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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

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei174SubstrateBy similarity1
Binding sitei184SubstrateBy similarity1
Binding sitei204SubstrateBy similarity1
Binding sitei206SubstrateBy similarity1
Active sitei276NucleophileBy similarity1

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.
ReactomeiR-MMU-429958. 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
Proteomesi
  • UP000000589 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

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00001097952 – 338m7GpppX diphosphataseAdd BLAST337

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineBy similarity1
Modified residuei23PhosphoserineBy similarity1
Modified residuei100PhosphoserineCombined sources1
Modified residuei137N6-acetyllysineCombined sources1
Modified residuei141N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9DAR7.
MaxQBiQ9DAR7.
PaxDbiQ9DAR7.
PeptideAtlasiQ9DAR7.
PRIDEiQ9DAR7.

PTM databases

iPTMnetiQ9DAR7.
PhosphoSitePlusiQ9DAR7.

Expressioni

Gene expression databases

BgeeiENSMUSG00000032040.
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

Protein-protein interaction databases

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

Structurei

Secondary structure

1338
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi42 – 44Combined sources3
Beta strandi47 – 55Combined sources9
Turni56 – 59Combined sources4
Beta strandi60 – 67Combined sources8
Beta strandi77 – 85Combined sources9
Helixi90 – 97Combined sources8
Beta strandi102 – 108Combined sources7
Beta strandi110 – 118Combined sources9
Helixi121 – 124Combined sources4
Beta strandi126 – 133Combined sources8
Helixi136 – 142Combined sources7
Beta strandi147 – 152Combined sources6
Helixi154 – 159Combined sources6
Helixi161 – 168Combined sources8
Helixi173 – 179Combined sources7
Beta strandi182 – 184Combined sources3
Beta strandi189 – 192Combined sources4
Turni195 – 197Combined sources3
Beta strandi199 – 203Combined sources5
Beta strandi216 – 224Combined sources9
Helixi229 – 231Combined sources3
Helixi234 – 236Combined sources3
Helixi237 – 255Combined sources19
Helixi259 – 261Combined sources3
Beta strandi262 – 269Combined sources8
Beta strandi271 – 274Combined sources4
Beta strandi276 – 281Combined sources6
Turni291 – 293Combined sources3
Beta strandi294 – 296Combined sources3
Helixi297 – 306Combined sources10
Helixi310 – 313Combined sources4
Beta strandi316 – 321Combined sources6
Helixi325 – 336Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9DAR7.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni267 – 278Substrate bindingBy similarityAdd BLAST12

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi9 – 12nuclear localization signal (NLS)By similarity4
Motifi141 – 153nuclear export sequence (NES)By similarityAdd BLAST13
Motifi274 – 278Histidine triad motifBy similarity5

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

Sequence similaritiesi

Belongs to the HIT family.Curated

Phylogenomic databases

eggNOGiKOG3969. Eukaryota.
COG5075. LUCA.
GeneTreeiENSGT00390000003924.
HOGENOMiHOG000182411.
HOVERGENiHBG051322.
InParanoidiQ9DAR7.
KOiK12584.
OMAiSFLVEET.
OrthoDBiEOG091G0DTP.
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)DescriptionActionsGraphical viewLength
Sequence conflicti141K → E in BAC37194 (PubMed:16141072).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1VLRX-ray1.83A/B1-338[»]
ProteinModelPortaliQ9DAR7.
SMRiQ9DAR7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

iPTMnetiQ9DAR7.
PhosphoSitePlusiQ9DAR7.

Proteomic databases

EPDiQ9DAR7.
MaxQBiQ9DAR7.
PaxDbiQ9DAR7.
PeptideAtlasiQ9DAR7.
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

eggNOGiKOG3969. Eukaryota.
COG5075. LUCA.
GeneTreeiENSGT00390000003924.
HOGENOMiHOG000182411.
HOVERGENiHBG051322.
InParanoidiQ9DAR7.
KOiK12584.
OMAiSFLVEET.
OrthoDBiEOG091G0DTP.
PhylomeDBiQ9DAR7.
TreeFamiTF105622.

Enzyme and pathway databases

BRENDAi3.6.1.59. 3474.
ReactomeiR-MMU-429958. mRNA decay by 3' to 5' exoribonuclease.

Miscellaneous databases

EvolutionaryTraceiQ9DAR7.
PROiQ9DAR7.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000032040.
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...

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: November 2, 2016
This is version 120 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.