PLPP3
entrez
8613
canonical
uniprot
O14495
canonical
ensembl
ENSG00000162407
resolver
ensp
ENSP00000360296
resolver
enst
ENST00000371250
resolver
genesymbol
PLPP3
resolver
genesymbol_syn
LPP3
resolver
genesymbol_syn
PPAP2B
resolver
hgnc
HGNC:9229
resolver
uniprot
B2R651
resolver
uniprot
D3DQ52
resolver
uniprot
Q5U0F7
resolver
uniprot
Q96GW0
resolver
uniprot
Q99782
resolver
uniprot_entry
PLPP3_HUMAN
resolver
uniprot_sec
B2R651
resolver
uniprot_sec
D3DQ52
resolver
uniprot_sec
Q5U0F7
resolver
uniprot_sec
Q96GW0
resolver
uniprot_sec
Q99782
resolver
activity_regulation
ACTIVITY REGULATION: Magnesium-independent phospholipid phosphatase (PubMed:9705349). Insensitive to N-ethylmaleimide (PubMed:9705349). Inhibited by sphingosine, zinc ions and modestly by propanolol (PubMed:9705349). {ECO:0000269|PubMed:9705349}.
uniprot
proteins
amino_acid_sequence
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIKPYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQNPYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYRCRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFYTGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVDIIDRNNHHNMM
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.1.3.4
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:27694435, PubMed:9607309, PubMed:9705349). Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound (PubMed:9607309). Has both an extracellular and an intracellular phosphatase activity, allowing the hydrolysis and the cellular uptake of these bioactive lipid mediators from the milieu, regulating signal transduction in different cellular processes (PubMed:23591818, PubMed:27694435, PubMed:9607309). Through the dephosphorylation of extracellular sphingosine-1-phosphate and the regulation of its extra- and intracellular availability, plays a role in vascular homeostasis, regulating endothelial cell migration, adhesion, survival, proliferation and the production of pro-inflammatory cytokines (PubMed:27694435). By maintaining the appropriate levels of this lipid in the cerebellum, also ensure its proper development and function (By similarity). Through its intracellular lipid phosphatase activity may act in early compartments of the secretory pathway, regulating the formation of Golgi to endoplasmic reticulum retrograde transport carriers (PubMed:23591818). {ECO:0000250|UniProtKB:Q99JY8, ECO:0000269|PubMed:23591818, ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.; FUNCTION: Independently of this phosphatase activity may also function in the Wnt signaling pathway and the stabilization of beta-catenin/CTNNB1, thereby regulating cell proliferation, migration and differentiation in angiogenesis or yet in tumor growth (PubMed:20123964, PubMed:21569306). Also plays a role in integrin-mediated cell-cell adhesion in angiogenesis (PubMed:12660161, PubMed:16099422). {ECO:0000269|PubMed:12660161, ECO:0000269|PubMed:16099422, ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:21569306}.
uniprot
proteins
mass_dalton
35116
uniprot
proteins
mutagenesis
MUTAGEN 106; /note="Y->A: No effect on basolateral localization in polarized cells."; /evidence="ECO:0000269|PubMed:17005594"; MUTAGEN 109; /note="Y->A: Loss of basolateral localization in polarized cells."; /evidence="ECO:0000269|PubMed:17005594"; MUTAGEN 110; /note="Y->A: Loss of basolateral localization in polarized cells."; /evidence="ECO:0000269|PubMed:17005594"; MUTAGEN 184; /note="D->E: Loss of binding to integrin. Loss of function in integrin-mediated cell-cell interaction."; /evidence="ECO:0000269|PubMed:9705349
uniprot
proteins
pathway_participation
PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:27694435, ECO:0000269|PubMed:9607309, ECO:0000269|PubMed:9705349}.
uniprot
proteins
post_translational_modification
PTM: N-glycosylated (PubMed:9705349). Contains high-mannose oligosaccharides (PubMed:9705349). {ECO:0000269|PubMed:9705349}.
uniprot
proteins
protein_family
PA-phosphatase related phosphoesterase family
uniprot
proteins
pubmed
12660161
uniprot
proteins
pubmed
14527693
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14725715
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16099422
uniprot
proteins
pubmed
17005594
uniprot
proteins
pubmed
18215144
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
20123964
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21569306
uniprot
proteins
pubmed
23591818
uniprot
proteins
pubmed
27694435
uniprot
proteins
pubmed
9110174
uniprot
proteins
pubmed
9305923
uniprot
proteins
pubmed
9607309
uniprot
proteins
pubmed
9705349
uniprot
proteins
sequence_length
311
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12660161, ECO:0000269|PubMed:20123964, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Basolateral cell membrane {ECO:0000269|PubMed:14527693}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:23591818}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Membrane raft {ECO:0000269|PubMed:17005594}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P97544}. Note=Cycles between the endoplasmic reticulum and the Golgi. {ECO:0000269|PubMed:23591818}.
uniprot
proteins
transmembrane_region
TRANSMEM 34..54; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 86..106; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 123..143; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 194..214; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 226..243; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 258..278; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins