Human Gene PDXP (ENST00000215904.7) from GENCODE V44
Description: Homo sapiens pyridoxal phosphatase (PDXP), mRNA. (from RefSeq NM_020315) RefSeq Summary (NM_020315): Pyridoxal 5-prime-phosphate (PLP) is the active form of vitamin B6 that acts as a coenzyme in maintaining biochemical homeostasis. The preferred degradation route from PLP to 4-pyridoxic acid involves the dephosphorylation of PLP by PDXP (Jang et al., 2003 [PubMed 14522954]).[supplied by OMIM, Mar 2008]. Gencode Transcript: ENST00000215904.7 Gencode Gene: ENSG00000241360.2 Transcript (Including UTRs) Position: hg38 chr22:37,658,723-37,666,932 Size: 8,210 Total Exon Count: 2 Strand: + Coding Region Position: hg38 chr22:37,658,783-37,665,871 Size: 7,089 Coding Exon Count: 2
ID:PLPP_HUMAN DESCRIPTION: RecName: Full=Pyridoxal phosphate phosphatase; Short=PLP phosphatase; EC=3.1.3.3; EC=3.1.3.74; AltName: Full=Chronophin; FUNCTION: Protein serine phosphatase that dephosphorylates 'Ser-3' in cofilin and probably also dephosphorylates phospho-serine residues in DSTN. Regulates cofilin-dependent actin cytoskeleton reorganization. Required for normal progress through mitosis and normal cytokinesis. Does not dephosphorylate phospho-threonines in LIMK1. Does not dephosphorylate peptides containing phospho- tyrosine. Pyridoxal phosphate phosphatase. Has some activity towards pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PMP) and pyridoxine 5'-phosphate (PNP), with a highest activity with PLP followed by PNP. CATALYTIC ACTIVITY: Pyridoxal 5'-phosphate + H(2)O = pyridoxal + phosphate. CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)- serine + phosphate. COFACTOR: Divalent ions. Magnesium is the most effective. ENZYME REGULATION: Inhibited by NaF, Zn(2+), Ca(2+), Mn(2+) and EDTA. SUBUNIT: Homodimer. INTERACTION: P29066:Arrb1 (xeno); NbExp=2; IntAct=EBI-4303060, EBI-4303019; SUBCELLULAR LOCATION: Cytoplasm, cytosol. Cytoplasm, cytoskeleton. Cell projection, ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. 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. TISSUE SPECIFICITY: Ubiquitous. Highly expressed in all the regions of central nerve system except the spinal cord. Also expressed at high level in liver and testis. In fetus, it is weakly expressed in all organs except brain. SIMILARITY: Belongs to the HAD-like hydrolase superfamily.
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on Q96GD0
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
Gene Ontology (GO) Annotations with Structured Vocabulary
Molecular Function: GO:0000287 magnesium ion binding GO:0004647 phosphoserine phosphatase activity GO:0004721 phosphoprotein phosphatase activity GO:0005515 protein binding GO:0016787 hydrolase activity GO:0016791 phosphatase activity GO:0031072 heat shock protein binding GO:0033883 pyridoxal phosphatase activity GO:0042803 protein homodimerization activity GO:0046872 metal ion binding GO:0098519 nucleotide phosphatase activity, acting on free nucleotides
Biological Process: GO:0006470 protein dephosphorylation GO:0007088 regulation of mitotic nuclear division GO:0008152 metabolic process GO:0030836 positive regulation of actin filament depolymerization GO:0031247 actin rod assembly GO:0032361 pyridoxal phosphate catabolic process GO:0032465 regulation of cytokinesis GO:0071318 cellular response to ATP
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