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Protein

m7GpppX diphosphatase

Gene

Dcps

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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)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

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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi628887. 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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 336335m7GpppX diphosphatasePRO_0000109797Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei23 – 231PhosphoserineBy similarity
Modified residuei137 – 1371N6-acetyllysineBy similarity
Modified residuei141 – 1411N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ8K4F7.
PRIDEiQ8K4F7.

PTM databases

iPTMnetiQ8K4F7.
PhosphoSiteiQ8K4F7.

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

STRINGi10116.ENSRNOP00000013763.

Structurei

3D structure databases

ProteinModelPortaliQ8K4F7.
SMRiQ8K4F7. Positions 37-335.
ModBaseiSearch...
MobiDBiSearch...

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

Sequence similaritiesi

Belongs to the HIT family.Curated

Phylogenomic databases

eggNOGiKOG3969. Eukaryota.
COG5075. LUCA.
HOGENOMiHOG000182411.
HOVERGENiHBG051322.
InParanoidiQ8K4F7.
KOiK12584.
PhylomeDBiQ8K4F7.

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]
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.

Q8K4F7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADTAPQLKR KREQEAEEAE TPSTEEKEAG VGNGTSAPVR LPFSGFRVQK
60 70 80 90 100
VLRESARDKI IFLHGKVNED SGDTHGEDAV VILEKTPFQV EHVAQLLTGN
110 120 130 140 150
PELKLQFSND IYSTYNLFPP RHLSDIKTTV VYPASEKHLQ KYMRQDLRLI
160 170 180 190 200
RETGDDYRSL TLPYLESQSL SIQWVYNILD KKAEADRIVF ENPDPSDGFV
210 220 230 240 250
LIPDLKWNQQ QLDDLYLIAI CHRRGIRSLR DLTPEHLPLL RNILREGQEA
260 270 280 290 300
ILKRYQVTGD RLRVYLHYLP SYYHLHVHFT ALGFEAPGSG VERAHLLAEV
310 320 330
IENLECDPKH YQRRTLTFAL RTDDPLLQLL QKAQQP
Length:336
Mass (Da):38,714
Last modified:October 1, 2002 - v1
Checksum:iAEFA4D106FC5B6AE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411249 mRNA. Translation: AAN03664.1.
RefSeqiNP_695214.1. NM_153302.1.
UniGeneiRn.162991.

Genome annotation databases

GeneIDi266605.
KEGGirno:266605.
UCSCiRGD:628887. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF411249 mRNA. Translation: AAN03664.1.
RefSeqiNP_695214.1. NM_153302.1.
UniGeneiRn.162991.

3D structure databases

ProteinModelPortaliQ8K4F7.
SMRiQ8K4F7. Positions 37-335.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000013763.

PTM databases

iPTMnetiQ8K4F7.
PhosphoSiteiQ8K4F7.

Proteomic databases

PaxDbiQ8K4F7.
PRIDEiQ8K4F7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi266605.
KEGGirno:266605.
UCSCiRGD:628887. rat.

Organism-specific databases

CTDi28960.
RGDi628887. Dcps.

Phylogenomic databases

eggNOGiKOG3969. Eukaryota.
COG5075. LUCA.
HOGENOMiHOG000182411.
HOVERGENiHBG051322.
InParanoidiQ8K4F7.
KOiK12584.
PhylomeDBiQ8K4F7.

Miscellaneous databases

PROiQ8K4F7.

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]
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_RAT
AccessioniPrimary (citable) accession number: Q8K4F7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 2005
Last sequence update: October 1, 2002
Last modified: September 7, 2016
This is version 89 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

Complete proteome, Reference proteome

Documents

  1. 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.