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P60487

- PLPP_MOUSE

UniProt

P60487 - PLPP_MOUSE

Protein

Pyridoxal phosphate phosphatase

Gene

Pdxp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 94 (01 Oct 2014)
      Sequence version 1 (01 Mar 2004)
      Previous versions | rss
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    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.By similarity2 Publications

    Catalytic activityi

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

    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 – 251NucleophileBy similarity
    Metal bindingi25 – 251Magnesium2 Publications
    Active sitei27 – 271Proton donorBy similarity
    Metal bindingi27 – 271Magnesium; via carbonyl oxygen2 Publications
    Binding sitei178 – 1781SubstrateBy similarity
    Binding sitei209 – 2091SubstrateBy similarity
    Metal bindingi234 – 2341Magnesium2 Publications

    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

    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 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.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

    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.2 Publications

    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.
    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

    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

    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: October 1, 2014
    This is version 94 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