O77932 · DXO_HUMAN

  • Protein
    Decapping and exoribonuclease protein
  • Gene
    DXO
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Decapping enzyme for NAD-capped RNAs: specifically hydrolyzes the nicotinamide adenine dinucleotide (NAD) cap from a subset of RNAs by removing the entire NAD moiety from the 5'-end of an NAD-capped RNA (PubMed:28283058).
The NAD-cap is present at the 5'-end of some RNAs and snoRNAs (PubMed:28283058).
In contrast to the canonical 5'-end N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay (PubMed:28283058).
Preferentially acts on NAD-capped transcripts in response to environmental stress (PubMed:31101919).
Also acts as a non-canonical decapping enzyme that removes the entire cap structure of m7G capped or incompletely capped RNAs and mediates their subsequent degradation (By similarity).
Specifically degrades pre-mRNAs with a defective 5'-end m7G cap and is part of a pre-mRNA capping quality control (By similarity).
Has decapping activity toward incomplete 5'-end m7G cap mRNAs such as unmethylated 5'-end-capped RNA (cap0), while it has no activity toward 2'-O-ribose methylated m7G cap (cap1) (PubMed:29601584).
In contrast to canonical decapping enzymes DCP2 and NUDT16, which cleave the cap within the triphosphate linkage, the decapping activity releases the entire cap structure GpppN and a 5'-end monophosphate RNA (By similarity).
Also has 5'-3' exoribonuclease activities: The 5'-end monophosphate RNA is then degraded by the 5'-3' exoribonuclease activity, enabling this enzyme to decap and degrade incompletely capped mRNAs (PubMed:29601584).
Also possesses RNA 5'-pyrophosphohydrolase activity by hydrolyzing the 5'-end triphosphate to release pyrophosphates (By similarity).
Exhibits decapping activity towards FAD-capped RNAs (PubMed:32374864).
Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 magnesium ions.

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site58substrate
Binding site101substrate
Binding site131-133substrate
Binding site192Mg2+ 1 (UniProtKB | ChEBI)
Binding site192Mg2+ 2 (UniProtKB | ChEBI)
Binding site217substrate
Binding site234Mg2+ 2 (UniProtKB | ChEBI)
Binding site234substrate
Binding site236Mg2+ 1 (UniProtKB | ChEBI)
Binding site236Mg2+ 2 (UniProtKB | ChEBI)
Binding site253Mg2+ 1 (UniProtKB | ChEBI)
Binding site254Mg2+ 1 (UniProtKB | ChEBI)
Binding site255substrate
Binding site280substrate

GO annotations

AspectTerm
Cellular Componentcytosol
Cellular Componentnucleoplasm
Cellular Componentnucleus
Cellular Componentplasma membrane
Molecular Function5'-3' exonuclease activity
Molecular Functionmagnesium ion binding
Molecular FunctionmRNA 5'-diphosphatase activity
Molecular FunctionmRNA binding
Molecular Functionnucleotide binding
Molecular FunctionRNA NAD+-cap (NAD+-forming) hydrolase activity
Biological ProcessmRNA catabolic process
Biological ProcessNAD-cap decapping
Biological Processnuclear mRNA surveillance
Biological Processnuclear-transcribed mRNA catabolic process
Biological Processnucleic acid metabolic process
Biological ProcessRNA destabilization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Decapping and exoribonuclease protein
  • EC number
  • Short names
    DXO
  • Alternative names
    • 5'-3' exoribonuclease DXO
      (EC:3.1.13.-
      ) . EC:3.1.13.- (UniProtKB | ENZYME | Rhea)
    • Dom-3 homolog Z
    • NAD-capped RNA hydrolase DXO
      (DeNADding enzyme DXO
      ) (EC:3.6.1.-
      ) . EC:3.6.1.- (UniProtKB | ENZYME | Rhea)

Gene names

    • Name
      DXO
    • Synonyms
      DOM3L, DOM3Z
      , NG6

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    O77932
  • Secondary accessions
    • A2CER3
    • B0UZ80
    • O15004
    • O78127
    • O78128

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis7-8Impaired subcellular location, leading to localization both in cytoplasm and nucleus.
Natural variantVAR_02749228in dbSNP:rs1056694
Natural variantVAR_02749363in dbSNP:rs2746396
Mutagenesis236Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-253.
Mutagenesis253Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-236.
Natural variantVAR_027494261in dbSNP:rs17207867
Natural variantVAR_027495332in dbSNP:rs12205138

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 808 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_00002498221-396Decapping and exoribonuclease protein
Modified residue392Phosphothreonine
Modified residue394Phosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Ubiquitously expressed.

Gene expression databases

Organism-specific databases

Structure

Family & Domains

Features

Showing features for compositional bias, region.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues
Region1-37Disordered

Sequence similarities

Belongs to the DXO/Dom3Z family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    396
  • Mass (Da)
    44,929
  • Last updated
    2006-09-19 v2
  • Checksum
    17C8119037EB6892
MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
F8WC68F8WC68_HUMANDXO210
H7C5D2H7C5D2_HUMANDXO174

Sequence caution

The sequence AAB67983.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB89306.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-19Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF059252
EMBL· GenBank· DDBJ
AAC78603.1
EMBL· GenBank· DDBJ
mRNA
AF019413
EMBL· GenBank· DDBJ
AAB67983.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL049547
EMBL· GenBank· DDBJ
CAB89305.1
EMBL· GenBank· DDBJ
Genomic DNA
AL049547
EMBL· GenBank· DDBJ
CAB89306.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL662849
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL844853
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR753822
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR759782
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AL645922
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CR753845
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471081
EMBL· GenBank· DDBJ
EAX03558.1
EMBL· GenBank· DDBJ
Genomic DNA
BC009344
EMBL· GenBank· DDBJ
AAH09344.1
EMBL· GenBank· DDBJ
mRNA
BC019083
EMBL· GenBank· DDBJ
AAH19083.1
EMBL· GenBank· DDBJ
mRNA
AF059253
EMBL· GenBank· DDBJ
AAC78604.1
EMBL· GenBank· DDBJ
mRNA
AF059254
EMBL· GenBank· DDBJ
AAC78605.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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