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Protein

Decapping and exoribonuclease protein

Gene

Dxo

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

Functioni

Ribonuclease that specifically degrades pre-mRNAs with a defective 5' end cap and is part of a pre-mRNA capping quality control. Has decapping, pyrophosphohydrolase and 5'-3' exonuclease activities. Has decapping activity toward incomplete 5' end cap mRNAs such as unmethylated 5' end-capped RNA to release GpppN and 5' end monophosphate RNA. The 5' end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs. Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5' end triphosphate to release pyrophosphates.1 Publication

Cofactori

Mg2+1 PublicationNote: Binds 2 magnesium ions.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei58Substrate1
Binding sitei101Substrate1
Binding sitei132Substrate1
Metal bindingi192Magnesium 11 Publication1
Metal bindingi192Magnesium 21 Publication1
Binding sitei217Substrate1
Metal bindingi234Magnesium 21 Publication1
Binding sitei234Substrate1
Metal bindingi236Magnesium 11 Publication1
Metal bindingi236Magnesium 21 Publication1
Metal bindingi253Magnesium 11 Publication1
Metal bindingi254Magnesium 1; via carbonyl oxygen1 Publication1
Binding sitei280Substrate1

GO - Molecular functioni

  • 5'-3' exonuclease activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • mRNA binding Source: UniProtKB
  • nucleotide binding Source: UniProtKB-KW
  • RNA pyrophosphohydrolase activity Source: UniProtKB

GO - Biological processi

  • metabolic process Source: UniProtKB
  • mRNA catabolic process Source: UniProtKB
  • nuclear mRNA surveillance Source: UniProtKB
  • nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
  • RNA destabilization Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Ligandi

Magnesium, Metal-binding, Nucleotide-binding, RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Decapping and exoribonuclease protein (EC:3.1.13.-, EC:3.6.1.-)
Short name:
DXO
Alternative name(s):
Dom-3 homolog Z
Gene namesi
Name:Dxo
Synonyms:Dom3z, Ng6
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1890444. Dxo.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi234E → A: Abolishes the decapping activity. 1 Publication1
Mutagenesisi236D → A: Abolishes the decapping activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002498231 – 397Decapping and exoribonuclease proteinAdd BLAST397

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei392PhosphothreonineBy similarity1
Modified residuei394PhosphoserineCombined sources1

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiO70348.
MaxQBiO70348.
PaxDbiO70348.
PRIDEiO70348.

PTM databases

iPTMnetiO70348.
PhosphoSitePlusiO70348.

Expressioni

Gene expression databases

BgeeiENSMUSG00000040482.
CleanExiMM_DOM3Z.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047018.

Structurei

Secondary structure

1397
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi33 – 35Combined sources3
Beta strandi47 – 54Combined sources8
Beta strandi60 – 64Combined sources5
Beta strandi75 – 77Combined sources3
Turni84 – 91Combined sources8
Beta strandi97 – 99Combined sources3
Helixi104 – 113Combined sources10
Helixi114 – 116Combined sources3
Turni121 – 123Combined sources3
Helixi124 – 126Combined sources3
Beta strandi128 – 131Combined sources4
Helixi132 – 140Combined sources9
Helixi141 – 143Combined sources3
Beta strandi149 – 156Combined sources8
Beta strandi159 – 164Combined sources6
Helixi168 – 175Combined sources8
Helixi179 – 195Combined sources17
Beta strandi196 – 199Combined sources4
Beta strandi215 – 224Combined sources10
Beta strandi227 – 234Combined sources8
Turni247 – 250Combined sources4
Beta strandi251 – 258Combined sources8
Helixi263 – 271Combined sources9
Helixi273 – 282Combined sources10
Turni283 – 285Combined sources3
Beta strandi288 – 294Combined sources7
Beta strandi298 – 307Combined sources10
Helixi308 – 315Combined sources8
Helixi324 – 341Combined sources18
Beta strandi349 – 355Combined sources7
Beta strandi361 – 368Combined sources8
Turni369 – 371Combined sources3
Helixi376 – 383Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FQIX-ray2.01A1-397[»]
3FQJX-ray2.62A1-397[»]
4J7LX-ray1.80A27-384[»]
4J7MX-ray1.70A27-384[»]
4J7NX-ray1.50A27-384[»]
ProteinModelPortaliO70348.
SMRiO70348.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70348.

Family & Domainsi

Sequence similaritiesi

Belongs to the DXO/Dom3Z family.Curated

Phylogenomic databases

eggNOGiKOG1982. Eukaryota.
ENOG410ZAFR. LUCA.
HOGENOMiHOG000200647.
HOVERGENiHBG080627.
InParanoidiO70348.
KOiK14845.
PhylomeDBiO70348.
TreeFamiTF322812.

Family and domain databases

InterProiIPR013961. RAI1.
[Graphical view]
PfamiPF08652. RAI1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O70348-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEPRGTKRKA EKTEVEKPLN KLPRAVPSLR TQPSLYSGPF PFYRRPSELG
60 70 80 90 100
CFSLDAQRQY HGDARALRYY SPPPINGPGP DFDLRDGYPD RYQPRDEEVQ
110 120 130 140 150
ERLDHLLRWV LEHRNQLEGG PGWLAGATVT WRGHLTKLLT TPYERQEGWQ
160 170 180 190 200
LAASRFQGTL YLSEVETPAA RAQRLARPPL LRELMYMGYK FEQYMCADKP
210 220 230 240 250
GGSPDPSGEV NTNVAYCSVL RSRLGNHPLL FSGEVDCLNP QAPCTQPPSC
260 270 280 290 300
YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPHVV AGFRNPEGFV
310 320 330 340 350
CSLKTFPTME MFENVRNDRE GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV
360 370 380 390
HLFSWEPGGP VTVSVHRDAP YAFLPSWYVE TMTQDLPPLS KTPSPKD
Length:397
Mass (Da):45,280
Last modified:September 19, 2006 - v2
Checksum:i02022DF0A77D503E
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti20N → H in AAC05281 (PubMed:14656967).Curated1
Sequence conflicti28S → L in AAC05281 (PubMed:14656967).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF049850 Genomic DNA. Translation: AAC05281.1.
BC004713 mRNA. Translation: AAH04713.1.
CCDSiCCDS28660.1.
RefSeqiNP_001157242.1. NM_001163770.1.
NP_291091.2. NM_033613.2.
UniGeneiMm.275309.

Genome annotation databases

GeneIDi112403.
KEGGimmu:112403.
UCSCiuc008cdr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF049850 Genomic DNA. Translation: AAC05281.1.
BC004713 mRNA. Translation: AAH04713.1.
CCDSiCCDS28660.1.
RefSeqiNP_001157242.1. NM_001163770.1.
NP_291091.2. NM_033613.2.
UniGeneiMm.275309.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3FQIX-ray2.01A1-397[»]
3FQJX-ray2.62A1-397[»]
4J7LX-ray1.80A27-384[»]
4J7MX-ray1.70A27-384[»]
4J7NX-ray1.50A27-384[»]
ProteinModelPortaliO70348.
SMRiO70348.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047018.

PTM databases

iPTMnetiO70348.
PhosphoSitePlusiO70348.

Proteomic databases

EPDiO70348.
MaxQBiO70348.
PaxDbiO70348.
PRIDEiO70348.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi112403.
KEGGimmu:112403.
UCSCiuc008cdr.2. mouse.

Organism-specific databases

CTDi1797.
MGIiMGI:1890444. Dxo.

Phylogenomic databases

eggNOGiKOG1982. Eukaryota.
ENOG410ZAFR. LUCA.
HOGENOMiHOG000200647.
HOVERGENiHBG080627.
InParanoidiO70348.
KOiK14845.
PhylomeDBiO70348.
TreeFamiTF322812.

Miscellaneous databases

EvolutionaryTraceiO70348.
PROiO70348.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000040482.
CleanExiMM_DOM3Z.

Family and domain databases

InterProiIPR013961. RAI1.
[Graphical view]
PfamiPF08652. RAI1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiDXO_MOUSE
AccessioniPrimary (citable) accession number: O70348
Secondary accession number(s): Q99KD8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: November 2, 2016
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Caution

In contrast to canonical decapping enzymes DCP2 and NUDT16, which release m7pppG (m7GDP), the decapping activity releases the entire cap structure GpppN and a 5' end monophosphate RNA.1 Publication

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.