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Q9DAR7

- DCPS_MOUSE

UniProt

Q9DAR7 - DCPS_MOUSE

Protein

m7GpppX diphosphatase

Gene

Dcps

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 102 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP. Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death By similarity.By similarity

    Catalytic activityi

    A 5'-(N(7)-methyl 5'-triphosphoguanosine)-(mRNA) + H2O = N(7)-methylguanosine 5'-phosphate + a 5'-diphospho-(mRNA).

    Enzyme regulationi

    The hydrolytic product 7-methylguanosine diphosphate (m7GDP) efficiently inhibits the decapping scavenger activity and acts as a competitive inhibitor in vitro. Inhibited by 2,4-diaminoquinazoline By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei174 – 1741SubstrateBy similarity
    Binding sitei184 – 1841SubstrateBy similarity
    Binding sitei204 – 2041SubstrateBy similarity
    Binding sitei206 – 2061SubstrateBy similarity
    Active sitei276 – 2761NucleophileBy similarity

    GO - Molecular functioni

    1. m7G(5')pppN diphosphatase activity Source: UniProtKB
    2. RNA 7-methylguanosine cap binding Source: UniProtKB

    GO - Biological processi

    1. cellular response to menadione Source: UniProtKB
    2. deadenylation-dependent decapping of nuclear-transcribed mRNA Source: InterPro
    3. mRNA cis splicing, via spliceosome Source: UniProtKB
    4. negative regulation of programmed cell death Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    m7GpppX diphosphatase (EC:3.6.1.59)
    Alternative name(s):
    DCS-1
    Decapping scavenger enzyme
    Hint-related 7meGMP-directed hydrolase
    Histidine triad nucleotide-binding protein 5
    Histidine triad protein member 5
    Short name:
    HINT-5
    Scavenger mRNA-decapping enzyme DcpS
    Gene namesi
    Name:Dcps
    Synonyms:Dcs1, Hint5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:1916555. Dcps.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity
    Note: Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. mitochondrion Source: Ensembl
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 338337m7GpppX diphosphatasePRO_0000109795Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei137 – 1371N6-acetyllysine1 Publication
    Modified residuei141 – 1411N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9DAR7.
    PaxDbiQ9DAR7.
    PRIDEiQ9DAR7.

    PTM databases

    PhosphoSiteiQ9DAR7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DAR7.
    BgeeiQ9DAR7.
    CleanExiMM_DCPS.
    GenevestigatoriQ9DAR7.

    Interactioni

    Subunit structurei

    Homodimer. Associates with components of the exosome multienzyme ribonuclease complex, such as EXOSC3 and EXOSC4. Interacts with NDOR1 By similarity.By similarity

    Protein-protein interaction databases

    IntActiQ9DAR7. 1 interaction.
    MINTiMINT-4092914.

    Structurei

    Secondary structure

    1
    338
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi42 – 443
    Beta strandi47 – 559
    Turni56 – 594
    Beta strandi60 – 678
    Beta strandi77 – 859
    Helixi90 – 978
    Beta strandi102 – 1087
    Beta strandi110 – 1189
    Helixi121 – 1244
    Beta strandi126 – 1338
    Helixi136 – 1427
    Beta strandi147 – 1526
    Helixi154 – 1596
    Helixi161 – 1688
    Helixi173 – 1797
    Beta strandi189 – 1924
    Turni195 – 1973
    Beta strandi199 – 2035
    Beta strandi216 – 2249
    Helixi229 – 2313
    Helixi234 – 2363
    Helixi237 – 25519
    Helixi259 – 2613
    Beta strandi262 – 2698
    Beta strandi271 – 2744
    Beta strandi276 – 2816
    Turni291 – 2933
    Beta strandi294 – 2963
    Helixi297 – 30610
    Helixi310 – 3134
    Beta strandi316 – 3216
    Helixi325 – 33612

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1VLRX-ray1.83A/B1-338[»]
    ProteinModelPortaliQ9DAR7.
    SMRiQ9DAR7. Positions 39-337.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9DAR7.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni267 – 27812Substrate bindingBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi9 – 124nuclear localization signal (NLS)By similarity
    Motifi141 – 15313nuclear export sequence (NES)By similarityAdd
    BLAST
    Motifi274 – 2785Histidine triad motifBy similarity

    Domaini

    The C-terminal histidine triad (HIT) motif and the N-terminal domain are required for the decapping activity. The N-terminus is necessary but not sufficient for binding cap structures By similarity.By similarity

    Sequence similaritiesi

    Belongs to the HIT family.Curated

    Phylogenomic databases

    eggNOGiCOG5075.
    GeneTreeiENSGT00390000003924.
    HOGENOMiHOG000182411.
    HOVERGENiHBG051322.
    InParanoidiQ9DAR7.
    KOiK12584.
    OMAiGENHGLW.
    OrthoDBiEOG7QNVMZ.
    PhylomeDBiQ9DAR7.
    TreeFamiTF105622.

    Family and domain databases

    Gene3Di3.30.428.10. 1 hit.
    InterProiIPR008594. DcpS/DCS2.
    IPR019808. Histidine_triad_CS.
    IPR011146. HIT-like.
    IPR011145. Scavenger_mRNA_decap_enz_N.
    [Graphical view]
    PANTHERiPTHR12978. PTHR12978. 1 hit.
    PfamiPF05652. DcpS. 1 hit.
    [Graphical view]
    PIRSFiPIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
    SUPFAMiSSF102860. SSF102860. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEiPS00892. HIT_1. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9DAR7-1 [UniParc]FASTAAdd to Basket

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    MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK    50
    VLRESARDKI IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGS 100
    PELKLQFSND IYSTYNLFPP RHLSDIKTTV VYPATEKHLQ KYMRQDLRLI 150
    RETGDDYRTI TLPYLESQSL SIQWVYNILD KKAEADRIVF ENPDPSDGFV 200
    LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL RNILREGQEA 250
    ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAQV 300
    IENLECDPKH YQQRTLTFAL RTDDPLLQLL QKAQQERN 338
    Length:338
    Mass (Da):38,988
    Last modified:June 1, 2001 - v1
    Checksum:iA9520CBE48293DFC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti141 – 1411K → E in BAC37194. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040775 mRNA. Translation: AAK91764.1.
    AK005584 mRNA. Translation: BAB24138.1.
    AK078253 mRNA. Translation: BAC37194.1.
    BC016273 mRNA. Translation: AAH16273.1.
    CCDSiCCDS22957.1.
    RefSeqiNP_081306.1. NM_027030.2.
    UniGeneiMm.229110.

    Genome annotation databases

    EnsembliENSMUST00000034539; ENSMUSP00000034539; ENSMUSG00000032040.
    GeneIDi69305.
    KEGGimmu:69305.
    UCSCiuc009osp.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY040775 mRNA. Translation: AAK91764.1 .
    AK005584 mRNA. Translation: BAB24138.1 .
    AK078253 mRNA. Translation: BAC37194.1 .
    BC016273 mRNA. Translation: AAH16273.1 .
    CCDSi CCDS22957.1.
    RefSeqi NP_081306.1. NM_027030.2.
    UniGenei Mm.229110.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1VLR X-ray 1.83 A/B 1-338 [» ]
    ProteinModelPortali Q9DAR7.
    SMRi Q9DAR7. Positions 39-337.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9DAR7. 1 interaction.
    MINTi MINT-4092914.

    PTM databases

    PhosphoSitei Q9DAR7.

    Proteomic databases

    MaxQBi Q9DAR7.
    PaxDbi Q9DAR7.
    PRIDEi Q9DAR7.

    Protocols and materials databases

    DNASUi 69305.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000034539 ; ENSMUSP00000034539 ; ENSMUSG00000032040 .
    GeneIDi 69305.
    KEGGi mmu:69305.
    UCSCi uc009osp.1. mouse.

    Organism-specific databases

    CTDi 28960.
    MGIi MGI:1916555. Dcps.

    Phylogenomic databases

    eggNOGi COG5075.
    GeneTreei ENSGT00390000003924.
    HOGENOMi HOG000182411.
    HOVERGENi HBG051322.
    InParanoidi Q9DAR7.
    KOi K12584.
    OMAi GENHGLW.
    OrthoDBi EOG7QNVMZ.
    PhylomeDBi Q9DAR7.
    TreeFami TF105622.

    Miscellaneous databases

    EvolutionaryTracei Q9DAR7.
    NextBioi 329076.
    PROi Q9DAR7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DAR7.
    Bgeei Q9DAR7.
    CleanExi MM_DCPS.
    Genevestigatori Q9DAR7.

    Family and domain databases

    Gene3Di 3.30.428.10. 1 hit.
    InterProi IPR008594. DcpS/DCS2.
    IPR019808. Histidine_triad_CS.
    IPR011146. HIT-like.
    IPR011145. Scavenger_mRNA_decap_enz_N.
    [Graphical view ]
    PANTHERi PTHR12978. PTHR12978. 1 hit.
    Pfami PF05652. DcpS. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
    SUPFAMi SSF102860. SSF102860. 1 hit.
    SSF54197. SSF54197. 1 hit.
    PROSITEi PS00892. HIT_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of a novel member of the histidine triad protein family (HINT-5) in different vertebrate species."
      Huang C.-H., Peng J., Chen H., Chen Y.
      Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: BALB/c.
      Tissue: Brain.
    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: Olfactory bulb and Testis.
    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].
      Strain: C57BL/6.
      Tissue: Eye.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    5. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
      Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
      Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-137, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    6. "Crystal structure of mRNA decapping enzyme (DCPS) from Mus musculus at 1.83 A resolution."
      Joint center for structural genomics (JCSG)
      Submitted (AUG-2004) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS).

    Entry informationi

    Entry nameiDCPS_MOUSE
    AccessioniPrimary (citable) accession number: Q9DAR7
    Secondary accession number(s): Q8C5I7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2005
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 102 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