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O70348 (DXO_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 79. 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:
Decapping and exoribonuclease protein

Short name=DXO
EC=3.1.13.-
EC=3.6.1.-
Alternative name(s):
Dom-3 homolog Z
Gene names
Name:Dxo
Synonyms:Dom3z, Ng6
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length397 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.4

Cofactor

Binds 2 magnesium ions. Ref.4

Subcellular location

Nucleus By similarity.

Sequence similarities

Belongs to the DXO/Dom3Z family.

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 (Ref.4).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 397397Decapping and exoribonuclease protein
PRO_0000249823

Sites

Metal binding1921Magnesium 1
Metal binding1921Magnesium 2
Metal binding2341Magnesium 2
Metal binding2361Magnesium 1
Metal binding2361Magnesium 2
Metal binding2531Magnesium 1
Metal binding2541Magnesium 1; via carbonyl oxygen
Binding site581Substrate
Binding site1011Substrate
Binding site1321Substrate
Binding site2171Substrate
Binding site2341Substrate
Binding site2801Substrate

Experimental info

Mutagenesis2341E → A: Abolishes the decapping activity. Ref.4
Mutagenesis2361D → A: Abolishes the decapping activity. Ref.4
Sequence conflict201N → H in AAC05281. Ref.1
Sequence conflict281S → L in AAC05281. Ref.1

Secondary structure

.......................................................... 397
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O70348 [UniParc].

Last modified September 19, 2006. Version 2.
Checksum: 02022DF0A77D503E

FASTA39745,280
        10         20         30         40         50         60 
MEPRGTKRKA EKTEVEKPLN KLPRAVPSLR TQPSLYSGPF PFYRRPSELG CFSLDAQRQY 

        70         80         90        100        110        120 
HGDARALRYY SPPPINGPGP DFDLRDGYPD RYQPRDEEVQ ERLDHLLRWV LEHRNQLEGG 

       130        140        150        160        170        180 
PGWLAGATVT WRGHLTKLLT TPYERQEGWQ LAASRFQGTL YLSEVETPAA RAQRLARPPL 

       190        200        210        220        230        240 
LRELMYMGYK FEQYMCADKP GGSPDPSGEV NTNVAYCSVL RSRLGNHPLL FSGEVDCLNP 

       250        260        270        280        290        300 
QAPCTQPPSC YVELKTSKEM HSPGQWRSFY RHKLLKWWAQ SFLPGVPHVV AGFRNPEGFV 

       310        320        330        340        350        360 
CSLKTFPTME MFENVRNDRE GWNPSVCMNF CAAFLSFAQS TVVQDDPRLV HLFSWEPGGP 

       370        380        390 
VTVSVHRDAP YAFLPSWYVE TMTQDLPPLS KTPSPKD 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse."
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.
Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129.
[2]"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: FVB/N.
Tissue: Mammary gland.
[3]"Structure and function of the 5'-->3' exoribonuclease Rat1 and its activating partner Rai1."
Xiang S., Cooper-Morgan A., Jiao X., Kiledjian M., Manley J.L., Tong L.
Nature 458:784-788(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) IN COMPLEX WITH GDP.
[4]"A mammalian pre-mRNA 5' end capping quality control mechanism and an unexpected link of capping to pre-mRNA processing."
Jiao X., Chang J.H., Kilic T., Tong L., Kiledjian M.
Mol. Cell 50:104-115(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 27-397 IN COMPLEX WITH MAGNESIUM AND M(7)GPPPG CAP, FUNCTION, COFACTOR, CATALYTIC ACTIVITY, MUTAGENESIS OF GLU-234 AND ASP-236.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF049850 Genomic DNA. Translation: AAC05281.1.
BC004713 mRNA. Translation: AAH04713.1.
RefSeqNP_001157242.1. NM_001163770.1.
NP_291091.2. NM_033613.2.
XP_006536561.1. XM_006536498.1.
XP_006537294.1. XM_006537231.1.
UniGeneMm.275309.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3FQIX-ray2.01A1-397[»]
3FQJX-ray2.62A1-397[»]
4J7LX-ray1.80A27-384[»]
4J7MX-ray1.70A27-384[»]
4J7NX-ray1.50A27-384[»]
ProteinModelPortalO70348.
SMRO70348. Positions 27-384.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING10090.ENSMUSP00000047018.

PTM databases

PhosphoSiteO70348.

Proteomic databases

PaxDbO70348.
PRIDEO70348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000046244; ENSMUSP00000047018; ENSMUSG00000040482.
ENSMUST00000180043; ENSMUSP00000137234; ENSMUSG00000040482.
GeneID112403.
KEGGmmu:112403.
UCSCuc008cdr.2. mouse.

Organism-specific databases

CTD1797.
MGIMGI:1890444. Dxo.

Phylogenomic databases

eggNOGNOG237475.
GeneTreeENSGT00390000006425.
HOGENOMHOG000200647.
HOVERGENHBG080627.
InParanoidO70348.
KOK14845.
PhylomeDBO70348.
TreeFamTF322812.

Gene expression databases

BgeeO70348.
CleanExMM_DOM3Z.
GenevestigatorO70348.

Family and domain databases

InterProIPR013961. RAI1.
[Graphical view]
PfamPF08652. RAI1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO70348.
NextBio367877.
PROO70348.
SOURCESearch...

Entry information

Entry nameDXO_MOUSE
AccessionPrimary (citable) accession number: O70348
Secondary accession number(s): Q99KD8
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: September 19, 2006
Last modified: April 16, 2014
This is version 79 of the entry and version 2 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