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Q9DAR7

- DCPS_MOUSE

UniProt

Q9DAR7 - DCPS_MOUSE

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Protein

m7GpppX diphosphatase

Gene

Dcps

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiQ9DAR7.
CleanExiMM_DCPS.
ExpressionAtlasiQ9DAR7. baseline and differential.
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

« Hide

        10         20         30         40         50
MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK
60 70 80 90 100
VLRESARDKI IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGS
110 120 130 140 150
PELKLQFSND IYSTYNLFPP RHLSDIKTTV VYPATEKHLQ KYMRQDLRLI
160 170 180 190 200
RETGDDYRTI TLPYLESQSL SIQWVYNILD KKAEADRIVF ENPDPSDGFV
210 220 230 240 250
LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL RNILREGQEA
260 270 280 290 300
ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAQV
310 320 330
IENLECDPKH YQQRTLTFAL RTDDPLLQLL QKAQQERN
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

Bgeei Q9DAR7.
CleanExi MM_DCPS.
ExpressionAtlasi Q9DAR7. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 103 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