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P60487 (PLPP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pyridoxal phosphate phosphatase

Short name=PLP phosphatase
EC=3.1.3.3
EC=3.1.3.74
Alternative name(s):
Chronophin
Gene names
Name:Pdxp
Synonyms:Cin, Plp, Plpp
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length292 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. 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. Ref.5 PubMed 24338473

Catalytic activity

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate. Ref.5 PubMed 24338473

O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate. Ref.5 PubMed 24338473

Cofactor

Divalent ions. Magnesium is the most effective. PubMed 24338473

Enzyme regulation

Inhibited by beryllium trifluoride. PubMed 24338473

Subunit structure

Homodimer. Ref.5

Subcellular location

Cytoplasmcytosol By similarity. Cytoplasmcytoskeleton By similarity. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Cell projectionlamellipodium 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.

Tissue specificity

Ubiquitous. highly expressed in brain (at protein level). PubMed 24338473

Sequence similarities

Belongs to the HAD-like hydrolase superfamily.

Ontologies

Keywords
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   LigandMagnesium
Metal-binding
Pyridoxal phosphate
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin rod assembly

Inferred from sequence orthology PubMed 19000834. Source: MGI

cellular response to ATP

Inferred from sequence orthology PubMed 19000834. Source: MGI

positive regulation of actin filament depolymerization

Inferred from sequence or structural similarity. Source: UniProtKB

protein dephosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

pyridoxal phosphate catabolic process

Inferred from direct assay PubMed 24338473. 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_componentactin cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cleavage furrow

Inferred from electronic annotation. Source: Ensembl

contractile ring

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

lamellipodium membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from electronic annotation. Source: Ensembl

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionheat shock protein binding

Inferred from sequence orthology PubMed 19000834. Source: MGI

magnesium ion binding

Inferred from direct assay Ref.5. Source: UniProtKB

phosphoprotein phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

phosphoserine phosphatase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein homodimerization activity

Inferred from physical interaction Ref.5. Source: UniProtKB

pyridoxal phosphatase activity

Inferred from direct assay PubMed 24338473. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 292292Pyridoxal phosphate phosphatase
PRO_0000068838

Regions

Region58 – 625Substrate binding By similarity

Sites

Active site251Nucleophile By similarity
Active site271Proton donor By similarity
Metal binding251Magnesium
Metal binding271Magnesium; via carbonyl oxygen
Metal binding2341Magnesium
Binding site1781Substrate By similarity
Binding site2091Substrate By similarity

Experimental info

Mutagenesis194 – 1952AA → KK: Abolishes homodimerization. Strongly decreases affinity for pyridoxal phosphate. Ref.5

Secondary structure

....................................................... 292
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P60487 [UniParc].

Last modified March 1, 2004. Version 1.
Checksum: B5F1B2C7E71A585D

FASTA29231,512
        10         20         30         40         50         60 
MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA GKNTLFVSNN 

        70         80         90        100        110        120 
SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL SGPPDASGAV FVLGGEGLRA 

       130        140        150        160        170        180 
ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF SFSRLTEACA HLRDPDCLLV ATDRDPWHPL 

       190        200        210        220        230        240 
SDGSRTPGTG SLAAAVETAS GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI 

       250        260        270        280        290 
LFGHRCGMTT VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED 

« Hide

References

« Hide 'large scale' references
[1]"Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution."
Jang Y.M., Kim D.W., Kang T.-C., Won M.H., Baek N.-I., Moon B.J., Choi S.Y., Kwon O.-S.
J. Biol. Chem. 278:50040-50046(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Swiss.
Tissue: Brain.
[2]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 100-119 AND 141-154, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Hippocampus.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-292.
Strain: C57BL/6.
Tissue: Brain.
[4]"Evolutionary and structural analyses of the mammalian haloacid dehalogenase-type phosphatases AUM and chronophin provide insight into the basis of their different substrate specificities."
Seifried A., Knobloch G., Duraphe P.S., Segerer G., Manhard J., Schindelin H., Schultz J., Gohla A.
J. Biol. Chem. 289:3416-3431(2014)
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-100 AND 208-233 IN COMPLEX WITH MAGNESIUM, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, FUNCTION.
[5]"Chronophin dimerization is required for proper positioning of its substrate specificity loop."
Kestler C., Knobloch G., Tessmer I., Jeanclos E., Schindelin H., Gohla A.
J. Biol. Chem. 289:3094-3103(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH MAGNESIUM AND BERYLLIUM TRIFLUORIDE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF 194-ALA-ALA-195.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY366300 mRNA. Translation: AAR12209.1.
BC058388 mRNA. Translation: AAH58388.1.
RefSeqNP_064667.2. NM_020271.3.
UniGeneMm.263169.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKMX-ray2.65A/B/C/D1-100[»]
A/B/C/D208-233[»]
4BX0X-ray1.75A1-292[»]
4BX2X-ray2.19A/B1-292[»]
4BX3X-ray2.19A/B1-292[»]
ProteinModelPortalP60487.
SMRP60487. Positions 2-290.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteP60487.

2D gel databases

REPRODUCTION-2DPAGEP60487.

Proteomic databases

PaxDbP60487.
PRIDEP60487.

Protocols and materials databases

DNASU57028.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000068221.
GeneID57028.
KEGGmmu:57028.
UCSCuc007wru.1. mouse.

Organism-specific databases

CTD57026.
MGIMGI:1919282. Pdxp.

Phylogenomic databases

eggNOGCOG0647.
GeneTreeENSGT00510000047020.
HOGENOMHOG000068104.
HOVERGENHBG049429.
InParanoidP60487.
KOK07758.
OMACITEDFS.
OrthoDBEOG7XDBG1.
PhylomeDBP60487.
TreeFamTF314344.

Enzyme and pathway databases

BRENDA3.1.3.74. 3474.

Gene expression databases

BgeeP60487.
CleanExMM_PDXP.
GenevestigatorP60487.

Family and domain databases

Gene3D3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProIPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view]
PfamPF13344. Hydrolase_6. 1 hit.
[Graphical view]
SUPFAMSSF56784. SSF56784. 1 hit.
TIGRFAMsTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNetSearch...

Other

ChiTaRSPDXP. mouse.
NextBio313473.
PROP60487.
SOURCESearch...

Entry information

Entry namePLPP_MOUSE
AccessionPrimary (citable) accession number: P60487
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: April 16, 2014
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot