Pyridoxal phosphate phosphatase - Bos taurus (Bovine)

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Q3ZBF9 (PLPP_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 48. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Pyridoxal phosphate phosphatase
Short name=PLP phosphatase

Alternative name(s):
Chronophin
EC=3.1.3.3
EC=3.1.3.74

Gene names

Name:	PDXP
Synonyms:	CIN

Organism

Bos taurus (Bovine)

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	296 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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 By similarity. Ref.2
Catalytic activity	Pyridoxal 5'-phosphate + H₂O = pyridoxal + phosphate. O-phospho-L(or D)-serine + H₂O = L(or D)-serine + phosphate.
Cofactor	Divalent ions. Magnesium is the most effective By similarity.
Subunit structure	Homodimer By similarity.
Subcellular location	Cytoplasm › cytosol. Cytoplasm › cytoskeleton By similarity. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projection › lamellipodium membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell membrane; Peripheral membrane protein; 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. Ref.2
Tissue specificity	Detected in brain (at protein level). Ref.2
Sequence similarities	Belongs to the HAD-like hydrolase superfamily.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Ligand	Magnesium Metal-binding Pyridoxal phosphate
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	positive regulation of actin filament depolymerization Inferred from sequence or structural similarity. Source: UniProtKB protein dephosphorylation Inferred from direct assay Ref.2. Source: UniProtKB regulation of cytokinesis Inferred from sequence or structural similarity. Source: UniProtKB regulation of mitosis Inferred from sequence or structural similarity. Source: UniProtKB
Cellular component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay Ref.2. Source: UniProtKB lamellipodium membrane Inferred from electronic annotation. Source: UniProtKB-SubCell ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoprotein phosphatase activity Inferred from direct assay Ref.2. Source: UniProtKB phosphoserine phosphatase activity Inferred from electronic annotation. Source: EC pyridoxal phosphatase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 296

296

Pyridoxal phosphate phosphatase

PRO_0000254016

Regions

Region

58 – 62

Substrate binding By similarity

Sites

Active site

Nucleophile By similarity

Active site

Proton donor By similarity

Metal binding

Magnesium By similarity

Metal binding

Magnesium; via carbonyl oxygen By similarity

Metal binding

238

Magnesium By similarity

Binding site

182

Substrate By similarity

Binding site

213

Substrate By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q3ZBF9 [UniParc].

Last modified September 27, 2005. Version 1.
Checksum: A3F0B3AA9D5D1E19
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FASTA

296

31,749

        10         20         30         40         50         60 
MARCERLRGA ALRDVVGRAQ GVLFDCNGVL WNGERAVPGA PELLERLAQA GKATLFVSNN 

        70         80         90        100        110        120 
SRRARPELAL RFARLGFGGL RSEQLFSSAL CAARLLRQRL LGPPDTQGAV FVLGGEGLRA 

       130        140        150        160        170        180 
ELRAAGLRLA GDPSEDPGAA PRVRAVLVGY DEHFSFAKLS EACAHLRDPD CLLVATDRDP 

       190        200        210        220        230        240 
WHPLSDGSRT PGTGSLAAAV ETASGRQALV VGKPSPYMFE CITEHFSVDP GRTLMVGDRL 

       250        260        270        280        290 
ETDILFGHRC GMTTVLTLTG VSSLEEAQAY LAAGQHDLVP HYYVESIADL MEGLED

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15580268] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BC103329 mRNA. Translation: AAI03330.1.
IPI	IPI00713190.
RefSeq	NP_001030207.1. NM_001035035.1.
UniGene	Bt.45290.
3D structure databases
HSSP	HSSP built from PDB template 1ZJJ based on UniProtKB O59622.
ProteinModelPortal	Q3ZBF9.
SMR	Q3ZBF9. Positions 3-296.
ModBase	Search...
Protein-protein interaction databases
STRING	Q3ZBF9.
Proteomic databases
PRIDE	Q3ZBF9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	506308.
KEGG	bta:506308.
Organism-specific databases
CTD	57026.
Phylogenomic databases
eggNOG	maNOG18850.
GeneTree	ENSGT00510000047020.
HOVERGEN	HBG049429.
InParanoid	Q3ZBF9.
OrthoDB	EOG44F69M.
PhylomeDB	Q3ZBF9.
Family and domain databases
InterPro	IPR005834. Dehalogen-like_hydro. IPR023214. HAD-like_dom. IPR006357. HAD-SF_hydro_IIA. IPR023215. NPhePase-like_dom. IPR006349. PGP_euk. [Graphical view]
Gene3D	G3DSA:3.40.50.1000. HAD-like_dom. 2 hits. G3DSA:3.40.50.10410. NPhePase-like_dom. 1 hit.
KO	K07758.
Pfam	PF00702. Hydrolase. 1 hit. [Graphical view]
SUPFAM	SSF56784. HAD-like_dom. 1 hit.
TIGRFAMs	TIGR01460. HAD-SF-IIA. 1 hit. TIGR01452. PGP_euk. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PLPP_BOVIN

Accession

Primary (citable) accession number: Q3ZBF9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	September 27, 2005
Last modified:	November 16, 2011
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Family and domain databases

Entry information

Relevant documents