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O70348

- DXO_MOUSE

UniProt

O70348 - DXO_MOUSE

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Protein

Decapping and exoribonuclease protein

Gene

Dxo

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

Binds 2 magnesium ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei58 – 581Substrate
Binding sitei101 – 1011Substrate
Binding sitei132 – 1321Substrate
Metal bindingi192 – 1921Magnesium 11 Publication
Metal bindingi192 – 1921Magnesium 21 Publication
Binding sitei217 – 2171Substrate
Metal bindingi234 – 2341Magnesium 21 Publication
Binding sitei234 – 2341Substrate
Metal bindingi236 – 2361Magnesium 11 Publication
Metal bindingi236 – 2361Magnesium 21 Publication
Metal bindingi253 – 2531Magnesium 11 Publication
Metal bindingi254 – 2541Magnesium 1; via carbonyl oxygen1 Publication
Binding sitei280 – 2801Substrate

GO - Molecular functioni

  1. 5'-3' exonuclease activity Source: UniProtKB
  2. magnesium ion binding Source: UniProtKB
  3. mRNA binding Source: UniProtKB
  4. nucleotide binding Source: UniProtKB-KW
  5. RNA pyrophosphohydrolase activity Source: UniProtKB

GO - Biological processi

  1. metabolic process Source: UniProtKB
  2. mRNA catabolic process Source: UniProtKB
  3. nuclear mRNA surveillance Source: UniProtKB
  4. nucleic acid phosphodiester bond hydrolysis Source: UniProtKB
  5. 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
ProteomesiUP000000589: Chromosome 17

Organism-specific databases

MGIiMGI:1890444. Dxo.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi234 – 2341E → A: Abolishes the decapping activity. 1 Publication
Mutagenesisi236 – 2361D → A: Abolishes the decapping activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 397397Decapping and exoribonuclease proteinPRO_0000249823Add
BLAST

Proteomic databases

MaxQBiO70348.
PaxDbiO70348.
PRIDEiO70348.

PTM databases

PhosphoSiteiO70348.

Expressioni

Gene expression databases

BgeeiO70348.
CleanExiMM_DOM3Z.
ExpressionAtlasiO70348. baseline and differential.
GenevestigatoriO70348.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000047018.

Structurei

Secondary structure

1
397
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 353
Beta strandi47 – 548
Beta strandi60 – 645
Beta strandi75 – 773
Turni84 – 918
Beta strandi97 – 993
Helixi104 – 11310
Helixi114 – 1163
Turni121 – 1233
Helixi124 – 1263
Beta strandi128 – 1314
Helixi132 – 1409
Helixi141 – 1433
Beta strandi149 – 1568
Beta strandi159 – 1646
Helixi168 – 1758
Helixi179 – 19517
Beta strandi196 – 1994
Beta strandi215 – 22410
Beta strandi227 – 2348
Turni247 – 2504
Beta strandi251 – 2588
Helixi263 – 2719
Helixi273 – 28210
Turni283 – 2853
Beta strandi288 – 2947
Beta strandi298 – 30710
Helixi308 – 3158
Helixi324 – 34118
Beta strandi349 – 3557
Beta strandi361 – 3688
Turni369 – 3713
Helixi376 – 3838

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 27-384.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO70348.

Family & Domainsi

Sequence similaritiesi

Belongs to the DXO/Dom3Z family.Curated

Phylogenomic databases

eggNOGiNOG237475.
GeneTreeiENSGT00390000006425.
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 [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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti20 – 201N → H in AAC05281. (PubMed:14656967)Curated
Sequence conflicti28 – 281S → L in AAC05281. (PubMed:14656967)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
XP_006536561.1. XM_006536498.1.
XP_006537294.1. XM_006537231.1.
UniGeneiMm.275309.

Genome annotation databases

EnsembliENSMUST00000046244; ENSMUSP00000047018; ENSMUSG00000040482.
ENSMUST00000180043; ENSMUSP00000137234; ENSMUSG00000040482.
GeneIDi112403.
KEGGimmu:112403.
UCSCiuc008cdr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF049850 Genomic DNA. Translation: AAC05281.1 .
BC004713 mRNA. Translation: AAH04713.1 .
CCDSi CCDS28660.1.
RefSeqi NP_001157242.1. NM_001163770.1.
NP_291091.2. NM_033613.2.
XP_006536561.1. XM_006536498.1.
XP_006537294.1. XM_006537231.1.
UniGenei Mm.275309.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3FQI X-ray 2.01 A 1-397 [» ]
3FQJ X-ray 2.62 A 1-397 [» ]
4J7L X-ray 1.80 A 27-384 [» ]
4J7M X-ray 1.70 A 27-384 [» ]
4J7N X-ray 1.50 A 27-384 [» ]
ProteinModelPortali O70348.
SMRi O70348. Positions 27-384.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 10090.ENSMUSP00000047018.

PTM databases

PhosphoSitei O70348.

Proteomic databases

MaxQBi O70348.
PaxDbi O70348.
PRIDEi O70348.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000046244 ; ENSMUSP00000047018 ; ENSMUSG00000040482 .
ENSMUST00000180043 ; ENSMUSP00000137234 ; ENSMUSG00000040482 .
GeneIDi 112403.
KEGGi mmu:112403.
UCSCi uc008cdr.2. mouse.

Organism-specific databases

CTDi 1797.
MGIi MGI:1890444. Dxo.

Phylogenomic databases

eggNOGi NOG237475.
GeneTreei ENSGT00390000006425.
HOGENOMi HOG000200647.
HOVERGENi HBG080627.
InParanoidi O70348.
KOi K14845.
PhylomeDBi O70348.
TreeFami TF322812.

Miscellaneous databases

EvolutionaryTracei O70348.
NextBioi 367877.
PROi O70348.
SOURCEi Search...

Gene expression databases

Bgeei O70348.
CleanExi MM_DOM3Z.
ExpressionAtlasi O70348. baseline and differential.
Genevestigatori O70348.

Family and domain databases

InterProi IPR013961. RAI1.
[Graphical view ]
Pfami PF08652. RAI1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.

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: October 29, 2014
This is version 82 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

External Data

Dasty 3