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Protein

Magnesium-dependent phosphatase 1

Gene

Mdp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Magnesium-dependent phosphatase which may act as a tyrosine phosphatase.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by vanadate and zinc, and slightly by calcium.1 Publication

Kineticsi

Dephosphorylates ribose-5-phosphate, 2-deoxy-ribose-5-phosphate, phosphotyrosine, arabinose-5-phosphate, fructose-6-phosphate, 5'-CMP, pNPP, 5'-AMP and glucose-6-phosphate with a decreasing relative rate of 1, 0.9, 0.8, 0.6, 0.5, 0.2, 0.2, 0.2 and 0.06. Dephosphorylates phosphotyrosine with a greater than 100 fold rate over phosphoserine or phosphothreonine.

  1. KM=9.5 mM for ribose-5-phosphate1 Publication
  2. KM=5.6 mM for 2-deoxy-ribose-5-phosphate1 Publication
  3. KM=15 mM for phosphotyrosine1 Publication
  4. KM=1.1 mM for arabinose-5-phosphate1 Publication
  5. KM=21 mM for fructose-6-phosphate1 Publication
  6. KM=12 mM for 5'-CMP1 Publication
  7. KM=1.7 mM for pNPP1 Publication
  8. KM=26 mM for 5'-AMP1 Publication
  9. KM=31 mM for glucose-6-phosphate1 Publication

    pH dependencei

    Optimum pH is 5.3.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Active sitei11NucleophileCurated1
    Metal bindingi11Magnesium1
    Binding sitei12Phosphate; via amide nitrogen1
    Active sitei13Proton donorCurated1
    Metal bindingi13Magnesium1
    Binding sitei13Phosphate; via amide nitrogen1
    Binding sitei20SubstrateCurated1
    Binding sitei69Phosphate1
    Binding sitei70Phosphate1
    Binding sitei70SubstrateCurated1
    Binding sitei100Phosphate1
    Metal bindingi123Magnesium1

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Magnesium-dependent phosphatase 1 (EC:3.1.3.-, EC:3.1.3.48)
    Short name:
    MDP-1
    Gene namesi
    Name:Mdp1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 14

    Organism-specific databases

    MGIiMGI:1915131. Mdp1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi11D → N or E: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi13D → N: 92% loss of enzymatic activity. 1 Publication1
    Mutagenesisi69S → A: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi100K → R: Abolishes enzymatic activity. 1 Publication1
    Mutagenesisi103H → K or A: 50% decrease in enzymatic activity. 1 Publication1
    Mutagenesisi122D → N: Abolishes enzymatic activity. 1
    Mutagenesisi123D → N: Abolishes enzymatic activity. 1
    Mutagenesisi127N → D: 50% decrease in enzymatic activity. 1
    Mutagenesisi138C → S, A or G: No effect on enzymatic activity. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00000688281 – 164Magnesium-dependent phosphatase 1Add BLAST164

    Proteomic databases

    EPDiQ9D967.
    MaxQBiQ9D967.
    PaxDbiQ9D967.
    PeptideAtlasiQ9D967.
    PRIDEiQ9D967.

    PTM databases

    PhosphoSitePlusiQ9D967.

    Expressioni

    Gene expression databases

    BgeeiENSMUSG00000002329.
    CleanExiMM_1810034K20RIK.
    GenevisibleiQ9D967. MM.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9D967. 1 interactor.
    MINTiMINT-4127783.
    STRINGi10090.ENSMUSP00000002400.

    Structurei

    Secondary structure

    1164
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi6 – 10Combined sources5
    Turni13 – 15Combined sources3
    Beta strandi16 – 19Combined sources4
    Turni21 – 23Combined sources3
    Beta strandi29 – 31Combined sources3
    Beta strandi37 – 39Combined sources3
    Helixi51 – 60Combined sources10
    Beta strandi65 – 69Combined sources5
    Helixi74 – 83Combined sources10
    Helixi87 – 89Combined sources3
    Beta strandi90 – 98Combined sources9
    Helixi100 – 111Combined sources12
    Helixi115 – 117Combined sources3
    Beta strandi118 – 123Combined sources6
    Helixi125 – 132Combined sources8
    Turni133 – 135Combined sources3
    Beta strandi137 – 140Combined sources4
    Beta strandi142 – 144Combined sources3
    Helixi147 – 160Combined sources14
    Turni161 – 163Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U7OX-ray1.90A1-164[»]
    1U7PX-ray1.90A/B/C/D1-164[»]
    ProteinModelPortaliQ9D967.
    SMRiQ9D967.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9D967.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAD-like hydrolase superfamily.Curated

    Phylogenomic databases

    eggNOGiKOG4549. Eukaryota.
    ENOG4111PHW. LUCA.
    GeneTreeiENSGT00390000004110.
    HOGENOMiHOG000216653.
    HOVERGENiHBG081971.
    InParanoidiQ9D967.
    KOiK17619.
    OMAiHVQNGMS.
    OrthoDBiEOG091G0SQ5.
    PhylomeDBiQ9D967.
    TreeFamiTF328413.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR010033. HAD_SF_ppase_IIIC.
    IPR024734. MDP_1_eu.
    IPR010036. MDP_1_eu_arc.
    [Graphical view]
    PANTHERiPTHR17901. PTHR17901. 1 hit.
    PfamiPF12689. Acid_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01681. HAD-SF-IIIC. 1 hit.
    TIGR01685. MDP-1. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9D967-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MTRLPKLAVF DLDYTLWPFW VDTHVDPPFH KSSDGTVRDR RGQNIQLYPE
    60 70 80 90 100
    VPEVLGRLQS LGVPVAAASR TSEIQGANQL LELFDLGKYF IQREIYPGSK
    110 120 130 140 150
    VTHFERLHHK TGVPFSQMVF FDDENRNIID VGRLGVTCIH IRDGMSLQTL
    160
    TQGLETFAKA QAGL
    Length:164
    Mass (Da):18,582
    Last modified:June 1, 2001 - v1
    Checksum:i209D39404DCB1930
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF230273 mRNA. Translation: AAK00763.1.
    AK007319 mRNA. Translation: BAB24954.1.
    AK160438 mRNA. Translation: BAE35788.1.
    BC046613 mRNA. Translation: AAH46613.1.
    CCDSiCCDS27123.1.
    RefSeqiNP_075886.1. NM_023397.4.
    UniGeneiMm.24601.

    Genome annotation databases

    EnsembliENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
    GeneIDi67881.
    KEGGimmu:67881.
    UCSCiuc007uaa.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF230273 mRNA. Translation: AAK00763.1.
    AK007319 mRNA. Translation: BAB24954.1.
    AK160438 mRNA. Translation: BAE35788.1.
    BC046613 mRNA. Translation: AAH46613.1.
    CCDSiCCDS27123.1.
    RefSeqiNP_075886.1. NM_023397.4.
    UniGeneiMm.24601.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    1U7OX-ray1.90A1-164[»]
    1U7PX-ray1.90A/B/C/D1-164[»]
    ProteinModelPortaliQ9D967.
    SMRiQ9D967.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    IntActiQ9D967. 1 interactor.
    MINTiMINT-4127783.
    STRINGi10090.ENSMUSP00000002400.

    PTM databases

    PhosphoSitePlusiQ9D967.

    Proteomic databases

    EPDiQ9D967.
    MaxQBiQ9D967.
    PaxDbiQ9D967.
    PeptideAtlasiQ9D967.
    PRIDEiQ9D967.

    Protocols and materials databases

    DNASUi67881.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000002400; ENSMUSP00000002400; ENSMUSG00000002329.
    GeneIDi67881.
    KEGGimmu:67881.
    UCSCiuc007uaa.2. mouse.

    Organism-specific databases

    CTDi145553.
    MGIiMGI:1915131. Mdp1.

    Phylogenomic databases

    eggNOGiKOG4549. Eukaryota.
    ENOG4111PHW. LUCA.
    GeneTreeiENSGT00390000004110.
    HOGENOMiHOG000216653.
    HOVERGENiHBG081971.
    InParanoidiQ9D967.
    KOiK17619.
    OMAiHVQNGMS.
    OrthoDBiEOG091G0SQ5.
    PhylomeDBiQ9D967.
    TreeFamiTF328413.

    Miscellaneous databases

    ChiTaRSiMdp1. mouse.
    EvolutionaryTraceiQ9D967.
    PROiQ9D967.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000002329.
    CleanExiMM_1810034K20RIK.
    GenevisibleiQ9D967. MM.

    Family and domain databases

    Gene3Di3.40.50.1000. 1 hit.
    InterProiIPR023214. HAD-like_dom.
    IPR010033. HAD_SF_ppase_IIIC.
    IPR024734. MDP_1_eu.
    IPR010036. MDP_1_eu_arc.
    [Graphical view]
    PANTHERiPTHR17901. PTHR17901. 1 hit.
    PfamiPF12689. Acid_PPase. 1 hit.
    [Graphical view]
    SUPFAMiSSF56784. SSF56784. 1 hit.
    TIGRFAMsiTIGR01681. HAD-SF-IIIC. 1 hit.
    TIGR01685. MDP-1. 1 hit.
    ProtoNetiSearch...

    Entry informationi

    Entry nameiMGDP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9D967
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 25, 2005
    Last sequence update: June 1, 2001
    Last modified: November 2, 2016
    This is version 108 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, 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

    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.