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Q9DAR7 (DCPS_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Dcps
Synonyms:Dcs1, Hint5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

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

Subcellular location

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.

Domain

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.

Sequence similarities

Belongs to the HIT family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 338337m7GpppX diphosphatase
PRO_0000109795

Regions

Region267 – 27812Substrate binding By similarity
Motif9 – 124nuclear localization signal (NLS) By similarity
Motif141 – 15313nuclear export sequence (NES) By similarity
Motif274 – 2785Histidine triad motif By similarity

Sites

Active site2761Nucleophile By similarity
Binding site1741Substrate By similarity
Binding site1841Substrate By similarity
Binding site2041Substrate By similarity
Binding site2061Substrate By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue1371N6-acetyllysine Ref.5
Modified residue1411N6-acetyllysine By similarity

Experimental info

Sequence conflict1411K → E in BAC37194. Ref.2

Secondary structure

........................................................... 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9DAR7 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: A9520CBE48293DFC

FASTA33838,988
        10         20         30         40         50         60 
MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK VLRESARDKI 

        70         80         90        100        110        120 
IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGS PELKLQFSND IYSTYNLFPP 

       130        140        150        160        170        180 
RHLSDIKTTV VYPATEKHLQ KYMRQDLRLI RETGDDYRTI TLPYLESQSL SIQWVYNILD 

       190        200        210        220        230        240 
KKAEADRIVF ENPDPSDGFV LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL 

       250        260        270        280        290        300 
RNILREGQEA ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAQV 

       310        320        330 
IENLECDPKH YQQRTLTFAL RTDDPLLQLL QKAQQERN 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
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).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY040775 mRNA. Translation: AAK91764.1.
AK005584 mRNA. Translation: BAB24138.1.
AK078253 mRNA. Translation: BAC37194.1.
BC016273 mRNA. Translation: AAH16273.1.
CCDSCCDS22957.1.
RefSeqNP_081306.1. NM_027030.2.
UniGeneMm.229110.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1VLRX-ray1.83A/B1-338[»]
ProteinModelPortalQ9DAR7.
SMRQ9DAR7. Positions 39-337.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DAR7. 1 interaction.
MINTMINT-4092914.

PTM databases

PhosphoSiteQ9DAR7.

Proteomic databases

MaxQBQ9DAR7.
PaxDbQ9DAR7.
PRIDEQ9DAR7.

Protocols and materials databases

DNASU69305.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000034539; ENSMUSP00000034539; ENSMUSG00000032040.
GeneID69305.
KEGGmmu:69305.
UCSCuc009osp.1. mouse.

Organism-specific databases

CTD28960.
MGIMGI:1916555. Dcps.

Phylogenomic databases

eggNOGCOG5075.
GeneTreeENSGT00390000003924.
HOGENOMHOG000182411.
HOVERGENHBG051322.
InParanoidQ9DAR7.
KOK12584.
OMAGENHGLW.
OrthoDBEOG7QNVMZ.
PhylomeDBQ9DAR7.
TreeFamTF105622.

Gene expression databases

ArrayExpressQ9DAR7.
BgeeQ9DAR7.
CleanExMM_DCPS.
GenevestigatorQ9DAR7.

Family and domain databases

Gene3D3.30.428.10. 1 hit.
InterProIPR008594. DcpS/DCS2.
IPR019808. Histidine_triad_CS.
IPR011146. HIT-like.
IPR011145. Scavenger_mRNA_decap_enz_N.
[Graphical view]
PANTHERPTHR12978. PTHR12978. 1 hit.
PfamPF05652. DcpS. 1 hit.
[Graphical view]
PIRSFPIRSF028973. Scavenger_mRNA_decap_enz. 1 hit.
SUPFAMSSF102860. SSF102860. 1 hit.
SSF54197. SSF54197. 1 hit.
PROSITEPS00892. HIT_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9DAR7.
NextBio329076.
PROQ9DAR7.
SOURCESearch...

Entry information

Entry nameDCPS_MOUSE
AccessionPrimary (citable) accession number: Q9DAR7
Secondary accession number(s): Q8C5I7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot