Plpp1
entrez
19012
canonical
uniprot
Q61469
canonical
ensembl
ENSMUSG00000021759
resolver
ensp
ENSMUSP00000016144
resolver
ensp
ENSMUSP00000064423
resolver
genesymbol
Plpp1
resolver
genesymbol_syn
Hpic53
resolver
genesymbol_syn
Lpp1
resolver
genesymbol_syn
Ppap2a
resolver
uniprot
Q61690
resolver
uniprot
Q6GT30
resolver
uniprot
Q8BPB8
resolver
uniprot_entry
PLPP1_MOUSE
resolver
uniprot_sec
Q61690
resolver
uniprot_sec
Q6GT30
resolver
uniprot_sec
Q8BPB8
resolver
activity_regulation
ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase. Insensitive to N-ethylmaleimide. {ECO:0000250|UniProtKB:O14494}.
uniprot
proteins
amino_acid_sequence
MFDKTRLPYVALDVICVLLAGLPFAILTSRHTPFQRGIFCNDDSIKYPYKEDTIPYALLGGIVIPFCIIVMSIGESLSVYFNVLHSNSFVGNPYIATIYKAVGAFLFGVSASQSLTDIAKYTIGSLRPHFLAICNPDWSKINCSDGYIEDYICQGNEEKVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPMLQFGLIAFSIYVGLSRVSDYKHHWSDVTVGLIQGAAMAILVALYVSDFFKDTHSYKERKEEDPHTTLHETASSRNYSTNHEP
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.1.3.106
uniprot
proteins
ec_number
3.1.3.4
uniprot
proteins
ec_number
3.6.1.75
uniprot
proteins
function
FUNCTION: Magnesium-independent phospholipid phosphatase of the plasma membrane that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, diacylglycerol pyrophosphate/DGPP, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P (PubMed:10359651, PubMed:10620492, PubMed:10818444, PubMed:15461590, PubMed:19215222, PubMed:8702556). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (By similarity). Through its extracellular phosphatase activity allows both the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:17379599). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (PubMed:17379599). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (PubMed:15461590, PubMed:17057224). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (PubMed:17057224). {ECO:0000250|UniProtKB:O14494, ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:10818444, ECO:0000269|PubMed:15461590, ECO:0000269|PubMed:17057224, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222, ECO:0000269|PubMed:8702556}.
uniprot
proteins
mass_dalton
31892
uniprot
proteins
mutagenesis
MUTAGEN 5; /note="T->P: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 106; /note="L->S: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 116; /note="T->I: No significant effect on lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 120; /note="K->R: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 122; /note="T->S: No effect on lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 127; /note="R->K: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 128; /note="P->I: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 142; /note="N->Q: Loss of N-glycosylation. No significant effect on lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 168; /note="Y->F: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 169; /note="S->T: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 170; /note="G->A: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 171; /note="H->L: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 217; /note="R->K: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:15461590"; MUTAGEN 221; /note="Y->W: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 223; /note="H->L: Loss of lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 233; /note="I->T: No significant effect on lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492"; MUTAGEN 276; /note="N->Q: No effect on lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:10620492
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:10818444, ECO:0000269|PubMed:15461590, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222, ECO:0000269|PubMed:8702556}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:10620492, PubMed:8702556). N-linked sugars are of the complex type (PubMed:8702556). N-glycosylation is not required for the phosphatase activity (PubMed:10620492). {ECO:0000269|PubMed:10620492, ECO:0000269|PubMed:8702556}.
uniprot
proteins
protein_family
PA-phosphatase related phosphoesterase family
uniprot
proteins
pubmed
10359651
uniprot
proteins
pubmed
10620492
uniprot
proteins
pubmed
10818444
uniprot
proteins
pubmed
11535125
uniprot
proteins
pubmed
14687668
uniprot
proteins
pubmed
14725715
uniprot
proteins
pubmed
15461590
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
17057224
uniprot
proteins
pubmed
17379599
uniprot
proteins
pubmed
19144319
uniprot
proteins
pubmed
19215222
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
7556647
uniprot
proteins
pubmed
8702556
uniprot
proteins
sequence_length
283
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:19215222}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:O14494}; Multi-pass membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:11535125}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 7..27; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 54..74; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 89..109; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 165..185; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 200..220; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 230..250; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins