O08564
uniprot
O08564
canonical
activity_regulation
ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase (PubMed:10359651, PubMed:8663293). Insensitive to N-ethylmaleimide (PubMed:10359651). {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}.
uniprot
proteins
amino_acid_sequence
MFDKPRLPYVVLDVICVLLAGLPFIILTSRHTPFQRGVFCTDESIKYPYREDTIPYALLGGIVIPFCIIVMITGETLSVYFNVLHSNSFVSNHYIATIYKAVGAFLFGASASQSLTDIAKYSIGRLRPHFLAVCNPDWSKINCSDGYIENFVCQGNEQKVREGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPMLQFGLVALSIYVGLSRVSDYKHHWSDVLIGLIQGAVVAILVVLYVTDFFKTTESNKERKEDSHTTLHETTNRQSYARNHEP
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:8663293). 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:10359651). It is for instance essential for the extracellular hydrolysis of S1P and subsequent conversion into intracellular S1P (By similarity). Involved in the regulation of inflammation, platelets activation, cell proliferation and migration among other processes (By similarity). 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:17057224, ECO:0000269|PubMed:8663293}.
uniprot
proteins
mass_dalton
31996
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:10359651, ECO:0000269|PubMed:8663293}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated. N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity. {ECO:0000250|UniProtKB:Q61469}.
uniprot
proteins
protein_family
PA-phosphatase related phosphoesterase family
uniprot
proteins
pubmed
10359651
uniprot
proteins
pubmed
11704545
uniprot
proteins
pubmed
17057224
uniprot
proteins
pubmed
8663293
uniprot
proteins
sequence_length
282
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8663293}; 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:0000250|UniProtKB:Q61469}; 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 195..215; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 230..250; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins