Pdxp
entrez
57028
canonical
uniprot
P60487
canonical
ensembl
ENSMUSG00000116165
resolver
ensp
ENSMUSP00000086796
resolver
enst
ENSMUST00000089378
resolver
genesymbol
Pdxp
resolver
genesymbol_syn
Cin
resolver
genesymbol_syn
Plp
resolver
genesymbol_syn
Plpp
resolver
uniprot
Q6IS27
resolver
uniprot_entry
PLPP_MOUSE
resolver
uniprot_entry
Q6IS27_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by beryllium trifluoride. {ECO:0000269|PubMed:24338473}.
uniprot
proteins
amino_acid_sequence
MARCERLRGAALRDVLGQAQGVLFDCDGVLWNGERIVPGAPELLQRLARAGKNTLFVSNNSRRARPELALRFARLGFAGLRAEQLFSSALCAARLLRQRLSGPPDASGAVFVLGGEGLRAELRAAGLRLAGDPGEDPRVRAVLVGYDEQFSFSRLTEACAHLRDPDCLLVATDRDPWHPLSDGSRTPGTGSLAAAVETASGRQALVVGKPSPYMFQCITEDFSVDPARTLMVGDRLETDILFGHRCGMTTVLTLTGVSSLEEAQAYLTAGQRDLVPHYYVESIADLMEGLED
uniprot
proteins
ec_number
3.1.3.16
uniprot
proteins
ec_number
3.1.3.74
uniprot
proteins
function
FUNCTION: Functions as a pyridoxal phosphate (PLP) phosphatase, which also catalyzes the dephosphorylation of pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), with order of substrate preference PLP > PNP > PMP and therefore plays a role in vitamin B6 metabolism (PubMed:24338473, PubMed:24338687, PubMed:25783190). Also functions as a protein serine phosphatase that specifically dephosphorylates 'Ser-3' in proteins of the actin-depolymerizing factor (ADF)/cofilin family like CFL1 and DSTN. Thereby, regulates cofilin-dependent actin cytoskeleton reorganization, being required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phosphothreonines in LIMK1. Does not dephosphorylate peptides containing phosphotyrosine (By similarity). {ECO:0000250|UniProtKB:Q96GD0, ECO:0000269|PubMed:24338473, ECO:0000269|PubMed:24338687, ECO:0000269|PubMed:25783190}.
uniprot
proteins
mass_dalton
31512
uniprot
proteins
mutagenesis
MUTAGEN 194..195; /note="AA->KK: Abolishes homodimerization. Strongly decreases affinity for pyridoxal phosphate."; /evidence="ECO:0000269|PubMed:24338687
uniprot
proteins
protein_family
HAD-like hydrolase superfamily
uniprot
proteins
pubmed
14522954
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24338473
uniprot
proteins
pubmed
24338687
uniprot
proteins
pubmed
25783190
uniprot
proteins
sequence_length
292
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q96GD0}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250, ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell projection, lamellipodium membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Cell membrane {ECO:0000250|UniProtKB:Q96GD0}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q96GD0}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GD0}. Note=Colocalizes with the actin cytoskeleton in membrane ruffles and lamellipodia. Diffusely distributed throughout the cytosol during pro-metaphase and metaphase. Detected at the dynamic cell poles during telophase. Detected at the cleavage furrow and contractile ring during cytokinesis. Transiently detected at the plasma membrane in late stages of cytokinesis. Detected at the midbody. {ECO:0000250|UniProtKB:Q96GD0}.
uniprot
proteins