O77932 · DXO_HUMAN
- ProteinDecapping and exoribonuclease protein
- GeneDXO
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids396 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + diphosphate + H+This reaction proceeds in the forward direction.
- a 5'-end NAD+-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + H+ + NAD+This reaction proceeds in the forward direction.
- a 5'-end NAD+-phospho-ribonucleoside in snoRNA + H2O = a 5'-end phospho-ribonucleoside in snoRNA + H+ + NAD+This reaction proceeds in the forward direction.
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside-ribonucleotide in mRNA + H2O = a (N7-methyl 5'-triphosphoguanosine)-nucleoside + a 5'-end phospho-ribonucleoside in mRNA + H+This reaction proceeds in the forward direction.
- a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + FAD + H+This reaction proceeds in the forward direction.
- a 5'-end CoA-ribonucleoside in mRNA + H2O = 3'-dephospho-CoA + a 5'-end phospho-ribonucleoside in mRNA + H+This reaction proceeds in the forward direction.
Cofactor
Note: Binds 2 magnesium ions.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 58 | substrate | ||||
Sequence: R | ||||||
Binding site | 101 | substrate | ||||
Sequence: E | ||||||
Binding site | 131-133 | substrate | ||||
Sequence: WRG | ||||||
Binding site | 192 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 192 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 217 | substrate | ||||
Sequence: C | ||||||
Binding site | 234 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 234 | substrate | ||||
Sequence: E | ||||||
Binding site | 236 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 236 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 253 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 254 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: L | ||||||
Binding site | 255 | substrate | ||||
Sequence: K | ||||||
Binding site | 280 | substrate | ||||
Sequence: Q |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Cellular Component | plasma membrane | |
Molecular Function | 5'-3' exonuclease activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | mRNA 5'-diphosphatase activity | |
Molecular Function | mRNA binding | |
Molecular Function | nucleotide binding | |
Molecular Function | RNA NAD+-cap (NAD+-forming) hydrolase activity | |
Biological Process | mRNA catabolic process | |
Biological Process | NAD-cap decapping | |
Biological Process | nuclear mRNA surveillance | |
Biological Process | nuclear-transcribed mRNA catabolic process | |
Biological Process | nucleic acid metabolic process | |
Biological Process | RNA destabilization |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDecapping and exoribonuclease protein
- EC number
- Short namesDXO
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO77932
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 7-8 | Impaired subcellular location, leading to localization both in cytoplasm and nucleus. | ||||
Sequence: KR → AA | ||||||
Natural variant | VAR_027492 | 28 | in dbSNP:rs1056694 | |||
Sequence: S → T | ||||||
Natural variant | VAR_027493 | 63 | in dbSNP:rs2746396 | |||
Sequence: D → E | ||||||
Mutagenesis | 236 | Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-253. | ||||
Sequence: D → A | ||||||
Mutagenesis | 253 | Abolishes the decapping activity on incomplete m7G cap mRNAs; when associated with A-236. | ||||
Sequence: E → A | ||||||
Natural variant | VAR_027494 | 261 | in dbSNP:rs17207867 | |||
Sequence: H → Q | ||||||
Natural variant | VAR_027495 | 332 | in dbSNP:rs12205138 | |||
Sequence: A → V |
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.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000249822 | 1-396 | Decapping and exoribonuclease protein | |||
Sequence: MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYSGPFPFYRRPSELGCFSLDAQRQYHGDARALRYYSPPPTNGPGPNFDLRDGYPDRYQPRDEEVQERLDHLLCWLLEHRGRLEGGPGWLAEAIVTWRGHLTKLLTTPYERQEGWQLAASRFQGTLYLSEVETPNARAQRLARPPLLRELMYMGYKFEQYMCADKPGSSPDPSGEVNTNVAFCSVLRSRLGSHPLLFSGEVDCTDPQAPSTQPPTCYVELKTSKEMHSPGQWRSFYRHKLLKWWAQSFLPGVPNVVAGFRNPDGFVSSLKTFPTMKMFEYVRNDRDGWNPSVCMNFCAAFLSFAQSTVVQDDPRLVHLFSWEPGGPVTVSVHQDAPYAFLPIWYVEAMTQDLPSPPKTPSPK | ||||||
Modified residue | 392 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 394 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Ubiquitously expressed.
Gene expression databases
Organism-specific databases
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O77932 | BAG6 P46379-2 | 3 | EBI-372173, EBI-10988864 | |
BINARY | O77932 | CCT7 Q99832 | 3 | EBI-372173, EBI-357046 | |
BINARY | O77932 | DNAJB6 O75190-2 | 3 | EBI-372173, EBI-12593112 | |
BINARY | O77932 | DNALI1 O14645 | 3 | EBI-372173, EBI-395638 | |
BINARY | O77932 | EIF2S3 P41091 | 3 | EBI-372173, EBI-1054228 | |
BINARY | O77932 | ERN1 O75460-2 | 3 | EBI-372173, EBI-25852368 | |
BINARY | O77932 | FKBP1A Q0VDC6 | 3 | EBI-372173, EBI-10226858 | |
BINARY | O77932 | HSPB1 P04792 | 3 | EBI-372173, EBI-352682 | |
BINARY | O77932 | HSPD1 P10809 | 3 | EBI-372173, EBI-352528 | |
BINARY | O77932 | KIF1B O60333-2 | 3 | EBI-372173, EBI-10975473 | |
BINARY | O77932 | KLF11 O14901 | 3 | EBI-372173, EBI-948266 | |
BINARY | O77932 | PECAM1 P16284 | 3 | EBI-372173, EBI-716404 | |
BINARY | O77932 | PRKN O60260-5 | 3 | EBI-372173, EBI-21251460 | |
BINARY | O77932 | PRPS1 P60891 | 3 | EBI-372173, EBI-749195 | |
BINARY | O77932 | RNF11 Q9Y3C5 | 3 | EBI-372173, EBI-396669 | |
BINARY | O77932 | SARS1 P49591 | 3 | EBI-372173, EBI-1053431 | |
BINARY | O77932 | UBE2K P61086 | 3 | EBI-372173, EBI-473850 | |
BINARY | O77932 | VIM P08670 | 3 | EBI-372173, EBI-353844 | |
BINARY | O77932 | WFS1 O76024 | 3 | EBI-372173, EBI-720609 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | ||||
Sequence: MDPRGTKRGAEKTEVAEPR | ||||||
Region | 1-37 | Disordered | ||||
Sequence: MDPRGTKRGAEKTEVAEPRNKLPRPAPSLPTDPALYS |
Sequence similarities
Belongs to the DXO/Dom3Z family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length396
- Mass (Da)44,929
- Last updated2006-09-19 v2
- Checksum17C8119037EB6892
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-19 | Basic and acidic residues | ||||
Sequence: MDPRGTKRGAEKTEVAEPR |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |