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Protein

dCTP pyrophosphatase 1

Gene

Dctpp1

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

Functioni

Hydrolyzes deoxynucleoside triphosphates (dNTPs) to the corresponding nucleoside monophosphates. Has a strong preference for modified dCTP. Activity is highest with 5-iodo-dCTP, followed by 5-bromo-dCTP, unmodified dCTP, 5-methyl-dCTP and 5-chloro-dCTP. Hydrolyzes 2-chloro-dATP and 2-hydroxy-dATP with lower efficiency, and has even lower activity with unmodified dATP, dTTP and dUTP (in vitro). Does not hydrolyze ATP, UTP, ITP, GTP, dADP, dCDP or dGTP. May protect DNA or RNA against the incorporation of non-canonical nucleotide triphosphates. May protect cells against inappropriate methylation of CpG islands by DNA methyltransferases.2 Publications

Catalytic activityi

dCTP + H2O = dCMP + diphosphate.2 Publications

Cofactori

Mg2+1 PublicationNote: Probably binds two or three Mg2+ ions per subunit.1 Publication

Enzyme regulationi

Inhibited by divalent calcium or cadmium ions.

Kineticsi

  1. KM=0.16 mM for 5-methyl-dCTP (at pH 9.0)2 Publications
  2. KM=44 µM for dCTP (at pH 8.0)2 Publications
  3. KM=118 µM for dATP (at pH 8.0)2 Publications
  4. KM=407 µM for dTTP (at pH 8.0)2 Publications
  5. KM=529 µM for CTP (at pH 8.0)2 Publications
  6. KM=3.9 µM for 5-iodo-dCTP (at pH 8.0)2 Publications
  7. KM=21.7 µM for 5-bromo-dCTP (at pH 8.0)2 Publications
  8. KM=48.5 µM for 5-methyl-dCTP (at pH 8.0)2 Publications
  9. KM=50 µM for 5-chloro-dCTP (at pH 8.0)2 Publications

    pH dependencei

    Optimum pH is 9-9.5.2 Publications

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.2 Publications

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei38Substrate1
    Metal bindingi63MagnesiumCurated1
    Metal bindingi66MagnesiumCurated1
    Binding sitei73Substrate1
    Metal bindingi95MagnesiumCurated1
    Metal bindingi98MagnesiumCurated1
    Binding sitei102Substrate1

    GO - Molecular functioni

    • dCTP diphosphatase activity Source: Reactome
    • identical protein binding Source: MGI
    • magnesium ion binding Source: UniProtKB
    • nucleoside-triphosphate diphosphatase activity Source: UniProtKB
    • pyrimidine deoxyribonucleotide binding Source: MGI
    • pyrophosphatase activity Source: MGI

    GO - Biological processi

    • nucleobase-containing small molecule interconversion Source: Reactome
    • nucleoside triphosphate catabolic process Source: UniProtKB
    • protein homotetramerization Source: MGI
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Ligandi

    Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17900.
    BRENDAi3.6.1.12. 3474.
    ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    dCTP pyrophosphatase 1 (EC:3.6.1.12)
    Alternative name(s):
    Deoxycytidine-triphosphatase 1
    Short name:
    dCTPase 1
    RS21-C6
    XTP3-transactivated gene A protein homolog
    Gene namesi
    Name:Dctpp1
    Synonyms:Tdrg-TL1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    Proteomesi
    • UP000000589 Componenti: Chromosome 7

    Organism-specific databases

    MGIiMGI:1913672. Dctpp1.

    Subcellular locationi

    • Cytoplasm 1 Publication

    GO - Cellular componenti

    • cytosol Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi38H → A: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication1
    Mutagenesisi47W → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication1
    Mutagenesisi63E → Q: Loss of activity. 1 Publication1
    Mutagenesisi66E → Q: Loss of activity. 1 Publication1
    Mutagenesisi73W → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication1
    Mutagenesisi95E → Q: Loss of activity. 1 Publication1
    Mutagenesisi98D → N: Loss of activity. 1 Publication1
    Mutagenesisi102Y → I: Reduces affinity for substrate and catalytic activity by about 50%. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Initiator methionineiRemovedBy similarity
    ChainiPRO_00002917702 – 170dCTP pyrophosphatase 1Add BLAST169

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei2N-acetylserineBy similarity1
    Modified residuei2PhosphoserineBy similarity1

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    EPDiQ9QY93.
    MaxQBiQ9QY93.
    PaxDbiQ9QY93.
    PeptideAtlasiQ9QY93.
    PRIDEiQ9QY93.

    PTM databases

    PhosphoSitePlusiQ9QY93.
    SwissPalmiQ9QY93.

    Expressioni

    Tissue specificityi

    Ubiquitous. Highly expressed in heart, liver, skeletal muscle, cerebellum, brain, and salivary gland.1 Publication

    Gene expression databases

    BgeeiENSMUSG00000042462.
    CleanExiMM_2410015N17RIK.
    GenevisibleiQ9QY93. MM.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    GO - Molecular functioni

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000047845.

    Structurei

    Secondary structure

    1170
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi31 – 43Combined sources13
    Turni44 – 46Combined sources3
    Helixi48 – 50Combined sources3
    Helixi53 – 72Combined sources20
    Beta strandi76 – 78Combined sources3
    Helixi81 – 83Combined sources3
    Helixi86 – 109Combined sources24
    Helixi114 – 119Combined sources6
    Turni120 – 122Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2A3QX-ray2.32A/B1-170[»]
    2OIEX-ray2.20A/B/C/D21-126[»]
    2OIGX-ray3.30A/B/C/D21-126[»]
    2Q4PX-ray2.32A/B1-170[»]
    ProteinModelPortaliQ9QY93.
    SMRiQ9QY93.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9QY93.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Repeati29 – 75EARAdd BLAST47

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni47 – 51Substrate binding5

    Sequence similaritiesi

    Contains 1 EAR repeat.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiENOG410IXWQ. Eukaryota.
    ENOG4111PYX. LUCA.
    GeneTreeiENSGT00390000017709.
    HOGENOMiHOG000056700.
    InParanoidiQ9QY93.
    KOiK16904.
    OMAiWKTDGEP.
    OrthoDBiEOG091G0RYZ.
    PhylomeDBiQ9QY93.
    TreeFamiTF300237.

    Family and domain databases

    CDDicd11537. NTP-PPase_RS21-C6_like. 1 hit.
    InterProiIPR025984. DCTPP.
    IPR009039. EAR.
    [Graphical view]
    PfamiPF12643. MazG-like. 1 hit.
    [Graphical view]
    PROSITEiPS50912. EAR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q9QY93-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSTAGDGERG TVGQEDSAAA RPFRFSPEPT LEDIRRLHAE FAAERDWEQF
    60 70 80 90 100
    HQPRNLLLAL VGEVGELAEL FQWKSDTEPG PQAWPPKERA ALQEELSDVL
    110 120 130 140 150
    IYLVALAARC HVDLPQAVIS KMDTNRQRYP VHLSRGSACK YTDLPRGTIS
    160 170
    ENQAVGAGDP ASELRDQAST
    Length:170
    Mass (Da):18,795
    Last modified:May 1, 2000 - v1
    Checksum:iA20ECDA7857446A3
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF110764 mRNA. Translation: AAF15970.1.
    AK003643 mRNA. Translation: BAB22909.1.
    AK010508 mRNA. Translation: BAB26992.1.
    AK010606 mRNA. Translation: BAB27056.1.
    BC004623 mRNA. Translation: AAH04623.1.
    CCDSiCCDS21862.1.
    RefSeqiNP_075692.1. NM_023203.1.
    UniGeneiMm.29898.

    Genome annotation databases

    EnsembliENSMUST00000035276; ENSMUSP00000047845; ENSMUSG00000042462.
    GeneIDi66422.
    KEGGimmu:66422.
    UCSCiuc009juw.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF110764 mRNA. Translation: AAF15970.1.
    AK003643 mRNA. Translation: BAB22909.1.
    AK010508 mRNA. Translation: BAB26992.1.
    AK010606 mRNA. Translation: BAB27056.1.
    BC004623 mRNA. Translation: AAH04623.1.
    CCDSiCCDS21862.1.
    RefSeqiNP_075692.1. NM_023203.1.
    UniGeneiMm.29898.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2A3QX-ray2.32A/B1-170[»]
    2OIEX-ray2.20A/B/C/D21-126[»]
    2OIGX-ray3.30A/B/C/D21-126[»]
    2Q4PX-ray2.32A/B1-170[»]
    ProteinModelPortaliQ9QY93.
    SMRiQ9QY93.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000047845.

    PTM databases

    PhosphoSitePlusiQ9QY93.
    SwissPalmiQ9QY93.

    Proteomic databases

    EPDiQ9QY93.
    MaxQBiQ9QY93.
    PaxDbiQ9QY93.
    PeptideAtlasiQ9QY93.
    PRIDEiQ9QY93.

    Protocols and materials databases

    DNASUi66422.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENSMUST00000035276; ENSMUSP00000047845; ENSMUSG00000042462.
    GeneIDi66422.
    KEGGimmu:66422.
    UCSCiuc009juw.2. mouse.

    Organism-specific databases

    CTDi79077.
    MGIiMGI:1913672. Dctpp1.

    Phylogenomic databases

    eggNOGiENOG410IXWQ. Eukaryota.
    ENOG4111PYX. LUCA.
    GeneTreeiENSGT00390000017709.
    HOGENOMiHOG000056700.
    InParanoidiQ9QY93.
    KOiK16904.
    OMAiWKTDGEP.
    OrthoDBiEOG091G0RYZ.
    PhylomeDBiQ9QY93.
    TreeFamiTF300237.

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-17900.
    BRENDAi3.6.1.12. 3474.
    ReactomeiR-MMU-499943. Synthesis and interconversion of nucleotide di- and triphosphates.

    Miscellaneous databases

    EvolutionaryTraceiQ9QY93.
    PROiQ9QY93.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSMUSG00000042462.
    CleanExiMM_2410015N17RIK.
    GenevisibleiQ9QY93. MM.

    Family and domain databases

    CDDicd11537. NTP-PPase_RS21-C6_like. 1 hit.
    InterProiIPR025984. DCTPP.
    IPR009039. EAR.
    [Graphical view]
    PfamiPF12643. MazG-like. 1 hit.
    [Graphical view]
    PROSITEiPS50912. EAR. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiDCTP1_MOUSE
    AccessioniPrimary (citable) accession number: Q9QY93
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: May 1, 2000
    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.