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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)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei11 – 111NucleophileCurated
    Metal bindingi11 – 111Magnesium
    Binding sitei12 – 121Phosphate; via amide nitrogen
    Active sitei13 – 131Proton donorCurated
    Metal bindingi13 – 131Magnesium
    Binding sitei13 – 131Phosphate; via amide nitrogen
    Binding sitei20 – 201SubstrateCurated
    Binding sitei69 – 691Phosphate
    Binding sitei70 – 701Phosphate
    Binding sitei70 – 701SubstrateCurated
    Binding sitei100 – 1001Phosphate
    Metal bindingi123 – 1231Magnesium

    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
    ProteomesiUP000000589 Componenti: Chromosome 14

    Organism-specific databases

    MGIiMGI:1915131. Mdp1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi11 – 111D → N or E: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi13 – 131D → N: 92% loss of enzymatic activity. 1 Publication
    Mutagenesisi69 – 691S → A: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi100 – 1001K → R: Abolishes enzymatic activity. 1 Publication
    Mutagenesisi103 – 1031H → K or A: 50% decrease in enzymatic activity. 1 Publication
    Mutagenesisi122 – 1221D → N: Abolishes enzymatic activity.
    Mutagenesisi123 – 1231D → N: Abolishes enzymatic activity.
    Mutagenesisi127 – 1271N → D: 50% decrease in enzymatic activity.
    Mutagenesisi138 – 1381C → S, A or G: No effect on enzymatic activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 164164Magnesium-dependent phosphatase 1PRO_0000068828Add
    BLAST

    Proteomic databases

    MaxQBiQ9D967.
    PaxDbiQ9D967.
    PRIDEiQ9D967.

    PTM databases

    PhosphoSiteiQ9D967.

    Expressioni

    Gene expression databases

    BgeeiQ9D967.
    CleanExiMM_1810034K20RIK.
    GenevisibleiQ9D967. MM.

    Interactioni

    Protein-protein interaction databases

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

    Structurei

    Secondary structure

    1
    164
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 105Combined sources
    Turni13 – 153Combined sources
    Beta strandi16 – 194Combined sources
    Turni21 – 233Combined sources
    Beta strandi29 – 313Combined sources
    Beta strandi37 – 393Combined sources
    Helixi51 – 6010Combined sources
    Beta strandi65 – 695Combined sources
    Helixi74 – 8310Combined sources
    Helixi87 – 893Combined sources
    Beta strandi90 – 989Combined sources
    Helixi100 – 11112Combined sources
    Helixi115 – 1173Combined sources
    Beta strandi118 – 1236Combined sources
    Helixi125 – 1328Combined sources
    Turni133 – 1353Combined sources
    Beta strandi137 – 1404Combined sources
    Beta strandi142 – 1443Combined sources
    Helixi147 – 16014Combined sources
    Turni161 – 1633Combined sources

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiQ9D967.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the HAD-like hydrolase superfamily.Curated

    Phylogenomic databases

    eggNOGiNOG279690.
    GeneTreeiENSGT00390000004110.
    HOGENOMiHOG000216653.
    HOVERGENiHBG081971.
    InParanoidiQ9D967.
    KOiK17619.
    OMAiHVQNGMS.
    OrthoDBiEOG7PK913.
    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
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1U7OX-ray1.90A1-164[»]
    1U7PX-ray1.90A/B/C/D1-164[»]
    ProteinModelPortaliQ9D967.
    SMRiQ9D967. Positions 1-164.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

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

    PTM databases

    PhosphoSiteiQ9D967.

    Proteomic databases

    MaxQBiQ9D967.
    PaxDbiQ9D967.
    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

    eggNOGiNOG279690.
    GeneTreeiENSGT00390000004110.
    HOGENOMiHOG000216653.
    HOVERGENiHBG081971.
    InParanoidiQ9D967.
    KOiK17619.
    OMAiHVQNGMS.
    OrthoDBiEOG7PK913.
    PhylomeDBiQ9D967.
    TreeFamiTF328413.

    Miscellaneous databases

    ChiTaRSiMdp1. mouse.
    EvolutionaryTraceiQ9D967.
    NextBioi325825.
    PROiQ9D967.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9D967.
    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...

    Publicationsi

    « Hide 'large scale' publications
    1. "MDP-1: a novel eukaryotic magnesium-dependent phosphatase."
      Selengut J.D., Levine R.L.
      Biochemistry 39:8315-8324(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION, MUTAGENESIS OF HIS-103 AND CYS-138.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Pancreas.
    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].
      Tissue: Eye.
    4. "MDP-1 is a new and distinct member of the haloacid dehalogenase family of aspartate-dependent phosphohydrolases."
      Selengut J.D.
      Biochemistry 40:12704-12711(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-11; ASP-13; SER-69 AND LYS-100, FUNCTION.
    5. "X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily."
      Peisach E., Selengut J.D., Dunaway-Mariano D., Allen K.N.
      Biochemistry 43:12770-12779(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164, X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-164 WITH MAGNESIUM AND TUNGSTATE, FUNCTION.

    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: June 24, 2015
    This is version 100 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

    External Data

    Dasty 3

    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 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.