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Protein

Pyridoxal phosphate phosphatase

Gene

PDXP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.By similarity
O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.By similarity

Cofactori

Mg2+By similarityNote: Divalent metal ions. Mg2+ is the most effective.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251NucleophileBy similarity
Metal bindingi25 – 251MagnesiumBy similarity
Active sitei27 – 271Proton donorBy similarity
Metal bindingi27 – 271Magnesium; via carbonyl oxygenBy similarity
Binding sitei182 – 1821SubstrateBy similarity
Binding sitei213 – 2131SubstrateBy similarity
Metal bindingi238 – 2381MagnesiumBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal phosphate phosphatase (EC:3.1.3.3By similarity, EC:3.1.3.74By similarity)
Short name:
PLP phosphatase
Alternative name(s):
Chronophin
Gene namesi
Name:PDXP
Synonyms:CIN
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Unplaced

Subcellular locationi

  • Cytoplasmcytosol 1 Publication
  • Cytoplasmcytoskeleton By similarity
  • Cell projectionruffle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cell projectionlamellipodium membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  • 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.By similarity

GO - Cellular componenti

  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • lamellipodium membrane Source: UniProtKB-SubCell
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Pyridoxal phosphate phosphatasePRO_0000254016Add
BLAST

Proteomic databases

PaxDbiQ3ZBF9.
PRIDEiQ3ZBF9.

Expressioni

Tissue specificityi

Detected in brain (at protein level).1 Publication

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016505.

Structurei

3D structure databases

ProteinModelPortaliQ3ZBF9.
SMRiQ3ZBF9. Positions 3-296.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 625Substrate bindingBy similarity

Sequence similaritiesi

Belongs to the HAD-like hydrolase superfamily.Curated

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiQ3ZBF9.
KOiK07758.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3ZBF9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARCERLRGA ALRDVVGRAQ GVLFDCNGVL WNGERAVPGA PELLERLAQA
60 70 80 90 100
GKATLFVSNN SRRARPELAL RFARLGFGGL RSEQLFSSAL CAARLLRQRL
110 120 130 140 150
LGPPDTQGAV FVLGGEGLRA ELRAAGLRLA GDPSEDPGAA PRVRAVLVGY
160 170 180 190 200
DEHFSFAKLS EACAHLRDPD CLLVATDRDP WHPLSDGSRT PGTGSLAAAV
210 220 230 240 250
ETASGRQALV VGKPSPYMFE CITEHFSVDP GRTLMVGDRL ETDILFGHRC
260 270 280 290
GMTTVLTLTG VSSLEEAQAY LAAGQHDLVP HYYVESIADL MEGLED
Length:296
Mass (Da):31,749
Last modified:September 27, 2005 - v1
Checksum:iA3F0B3AA9D5D1E19
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103329 mRNA. Translation: AAI03330.1.
RefSeqiNP_001030207.1. NM_001035035.2.
UniGeneiBt.45290.

Genome annotation databases

GeneIDi506308.
KEGGibta:506308.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103329 mRNA. Translation: AAI03330.1.
RefSeqiNP_001030207.1. NM_001035035.2.
UniGeneiBt.45290.

3D structure databases

ProteinModelPortaliQ3ZBF9.
SMRiQ3ZBF9. Positions 3-296.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016505.

Proteomic databases

PaxDbiQ3ZBF9.
PRIDEiQ3ZBF9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi506308.
KEGGibta:506308.

Organism-specific databases

CTDi57026.

Phylogenomic databases

eggNOGiKOG2882. Eukaryota.
COG0647. LUCA.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiQ3ZBF9.
KOiK07758.

Miscellaneous databases

NextBioi20867551.

Family and domain databases

Gene3Di3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProiIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamiPF13344. Hydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF000915. PGP-type_phosphatase. 1 hit.
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Crossbred X Angus.
    Tissue: Ileum.
  2. "Chronophin, a novel HAD-type serine protein phosphatase, regulates cofilin-dependent actin dynamics."
    Gohla A., Birkenfeld J., Bokoch G.M.
    Nat. Cell Biol. 7:21-29(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Entry informationi

Entry nameiPLPP_BOVIN
AccessioniPrimary (citable) accession number: Q3ZBF9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 2006
Last sequence update: September 27, 2005
Last modified: January 20, 2016
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.