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Protein

m7GpppX diphosphatase

Gene

Dcps

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

mRNA processing, mRNA splicing

Enzyme and pathway databases

BRENDAi3.6.1.59. 3474.
ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.

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 Componenti: 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

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.
GenevisibleiQ9DAR7. MM.

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.
STRINGi10090.ENSMUSP00000034539.

Structurei

Secondary structure

1
338
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Beta strandi47 – 559Combined sources
Turni56 – 594Combined sources
Beta strandi60 – 678Combined sources
Beta strandi77 – 859Combined sources
Helixi90 – 978Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi110 – 1189Combined sources
Helixi121 – 1244Combined sources
Beta strandi126 – 1338Combined sources
Helixi136 – 1427Combined sources
Beta strandi147 – 1526Combined sources
Helixi154 – 1596Combined sources
Helixi161 – 1688Combined sources
Helixi173 – 1797Combined sources
Beta strandi182 – 1843Combined sources
Beta strandi189 – 1924Combined sources
Turni195 – 1973Combined sources
Beta strandi199 – 2035Combined sources
Beta strandi216 – 2249Combined sources
Helixi229 – 2313Combined sources
Helixi234 – 2363Combined sources
Helixi237 – 25519Combined sources
Helixi259 – 2613Combined sources
Beta strandi262 – 2698Combined sources
Beta strandi271 – 2744Combined sources
Beta strandi276 – 2816Combined sources
Turni291 – 2933Combined sources
Beta strandi294 – 2963Combined sources
Helixi297 – 30610Combined sources
Helixi310 – 3134Combined sources
Beta strandi316 – 3216Combined sources
Helixi325 – 33612Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiYKNVTLP.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9DAR7. 1 interaction.
MINTiMINT-4092914.
STRINGi10090.ENSMUSP00000034539.

PTM databases

PhosphoSiteiQ9DAR7.

Proteomic databases

MaxQBiQ9DAR7.
PaxDbiQ9DAR7.
PRIDEiQ9DAR7.

Protocols and materials databases

DNASUi69305.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi28960.
MGIiMGI:1916555. Dcps.

Phylogenomic databases

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

Enzyme and pathway databases

BRENDAi3.6.1.59. 3474.
ReactomeiREACT_291652. mRNA decay by 3' to 5' exoribonuclease.

Miscellaneous databases

EvolutionaryTraceiQ9DAR7.
NextBioi329076.
PROiQ9DAR7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DAR7.
CleanExiMM_DCPS.
ExpressionAtlasiQ9DAR7. baseline and differential.
GenevisibleiQ9DAR7. MM.

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]
ProtoNetiSearch...

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: June 24, 2015
This is version 109 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.