-
-
dimethylsphingosine
-
-
ethanol
-
inhibition of PAP-1
Mg2+
-
MgCl2
N-ethylmaleimide
-
-
phosphatidic acid
-
competitive inhibition
propanolol
propranolol
RNAi2
reduces expression levels of LPR1 by ca. 60% in SK-OV-3 cells
-
siRNA
-
rat2 fibroblasts treated with siRNA for LPP2 show a ca. 60% decrease in mRNA for the targeted LPP
-
sphingosine
-
-
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
androgen
-
highly induces LPP1 expression in LNCaP cells
-
methyltrienolone
-
induces LPP1 expression
Triton X-100
-
plasma membrane-associated activity is absolutely dependent on detergent
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.041 - 0.104
diacylglycerol diphosphate
1.4
dioctanoyl phosphatidic acid
-
-
0.295 - 0.58
lysophosphatidic acid
0.062 - 0.506
phosphatidic acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00035
-
LPP3 activity against FTY720-P
0.00285
-
LPP3 activity against sphingosine 1-phosphate
0.1175
-
-
additional information
-
development of a HPLC-fluorescence detection method, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
assay at
7.4
assay at
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
synovium containing, specific expression of DPPL2
Manually annotated by BRENDA team
specific expression of DPPL2, expression in endothelial cell lines, overview
Manually annotated by BRENDA team
-
isozyme LPP3
Manually annotated by BRENDA team
-
U937, THP-1 and MonoMac
Manually annotated by BRENDA team
specific expression of DPPL2
Manually annotated by BRENDA team
specific expression of DPPL2
Manually annotated by BRENDA team
-
promonocytic leukemia macrophage cell line
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme active site exposed to the cytosolic side of the membrane
Manually annotated by BRENDA team
-
early stage, wild-type and mutant
Manually annotated by BRENDA team
-
CHAPS-resistant complexes containing LPP1
Manually annotated by BRENDA team
-
lipin-1gamma partially translocates from subcellular membranes to lipid droplets upon fatty acid loading
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
isoform lipin-1 binds to serine/threonine protein phosphatase-1 catalytic subunit through a HVRF binding motif. Mutating the HVRF motif in the highly conserved N terminus of lipin-1 greatly decreases serine/threonine protein phosphatase-1 catalytic subunit interaction. Mutations of other residues in the N terminus of lipin-1 also modulate serine/threonine protein phosphatase-1 catalytic subunit binding. Serine/threonine protein phosphatase-1 catalytic subuni binds poorly to a phosphomimetic mutant of lipin-1 andbinds well to the non-phosphorylatable lipin-1 mutant. Mutating the HVRFmotif also abrogates the nuclear translocation and phosphatidate phosphatase activity of lipin-1
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
LPIN1_HUMAN
890
0
98664
Swiss-Prot
other Location (Reliability: 3)
LPIN2_HUMAN
896
0
99399
Swiss-Prot
other Location (Reliability: 3)
LPIN3_HUMAN
851
0
93614
Swiss-Prot
other Location (Reliability: 2)
PLPP1_HUMAN
284
6
32156
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLPP2_HUMAN
288
6
32574
Swiss-Prot
Secretory Pathway (Reliability: 1)
PLPP3_HUMAN
311
6
35116
Swiss-Prot
other Location (Reliability: 4)
PLPP4_HUMAN
271
6
30395
Swiss-Prot
Secretory Pathway (Reliability: 2)
PLPP5_HUMAN
264
6
29484
Swiss-Prot
Secretory Pathway (Reliability: 2)
A0A024QZU7_HUMAN
285
5
32150
TrEMBL
Secretory Pathway (Reliability: 1)
A0A024QZS3_HUMAN
284
6
32156
TrEMBL
Secretory Pathway (Reliability: 1)
PLPR5_HUMAN
321
0
35427
Swiss-Prot
-
PLPR3_HUMAN
718
0
76037
Swiss-Prot
-
PLPR4_HUMAN
763
0
82983
Swiss-Prot
-
PLPR1_HUMAN
325
0
35795
Swiss-Prot
-
PLPR2_HUMAN
343
0
36880
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32000
-
x * 33000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP2. x * 32000 + x * 34000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP3
32158
-
x * 32158, isoenzyme PAP-2a, calculation from nucleotide sequence
32400
-
x * 32400, recombinant PA-PSP, SDS-PAGE
33000
-
x * 33000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP2. x * 32000 + x * 34000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP3
34000
-
x * 33000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP2. x * 32000 + x * 34000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP3
35000
LPR1, Western blot analysis
35119
-
x * 35119, isoenzyme PAP-2b, calculation from nucleotide sequence
36000
-
x * 33000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP2. x * 32000 + x * 34000 + x * 36000, SDS-PAGE, FLAG-tagged and Myc-tagged LPP3
38000
LPR1, Western blot analysis
60000
-
immunoprecipitation, band only visible at mRNA overexpression levels of 100fold or more
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
homodimer
hexamer
-
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
sumoylation
-
isoforms lipin-1alpha and lipin-1beta undergo sumoylation on two consensus sumoylation sites
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D712E/D714E
catalytically inactive. Mutant binds to serine/threonine protein phosphatase-1 catalytic subunit to the same extent as wild-type
F87A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
I67A/I69A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to a decrase in binding to serine/threonine protein phosphatase-1 catalytic subunit
L58A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
L80A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation leads to n intermediate phenotype in binding to serine/threonine protein phosphatase-1 catalytic subunit
R127K/H223L
-
negligible LPP1 activity, although each mutant is still able to form oligomers
R214K
S734L
-
Majeed mutation in lipin-2, which alters a serine residue that is located in the C-LIP domain downstream of the enzyme active site and coactivator motifs. Mutation completely abolishes PAP activity in both lipin-1 and lipin-2 backgrounds
V57A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
V64A
mutant based on non-phosphorylatable mutant, in which 21 serine/threonine residues are mutated to alanine. The additional mutation does not affect binding to serine/threonine protein phosphatase-1 catalytic subunit
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged lipin from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant LPP3 from Drosophila melanogaster cells S2 by immunoaffinity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of two Mg2+-independent isoenzymes, PAP-2a and PAP-2b
-
co-overexpression of lipin with murine LPP-1 in Escherichia coli strain BL21(DE3) as His-tagged enzymes
-
expressed either as untagged proteins or as Flag- or EGFP-tagged enzymes in HUVEC cells or in HEK-293 cells
-
expressed in HEK293 cells as a green fluorescent fusion protein
-
expressed in P-388D1 cells
-
expression in HEK-293 cell
expression of hemagglutinin epitope-tagged phosphatidic acid phosphohydrolase PAP-2a, PAP-2b and PAP-2c in HEK293 cells. Expression of phosphatidic acid phosphohydrolase PAP-2a, PAP-2b and PAP-2c in baculovirus-infected Sf9 insect cells. Expression of PAP-2a but not PAP-2b or PAP-2c results in high levels of cell surface PAP activity in intact insect cells
-
expression of isozyme DPPL1 in Spodoptera frugiperda Sf9 cells
expression of isozyme DPPL2 in Spodoptera frugiperda Sf9 cells
expression of lipin-1 in HeLa M cells
expression of PAP2a in Saos-2 cells, promoter determination and anaylsis, expression in HEK-293T cells, expression regulation anaylsis, overview
-
expression of presqualene diphosphate phosphatase in COS-7 cells, co-expression with CTP:phosphocholine cytidylyltransferase-alpha
-
full-length cDNAs for human lipin-1 transferred to the pCMV/V5-DEST vector. Plasmid DNA transformed and amplified using DH5alpha bacteria, and transfection of L6 myocytes
-
functional overexpression of GFP-tagged LPPs in rat2 fibroblasts, the transformed cells show reduced proliferation, overview
-
gene LPIN2 is located on chromosome 18p11
-
LPIN1 reporter plasmid transiently transfected into Hep-G2 cells
-
LPP1 and LPR1 expressed in Sf9 cells using a baculovirus vector. Recombinant LPR1 and mutants incorporating a C-terminal EGFP tag expressed in HeLa and COS7 cells. Overexpression of EGFP-LPR1 in SK-OV-3 cells
LPP1, LPP2 and LPP3
-
LPP2 and LPP3 inserted into vector pcDNA3.1 with a C-terminal Myc epitope tag or FLAG epitope tag and transiently transfected into HEK-293 cells
-
NIH3T3 cells stably expressing LPP1-CFP or LPP3-CFP. MDCK cells stably expressing LPP1-GFP and LPP3-GFP. COS-7 and PC-12 cells transiently expressing LPP1
-
overexpression of LPP-3 in HEK293 cells and in Xenopus laevis dorsal blastomeres of embryos causing a mild ventralizing effect
overexpression of LPP3 and LPP2 in HEK-293 cells, LPP2 and LPP3 are constitutively co-localized with sphingosine kinase 1, SK1, in cytoplasmic vesicles in HEK-293 cells, LPP2, not LPP3, prevents SK1 from being recruited to the perinuclear space upon induction of phospholipase D1
-
overexpression of LPPs in HEK293 cells, expression of LPP3 in Drosophila melanogaster cells S2
-
rat2 fibroblasts transduced and overexpressed with LPP2, LPP2-GFP and mutant LPP2(R214K)-GFP
-
separate overexpression of isozymes LPP1, LPP2, or LPP3 in HEK-293 cells reducing lysophosphatidic acid-stimulated p42/p44 MAPK activation
-
transcript PAP2d_v1, cDNA library construction, DNA and amino acid sequence determination and analysis, genomic localization of the two splicing variants, expression patterns, expression in Escherichia coli strain DH5alpha
transcript PAP2d_v2, cDNA library construction, DNA and amino acid sequence determination and analysis, genomic localization of the two splicing variants, expression patterns, expression in Escherichia coli strain DH5alpha
transient and stable overexpression in HEK-293 cells, baculovirus vectors for recombinant expression of LPPs in cultured Sf9 cells
-
wild-type and mutant LPP1, LPP2, and LPP3 cDNAs subcloned into the pLNCX2 retroviral vector directly downstream of the human cytomegalovirus immediate-early promoter. Constructs transfected inot human dermal microvascular endothelial cells. HA-tagged wild-type LPP3 (pLNCX2-HA-WT-hLPP3) stably transfected into HEK-293 cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
epidermal growth factor increases LPP3 mRNA in HeLa cells. Androgen increases LPP1 mRNA in adenocarcinoma cells
-
expression of lipin 1beta in viscera adipose tissue does not correlate with PPARG, LPL, LIPE, adiponectin and SLC2A4 gene expression
-
hepatic lipin-1 expression is selectively repressed by insulin
-
hepatic lipin-1 expression is selectively stimulated by glucocorticoids. The expression of lipin-1 is markedly up-regulated under stress conditions
-
in polycystic ovary syndrome patients, lipin 1beta expression in subcutaneous and visceral adipose tissue depots is lower than in controls. In polycystic ovary syndrome patients, visceral adipose lipin 1beta expression correlates negatively with homeostasis model assessment-insulin resistance, body mass index and waist circumference. Subcutaneous lipin 1beta expression in polycystic ovary syndrome patients correlates negatively with body mass index, waist circumference and plasma triglycerides
-
lipin-1 gene expression is regulated in a glucocorticoid receptor-dependent manner
-
lipin1 is induced in the late stages of adipocyte differentiation. During the maturation of adipocytes, the increase of lipin1alpha is less than that of lipin1beta. CCAAT/enhancer-binding protein alpha directly controls the expression of lipin1, overexpression of CCAAT/enhancer-binding protein alpha activates the lipin1 promoter (from nt -1340 to -524) about 6fold over the basal activity in a transient transfection assay
-
LPIN1 mRNA does not change in cells transfected with SREBP-2 siRNA. Both the sterol regulatory element and the nuclear factor Y-binding site are important in the regulation of LPIN1 transcription
-
LPIN1 mRNA levels decrease significantly after transfection with LPIN1 siRNA. LPIN1 mRNA levels are reduced to ca. 0.6fold after transfection with SREBP-1 siRNA
-
LPP3 expression is negatively correlated with vascular endothelial growth factor expression
positive correlation between lipin-1 expression levels in adipose tissue and insulin sensitivity in obese subjects with normal or impaired glucose tolerance and in healthy young men. Lipin-1 expression is induced in adipocytes by insulin-sensitizing drugs such as thiazolidinediones and harmine. Lipin-2 expression in human adipose tissue
-
sterol regulatory element-binding protein 1 (SREBP-1) and nuclear factor Y are necessary for the activation of LPIN1 transcription. Induction of the LPIN1 gene by sterol depletion. The region between nucleotides -2428 and -2378 of the LPIN1 promoter contains sequences that mediate the induction of LPIN1 by sterol depletion. LPIN1 mRNA levels are induced 3.3fold in lipoprotein-deficient serum medium relative to those in sterol-containing medium. In statin-containing medium, LPIN1 mRNA increases 7.2fold
-
subcutaneous lipin 1beta expression in polycystic ovary syndrome patients correlates positively with high density lipoprotein-cholesterol. Expression of lipin 1beta in subcutaneous adipose tissue correlates positively with PPARG, LPL, LIPE, adiponectin and SLC2A4 gene expression
-
total lipin-1 mRNA expression is significantly induced by dexamethasone in human preadipocytes and differentiated adipocytes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
radiolabeled and fluorescent lipid substrates for the detection, quantitation and analysis of the enzymatic activities of the LPPs measured using intact or broken cell preparations as the source of enzyme
medicine
-
LPP3 acts as an ecto-phosphatase that contributes to the equilibration between FTY720 and FTY720-P in vivo
additional information
-
increasing LPP2 activity causes premature entry into S-phase, premature cyclin A expression and decreased rates of proliferation at high passage and accumulation in G2/M. Cells transduced with LPP2 activate the G2/M checkpoint and show characteristics of senescence at high passage
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Roberts, R.; Sciorra, V.A.; Morris, A.J.
Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform
J. Biol. Chem.
273
22059-22067
1998
Homo sapiens
Manually annotated by BRENDA team
Balboa, M.A.; Balsinde, J.; Dennis, E.A.
Involvement of phosphatidate phosphohydrolase in arachidonic acid mobilization in human amniotic WISH cells
J. Biol. Chem.
273
7684-7690
1998
Homo sapiens
Manually annotated by BRENDA team
Kai, M.; Wada, I.; Imai, S.; Sakane, F.; Kanoh, H.
Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase
J. Biol. Chem.
272
24572-24578
1997
Homo sapiens
Manually annotated by BRENDA team
Taylor, G.S.; Ladd, A.; James, J.; Greene, B.; English, D.
Characterization of phosphatidic acid phosphohydrolase in neutrophil subcellular fractions
Biochim. Biophys. Acta
1175
219-224
1993
Homo sapiens
Manually annotated by BRENDA team
Day, C.P.; Burt, A.D.; Brown, A.S.M.; Bennett, M.K.; Farrell, D.J.; James, O.F.W.; Yeaman, S.J.
Plasma membrane form of phosphatidate phosphohydrolase: a possible role in signal transduction during liver fibrogenesis
Clin. Sci.
85
281-287
1993
Homo sapiens
Manually annotated by BRENDA team
English, D.; Martin, M.; Harvea, K.A.; Akard, L.P.; Allen, R.; Widlanski, T.S.; Garcia, J.G.; Siddiqui, R.A.
Characterization and purification of neutrophil ecto-phosphatidic acid phosphohydrolase
Biochem. J.
324
941-950
1997
Homo sapiens
-
Manually annotated by BRENDA team
Ishikawa, T.; Kai, M.; Wada, I.; Kanoh, H.
Cell surface activities of the human type 2b phosphatidic acid phosphatase
J. Biochem.
127
645-651
2000
Homo sapiens
Manually annotated by BRENDA team
Fuentes, L.; Perez, R.; Nieto, M.L.; Balsinde, J.; Balboa, M.A.
Bromoenol lactone promotes cell death by a mechanism involving phosphatidate phosphohydrolase-1 rather than calcium-independent phospholipase A2
J. Biol. Chem.
278
44683-44690
2003
Homo sapiens
Manually annotated by BRENDA team
Long, J.; Darroch, P.; Wan, K.F.; Kong, K.C.; Ktistakis, N.; Pyne, N.J.; Pyne, S.
Regulation of cell survival by lipid phosphate phosphatases involves the modulation of intracellular phosphatidic acid and sphingosine 1-phosphate pools
Biochem. J.
391
25-32
2005
Homo sapiens
Manually annotated by BRENDA team
Pyne, S.; Long, J.S.; Ktistakis, N.T.; Pyne, N.J.
Lipid phosphate phosphatases and lipid phosphate signalling
Biochem. Soc. Trans.
33
1370-1374
2005
Canis lupus familiaris, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Han, G.S.; Wu, W.I.; Carman, G.M.
The Saccharomyces cerevisiae lipin homologue is a Mg2+-dependent phosphatidate phosphatase enzyme
J. Biol. Chem.
281
9210-9218
2006
Saccharomyces cerevisiae, Homo sapiens
Manually annotated by BRENDA team
Brindley, D.N.
Lipid phosphate phosphatases and related proteins: signaling functions in development, cell division, and cancer
J. Cell. Biochem.
92
900-912
2004
Drosophila melanogaster, Mus musculus, Rattus norvegicus, Homo sapiens (Q6T4P5), Homo sapiens (Q7Z2D5), Homo sapiens (Q8TBJ4), Homo sapiens (Q96GM1)
Manually annotated by BRENDA team
Sun, L.; Gu, S.; Sun, Y.; Zheng, D.; Wu, Q.; Li, X.; Dai, J.; Ji, C.; Xie, Y.; Mao, Y.
Cloning and characterization of a novel human phosphatidic acid phosphatase type 2, PAP2d, with two different transcripts PAP2d_v1 and PAP2d_v2
Mol. Cell. Biochem.
272
91-96
2005
Homo sapiens, Homo sapiens (Q32ZL2)
Manually annotated by BRENDA team
Pyne, S.; Kong, K.C.; Darroch, P.I.
Lysophosphatidic acid and sphingosine 1-phosphate biology: the role of lipid phosphate phosphatases
Semin. Cell Dev. Biol.
15
491-501
2004
Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Burgdorf, C.; Prey, A.; Richardt, G.; Kurz, T.
A HPLC-fluorescence detection method for determination of phosphatidic acid phosphohydrolase activity: application in human myocardium
Anal. Biochem.
374
291-297
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ishida, T.; Iwai, A.; Hijikata, M.; Shimotohno, K.
The expression of phosphatidic acid phosphatase 2a, which hydrolyzes lipids to generate diacylglycerol, is regulated by p73, a member of the p53 family
Biochem. Biophys. Res. Commun.
353
74-79
2007
Homo sapiens
Manually annotated by BRENDA team
Mechtcheriakova, D.; Wlachos, A.; Sobanov, J.; Bornancin, F.; Zlabinger, G.; Baumruker, T.; Billich, A.
FTY720-phosphate is dephosphorylated by lipid phosphate phosphatase 3
FEBS Lett.
581
3063-3068
2007
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Takeuchi, M.; Harigai, M.; Momohara, S.; Ball, E.; Abe, J.; Furuichi, K.; Kamatani, N.
Cloning and characterization of DPPL1 and DPPL2, representatives of a novel type of mammalian phosphatidate phosphatase
Gene
399
174-180
2007
Homo sapiens (Q5VZY2), Homo sapiens (Q8NEB5)
Manually annotated by BRENDA team
Kai, M.; Sakane, F.; Jia, Y.; Imai, S.; Yasuda, S.; Kanoh, H.
Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts
J. Biochem.
140
677-686
2006
Homo sapiens
Manually annotated by BRENDA team
Grkovich, A.; Johnson, C.A.; Buczynski, M.W.; Dennis, E.A.
Lipopolysaccharide-induced cyclooxygenase-2 expression in human U937 macrophages is phosphatidic acid phosphohydrolase-1-dependent
J. Biol. Chem.
281
32978-32987
2006
Homo sapiens
Manually annotated by BRENDA team
Morris, K.E.; Schang, L.M.; Brindley, D.N.
Lipid phosphate phosphatase-2 activity regulates S-phase entry of the cell cycle in Rat2 fibroblasts
J. Biol. Chem.
281
9297-9306
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Sigal, Y.J.; Quintero, O.A.; Cheney, R.E.; Morris, A.J.
Cdc42 and ARP2/3-independent regulation of filopodia by an integral membrane lipid-phosphatase-related protein
J. Cell Sci.
120
340-352
2007
Homo sapiens (Q8TBJ4)
Manually annotated by BRENDA team
Albert, D.; Pergola, C.; Koeberle, A.; Dodt, G.; Steinhilber, D.; Werz, O.
The role of diacylglyceride generation by phospholipase D and phosphatidic acid phosphatase in the activation of 5-lipoxygenase in polymorphonuclear leukocytes
J. Leukoc. Biol.
83
1019-1027
2008
Homo sapiens
Manually annotated by BRENDA team
McDermott, M.I.; Sigal, Y.J.; Crump, J.S.; Morris, A.J.
Enzymatic analysis of lipid phosphate phosphatases
Methods
39
169-179
2006
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Long, J.S.; Pyne, N.J.; Pyne, S.
Lipid phosphate phosphatases form homo- and hetero-oligomers: catalytic competency, subcellular distribution and function
Biochem. J.
411
371-377
2008
Cavia porcellus, Cricetulus griseus, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Theofilopoulos, S.; Lykidis, A.; Leondaritis, G.; Mangoura, D.
Novel function of the human presqualene diphosphate phosphatase as a type II phosphatidate phosphatase in phosphatidylcholine and triacylglyceride biosynthesis pathways
Biochim. Biophys. Acta
1781
731-742
2008
Homo sapiens
Manually annotated by BRENDA team
Grimsey, N.; Han, G.S.; OHara, L.; Rochford, J.J.; Carman, G.M.; Siniossoglou, S.
Temporal and spatial regulation of the phosphatidate phosphatases lipin 1 and 2
J. Biol. Chem.
283
29166-29174
2008
Mus musculus, Homo sapiens (Q14693)
Manually annotated by BRENDA team
Carman, G.M.; Han, G.
Phosphatidic acid phosphatase, a key enzyme in the regulation of lipid synthesis
J. Biol. Chem.
284
2593-2597
2009
Saccharomyces cerevisiae, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Reue, K.; Brindley, D.N.
Thematic Review Series: Glycerolipids. Multiple roles for lipins/phosphatidate phosphatase enzymes in lipid metabolism
J. Lipid Res.
49
2493-2503
2008
Saccharomyces cerevisiae, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Ong, K.L.; Leung, R.Y.; Wong, L.Y.; Cherny, S.S.; Sham, P.C.; Lam, T.H.; Lam, K.S.; Cheung, B.M.
Association of a polymorphism in the lipin 1 gene with systolic blood pressure in men
Am. J. Hypertens.
21
539-545
2008
Homo sapiens
Manually annotated by BRENDA team
Higashida, K.; Higuchi, M.; Terada, S.
Potential role of lipin-1 in exercise-induced mitochondrial biogenesis
Biochem. Biophys. Res. Commun.
374
587-591
2008
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Brindley, D.N.; Pilquil, C.; Sariahmetoglu, M.; Reue, K.
Phosphatidate degradation: phosphatidate phosphatases (lipins) and lipid phosphate phosphatases
Biochim. Biophys. Acta
1791
956-961
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Pyne, S.; Lee, S.C.; Long, J.; Pyne, N.J.
Role of sphingosine kinases and lipid phosphate phosphatases in regulating spatial sphingosine 1-phosphate signalling in health and disease
Cell. Signal.
21
14-21
2009
Drosophila melanogaster, Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Mlinar, B.; Pfeifer, M.; Vrtacnik-Bokal, E.; Jensterle, M.; Marc, J.
Decreased lipin 1 beta expression in visceral adipose tissue is associated with insulin resistance in polycystic ovary syndrome
Eur. J. Endocrinol.
159
833-839
2008
Homo sapiens
Manually annotated by BRENDA team
Ishimoto, K.; Nakamura, H.; Tachibana, K.; Yamasaki, D.; Ota, A.; Hirano, K.; Tanaka, T.; Hamakubo, T.; Sakai, J.; Kodama, T.; Doi, T.
Sterol-mediated regulation of human lipin 1 gene expression in hepatoblastoma cells
J. Biol. Chem.
284
22195-22205
2009
Homo sapiens
Manually annotated by BRENDA team
Donkor, J.; Zhang, P.; Wong, S.; OLoughlin, L.; Dewald, J.; Kok, B.P.; Brindley, D.N.; Reue, K.
A conserved serine residue is required for the phosphatidate phosphatase activity but not the transcriptional coactivator functions of lipin-1 and lipin-2
J. Biol. Chem.
284
29968-29978
2009
Homo sapiens, Mus musculus, Mus musculus C57/BL6J
Manually annotated by BRENDA team
Zhang, P.; OLoughlin, L.; Brindley, D.N.; Reue, K.
Regulation of lipin-1 gene expression by glucocorticoids during adipogenesis
J. Lipid Res.
49
1519-1528
2008
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Reue, K.; Dwyer, J.R.
Lipin proteins and metabolic homeostasis
J. Lipid Res.
50 Suppl
S109-S114
2009
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Brindley, D.N.; Pilquil, C.
Lipid phosphate phosphatases and signaling
J. Lipid Res.
50 Suppl
S225-S230
2009
Drosophila melanogaster, Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Humtsoe, J.O.; Liu, M.; Malik, A.B.; Wary, K.K.
Lipid phosphate phosphatase 3 stabilization of beta-catenin induces endothelial cell migration and formation of branching point structures
Mol. Cell. Biol.
30
1593-1606
2010
Homo sapiens, Mus musculus
Manually annotated by BRENDA team
Bou Khalil, M.; Blais, A.; Figeys, D.; Yao, Z.
Lipin - The bridge between hepatic glycerolipid biosynthesis and lipoprotein metabolism
Biochim. Biophys. Acta
1801
1249-1259
2010
Homo sapiens, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Wang, H.; Zhang, J.; Qiu, W.; Han, G.S.; Carman, G.M.; Adeli, K.
Lipin-1gamma isoform is a novel lipid droplet-associated protein highly expressed in the brain
FEBS Lett.
585
1979-1984
2011
Homo sapiens
Manually annotated by BRENDA team
Chatterjee, I.; Humtsoe, J.O.; Kohler, E.E.; Sorio, C.; Wary, K.K.
Lipid phosphate phosphatase-3 regulates tumor growth via beta-catenin and Cyclin-D1 signaling
Mol. Cancer
10
51
2011
Homo sapiens
Manually annotated by BRENDA team
Kok, B.P.; Skene-Arnold, T.D.; Ling, J.; Benesch, M.G.; Dewald, J.; Harris, T.E.; Holmes, C.F.; Brindley, D.N.
Conserved residues in the N terminus of lipin-1 are required for binding to protein phosphatase-1c, nuclear translocation, and phosphatidate phosphatase activity
J. Biol. Chem.
289
10876-10886
2014
Homo sapiens (Q14693)
Manually annotated by BRENDA team
Busnelli, M.; Manzini, S.; Parolini, C.; Escalante-Alcalde, D.; Chiesa, G.
Lipid phosphate phosphatase 3 in vascular pathophysiology
Atherosclerosis
271
156-165
2018
Homo sapiens (O14495), Mus musculus (Q99JY8)
Manually annotated by BRENDA team
Touat-Hamici, Z.; Weidmann, H.; Blum, Y.; Proust, C.; Durand, H.; Iannacci, F.; Codoni, V.; Gaignard, P.; Therond, P.; Civelek, M.; Karabina, S.A.; Lusis, A.J.; Cambien, F.; Ninio, E.
Role of lipid phosphate phosphatase 3 in human aortic endothelial cell function
Cardiovasc. Res.
112
702-713
2016
Homo sapiens (O14495), Homo sapiens
Manually annotated by BRENDA team
Mingorance, L.; Castro, V.; Avila-Perez, G.; Calvo, G.; Rodriguez, M.J.; Carrascosa, J.L.; Perez-Del-Pulgar, S.; Forns, X.; Gastaminza, P.
Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation
PLoS Pathog.
14
e1007284
2018
Homo sapiens
Manually annotated by BRENDA team