PLPP1
entrez
8611
canonical
uniprot
O14494
canonical
ensembl
ENSG00000067113
resolver
ensp
ENSP00000264775
resolver
ensp
ENSP00000302229
resolver
genesymbol
PLPP1
resolver
genesymbol_syn
LPP1
resolver
genesymbol_syn
PPAP2A
resolver
hgnc
HGNC:9228
resolver
uniprot
B7ZKN8
resolver
uniprot
G3XA95
resolver
uniprot
O60457
resolver
uniprot
O60463
resolver
uniprot
Q17RZ4
resolver
uniprot_entry
PLPP1_HUMAN
resolver
uniprot_sec
B7ZKN8
resolver
uniprot_sec
G3XA95
resolver
uniprot_sec
O60457
resolver
uniprot_sec
O60463
resolver
uniprot_sec
Q17RZ4
resolver
activity_regulation
ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase (PubMed:9305923). Insensitive to N-ethylmaleimide (PubMed:9305923). Inhibited by sphingosine, zinc ions and modestly by propanolol (PubMed:9305923, PubMed:9705349). Inhibited by vanadate (PubMed:10962286). {ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9705349}.
uniprot
proteins
amino_acid_sequence
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLGGIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAKYSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCMLFVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAILVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
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:10962286, PubMed:17379599, PubMed:9305923, PubMed:9607309, PubMed:9705349). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). 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:10962286, PubMed:12909631, PubMed:15461590, 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:12909631, PubMed:15461590). May also have an intracellular activity to regulate phospholipid-mediated signaling pathways (By similarity). {ECO:0000250|UniProtKB:O08564, ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:12909631, ECO:0000269|PubMed:15461590, ECO:0000269|PubMed:17379599, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.
uniprot
proteins
mass_dalton
32156
uniprot
proteins
mutagenesis
MUTAGEN 217; /note="R->K: Decreased lipid phosphatase activity."; /evidence="ECO:0000269|PubMed:15461590
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:10962286, PubMed:9305923). N-linked sugars are of the complex type. N-glycosylation is not required for the phosphatase activity (By similarity). {ECO:0000250|UniProtKB:Q61469, ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9305923}.
uniprot
proteins
protein_family
PA-phosphatase related phosphoesterase family
uniprot
proteins
pubmed
10962286
uniprot
proteins
pubmed
12909631
uniprot
proteins
pubmed
14527693
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15461590
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17005594
uniprot
proteins
pubmed
17379599
uniprot
proteins
pubmed
9305923
uniprot
proteins
pubmed
9468526
uniprot
proteins
pubmed
9570154
uniprot
proteins
pubmed
9607309
uniprot
proteins
pubmed
9705349
uniprot
proteins
sequence_length
284
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10962286, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:14527693}; Multi-pass membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:17005594}; 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 95..115; /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