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P60487

- PLPP_MOUSE

UniProt

P60487 - PLPP_MOUSE

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Protein

Pyridoxal phosphate phosphatase

Gene
Pdxp, Cin, Plp, Plpp
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 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.2 Publications

Catalytic activityi

Pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate.2 Publications
O-phospho-L(or D)-serine + H2O = L(or D)-serine + phosphate.2 Publications

Cofactori

Divalent ions. Magnesium is the most effective.1 Publication

Enzyme regulationi

Inhibited by beryllium trifluoride.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei25 – 251Nucleophile By similarity
Metal bindingi25 – 251Magnesium
Active sitei27 – 271Proton donor By similarity
Metal bindingi27 – 271Magnesium; via carbonyl oxygen
Binding sitei178 – 1781Substrate By similarity
Binding sitei209 – 2091Substrate By similarity
Metal bindingi234 – 2341Magnesium

GO - Molecular functioni

  1. heat shock protein binding Source: MGI
  2. magnesium ion binding Source: UniProtKB
  3. phosphoprotein phosphatase activity Source: UniProtKB
  4. phosphoserine phosphatase activity Source: UniProtKB-EC
  5. protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. pyridoxal phosphatase activity Source: UniProtKB

GO - Biological processi

  1. actin rod assembly Source: MGI
  2. cellular response to ATP Source: MGI
  3. positive regulation of actin filament depolymerization Source: UniProtKB
  4. protein dephosphorylation Source: UniProtKB
  5. pyridoxal phosphate catabolic process Source: UniProtKB
  6. regulation of cytokinesis Source: UniProtKB
  7. regulation of mitosis Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Magnesium, Metal-binding, Pyridoxal phosphate

Enzyme and pathway databases

BRENDAi3.1.3.74. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Pyridoxal phosphate phosphatase (EC:3.1.3.3, EC:3.1.3.74)
Short name:
PLP phosphatase
Alternative name(s):
Chronophin
Gene namesi
Name:Pdxp
Synonyms:Cin, Plp, Plpp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:1919282. Pdxp.

Subcellular locationi

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.

GO - Cellular componenti

  1. actin cytoskeleton Source: Ensembl
  2. cell-cell junction Source: MGI
  3. cleavage furrow Source: Ensembl
  4. contractile ring Source: Ensembl
  5. cytosol Source: UniProtKB
  6. lamellipodium membrane Source: UniProtKB-SubCell
  7. midbody Source: Ensembl
  8. ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi194 – 1952AA → KK: Abolishes homodimerization. Strongly decreases affinity for pyridoxal phosphate. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 292292Pyridoxal phosphate phosphatasePRO_0000068838Add
BLAST

Proteomic databases

PaxDbiP60487.
PRIDEiP60487.

2D gel databases

REPRODUCTION-2DPAGEP60487.

PTM databases

PhosphoSiteiP60487.

Expressioni

Tissue specificityi

Ubiquitous. highly expressed in brain (at protein level).1 Publication

Gene expression databases

BgeeiP60487.
CleanExiMM_PDXP.
GenevestigatoriP60487.

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1
292
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 1810
Beta strandi20 – 256
Turni27 – 293
Beta strandi30 – 323
Helixi40 – 4910
Beta strandi53 – 586
Helixi65 – 7410
Helixi82 – 843
Beta strandi85 – 873
Helixi88 – 9912
Turni104 – 1063
Beta strandi109 – 1146
Helixi116 – 1249
Beta strandi132 – 1343
Beta strandi139 – 1446
Helixi152 – 16110
Beta strandi167 – 1726
Beta strandi176 – 1794
Beta strandi185 – 1873
Helixi189 – 20012
Helixi213 – 2219
Helixi226 – 2283
Beta strandi229 – 2346
Turni236 – 2383
Helixi239 – 2468
Beta strandi249 – 2579
Helixi260 – 2689
Helixi272 – 2743
Beta strandi277 – 2826
Helixi283 – 2897

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4BKMX-ray2.65A/B/C/D1-100[»]
A/B/C/D208-292[»]
4BX0X-ray1.75A1-292[»]
4BX2X-ray2.19A/B1-292[»]
4BX3X-ray2.19A/B1-292[»]
ProteinModelPortaliP60487.
SMRiP60487. Positions 1-291.

Family & Domainsi

Region

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0647.
GeneTreeiENSGT00510000047020.
HOGENOMiHOG000068104.
HOVERGENiHBG049429.
InParanoidiP60487.
KOiK07758.
OMAiFECISSQ.
OrthoDBiEOG7XDBG1.
PhylomeDBiP60487.
TreeFamiTF314344.

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]
SUPFAMiSSF56784. SSF56784. 1 hit.
TIGRFAMsiTIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.

Sequencei

Sequence statusi: Complete.

P60487-1 [UniParc]FASTAAdd to Basket

« Hide

MARCERLRGA ALRDVLGQAQ GVLFDCDGVL WNGERIVPGA PELLQRLARA    50
GKNTLFVSNN SRRARPELAL RFARLGFAGL RAEQLFSSAL CAARLLRQRL 100
SGPPDASGAV FVLGGEGLRA ELRAAGLRLA GDPGEDPRVR AVLVGYDEQF 150
SFSRLTEACA HLRDPDCLLV ATDRDPWHPL SDGSRTPGTG SLAAAVETAS 200
GRQALVVGKP SPYMFQCITE DFSVDPARTL MVGDRLETDI LFGHRCGMTT 250
VLTLTGVSSL EEAQAYLTAG QRDLVPHYYV ESIADLMEGL ED 292
Length:292
Mass (Da):31,512
Last modified:March 1, 2004 - v1
Checksum:iB5F1B2C7E71A585D
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY366300 mRNA. Translation: AAR12209.1.
BC058388 mRNA. Translation: AAH58388.1.
CCDSiCCDS27627.1.
RefSeqiNP_064667.2. NM_020271.3.
UniGeneiMm.263169.

Genome annotation databases

EnsembliENSMUST00000089378; ENSMUSP00000086796; ENSMUSG00000068221.
GeneIDi57028.
KEGGimmu:57028.
UCSCiuc007wru.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY366300 mRNA. Translation: AAR12209.1 .
BC058388 mRNA. Translation: AAH58388.1 .
CCDSi CCDS27627.1.
RefSeqi NP_064667.2. NM_020271.3.
UniGenei Mm.263169.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4BKM X-ray 2.65 A/B/C/D 1-100 [» ]
A/B/C/D 208-292 [» ]
4BX0 X-ray 1.75 A 1-292 [» ]
4BX2 X-ray 2.19 A/B 1-292 [» ]
4BX3 X-ray 2.19 A/B 1-292 [» ]
ProteinModelPortali P60487.
SMRi P60487. Positions 1-291.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei P60487.

2D gel databases

REPRODUCTION-2DPAGE P60487.

Proteomic databases

PaxDbi P60487.
PRIDEi P60487.

Protocols and materials databases

DNASUi 57028.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000089378 ; ENSMUSP00000086796 ; ENSMUSG00000068221 .
GeneIDi 57028.
KEGGi mmu:57028.
UCSCi uc007wru.1. mouse.

Organism-specific databases

CTDi 57026.
MGIi MGI:1919282. Pdxp.

Phylogenomic databases

eggNOGi COG0647.
GeneTreei ENSGT00510000047020.
HOGENOMi HOG000068104.
HOVERGENi HBG049429.
InParanoidi P60487.
KOi K07758.
OMAi FECISSQ.
OrthoDBi EOG7XDBG1.
PhylomeDBi P60487.
TreeFami TF314344.

Enzyme and pathway databases

BRENDAi 3.1.3.74. 3474.

Miscellaneous databases

ChiTaRSi PDXP. mouse.
NextBioi 313473.
PROi P60487.
SOURCEi Search...

Gene expression databases

Bgeei P60487.
CleanExi MM_PDXP.
Genevestigatori P60487.

Family and domain databases

Gene3Di 3.40.50.1000. 2 hits.
3.40.50.10410. 1 hit.
InterProi IPR023214. HAD-like_dom.
IPR006357. HAD-SF_hydro_IIA.
IPR023215. NPhePase-like_dom.
IPR006349. PGP_euk.
[Graphical view ]
Pfami PF13344. Hydrolase_6. 1 hit.
[Graphical view ]
SUPFAMi SSF56784. SSF56784. 1 hit.
TIGRFAMsi TIGR01460. HAD-SF-IIA. 1 hit.
TIGR01452. PGP_euk. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiPLPP_MOUSE
AccessioniPrimary (citable) accession number: P60487
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: March 1, 2004
Last modified: July 9, 2014
This is version 93 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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