PLPP6
entrez
403313
canonical
uniprot
Q8IY26
canonical
ensembl
ENSG00000205808
resolver
ensp
ENSP00000371307
resolver
enst
ENST00000381883
resolver
genesymbol
PLPP6
resolver
genesymbol_syn
PDP1
resolver
genesymbol_syn
PPAPDC2
resolver
hgnc
HGNC:23682
resolver
uniprot
B3KY05
resolver
uniprot
Q5JVJ6
resolver
uniprot
Q8NCK9
resolver
uniprot_entry
PLPP6_HUMAN
resolver
uniprot_sec
B3KY05
resolver
uniprot_sec
Q5JVJ6
resolver
uniprot_sec
Q8NCK9
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by propranolol (PubMed:18930839). Not inhibited by N-ethylmaleimide or bromoenolactome (PubMed:18930839). {ECO:0000269|PubMed:18930839}.
uniprot
proteins
amino_acid_sequence
MPSPRRSMEGRPLGVSASSSSSSPGSPAHGGGGGGSRFEFQSLLSSRATAVDPTCARLRASESPVHRRGSFPLAAAGPSQSPAPPLPEEDRMDLNPSFLGIALRSLLAIDLWLSKKLGVCAGESSSWGSVRPLMKLLEISGHGIPWLLGTLYCLCRSDSWAGREVLMNLLFALLLDLLLVALIKGLVRRRRPAHNQMDMFVTLSVDKYSFPSGHATRAALMSRFILNHLVLAIPLRVLVVLWAFVLGLSRVMLGRHNVTDVAFGFFLGYMQYSIVDYCWLSPHNAPVLFLLWSQR
uniprot
proteins
ec_number
3.1.3.-
uniprot
proteins
ec_number
3.6.1.-
uniprot
proteins
ec_number
3.6.1.68
uniprot
proteins
function
FUNCTION: Magnesium-independent polyisoprenoid diphosphatase that catalyzes the sequential dephosphorylation of presqualene, farnesyl, geranyl and geranylgeranyl diphosphates (PubMed:16464866, PubMed:19220020, PubMed:20110354). Functions in the innate immune response through the dephosphorylation of presqualene diphosphate which acts as a potent inhibitor of the signaling pathways contributing to polymorphonuclear neutrophils activation (PubMed:16464866, PubMed:23568778). May regulate the biosynthesis of cholesterol and related sterols by dephosphorylating presqualene and farnesyl diphosphate, two key intermediates in this biosynthetic pathway (PubMed:20110354). May also play a role in protein prenylation by acting on farnesyl diphosphate and its derivative geranylgeranyl diphosphate, two precursors for the addition of isoprenoid anchors to membrane proteins (PubMed:20110354). Has a lower activity towards phosphatidic acid (PA), but through phosphatidic acid dephosphorylation may participate in the biosynthesis of phospholipids and triacylglycerols (PubMed:18930839). May also act on ceramide-1-P, lysophosphatidic acid (LPA) and sphing-4-enine 1-phosphate/sphingosine-1-phosphate (PubMed:18930839, PubMed:20110354). {ECO:0000269|PubMed:16464866, ECO:0000269|PubMed:18930839, ECO:0000269|PubMed:19220020, ECO:0000269|PubMed:20110354, ECO:0000269|PubMed:23568778}.
uniprot
proteins
mass_dalton
32194
uniprot
proteins
mutagenesis
MUTAGEN 184; /note="K->R: Loss of polyisoprenoid diphosphate phosphatase activity."; /evidence="ECO:0000269|PubMed:20110354"; MUTAGEN 212; /note="S->T: Loss of polyisoprenoid diphosphate phosphatase activity."; /evidence="ECO:0000269|PubMed:20110354"; MUTAGEN 256; /note="H->A: Loss of polyisoprenoid diphosphate phosphatase activity."; /evidence="ECO:0000269|PubMed:20110354
uniprot
proteins
post_translational_modification
PTM: Phosphorylation by PKC activates the phosphatase activity towards presqualene diphosphate. {ECO:0000269|PubMed:19220020, ECO:0000269|PubMed:23568778}.
uniprot
proteins
protein_family
PA-phosphatase related phosphoesterase family
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164053
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16464866
uniprot
proteins
pubmed
18930839
uniprot
proteins
pubmed
19220020
uniprot
proteins
pubmed
20110354
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23568778
uniprot
proteins
pubmed
24275569
uniprot
proteins
sequence_length
295
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16464866, ECO:0000269|PubMed:18930839, ECO:0000269|PubMed:20110354}; Multi-pass membrane protein {ECO:0000305|PubMed:20110354}. Nucleus envelope {ECO:0000269|PubMed:18930839}. Nucleus inner membrane {ECO:0000305|PubMed:20110354}.
uniprot
proteins
transmembrane_region
TRANSMEM 133..153; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 165..185; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 229..249; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 261..281; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins