O62255 · DCP2_CAEEL
- Proteinm7GpppN-mRNA hydrolase dcap-2
- Genedcap-2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids786 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:16199859).
Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:16199859).
RNA-decapping enzyme although it does not bind the RNA cap (PubMed:16199859).
May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs (PubMed:16199859).
In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia (PubMed:18439994).
Required for the developmental axon guidance and regrowth of PLM touch receptor neurons (PubMed:31983639).
Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons (PubMed:28887031).
Promotes survival at high temperatures (PubMed:25061667).
Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:16199859).
RNA-decapping enzyme although it does not bind the RNA cap (PubMed:16199859).
May contribute to gene regulation in multiple RNA pathways including monomethylguanosine- and trimethylguanosine-capped RNAs (PubMed:16199859).
In oocytes, may play a role in the response to stress induced by heat shock, osmotic stress and anoxia (PubMed:18439994).
Required for the developmental axon guidance and regrowth of PLM touch receptor neurons (PubMed:31983639).
Early in embryogenesis, plays a role in ciliary shape formation in sensory neurons (PubMed:28887031).
Promotes survival at high temperatures (PubMed:25061667).
Catalytic activity
- a 5'-end (N7-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H+ + N7-methyl-GDPThis reaction proceeds in the forward direction.
- a 5'-end (N2,N2,N7-trimethyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + H2O = a 5'-end phospho-ribonucleoside in mRNA + 2 H+ + N2,N2,N7-trimethyl-GDPThis reaction proceeds in the forward direction.
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Activity regulation
Inhibited by capped and uncapped RNA (PubMed:16199859).
Not inhibited by dinucleotide cap or methylated nucleotide analogs (PubMed:16199859).
Not inhibited by dinucleotide cap or methylated nucleotide analogs (PubMed:16199859).
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | P granule | |
Cellular Component | P-body | |
Cellular Component | perinuclear region of cytoplasm | |
Molecular Function | 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA] diphosphatase activity | |
Molecular Function | 5'-(N(7)-methylguanosine 5'-triphospho)-[mRNA] hydrolase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | RNA binding | |
Biological Process | deadenylation-dependent decapping of nuclear-transcribed mRNA | |
Biological Process | determination of adult lifespan | |
Biological Process | mRNA processing | |
Biological Process | nematode larval development | |
Biological Process | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay | |
Biological Process | regulation of locomotion | |
Biological Process | reproductive process | |
Biological Process | response to heat | |
Biological Process | response to oxidative stress | |
Biological Process | response to UV |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namem7GpppN-mRNA hydrolase dcap-2
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Nematoda > Chromadorea > Rhabditida > Rhabditina > Rhabditomorpha > Rhabditoidea > Rhabditidae > Peloderinae > Caenorhabditis
Accessions
- Primary accessionO62255
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Double RNAi-mediated knockdown with dcap-1 reduces survival at 20 degrees Celsius.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 287 | In var1; defective ADL, ADF, AWB and AWC sensory neuron cilia. | ||||
Sequence: R → E | ||||||
Mutagenesis | 291 | Abolishes mRNA decapping activity. | ||||
Sequence: E → Q |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000057135 | 1-786 | m7GpppN-mRNA hydrolase dcap-2 | |||
Sequence: MEISTENWCKKPKNRSIFSKNISFQKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPRIPTDILDELEFRFISNMVECEINDNIRVCFHLELAHWYYIDHMVEDDKISGCPNVGSRDFNFQMCQHCRVLRKYAHRADEVLAKFREYKSTVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKFYMVMPFVKDIQIYVQKEKEKLRRRKAEAVQSTPSSSIFSQLFPAQPPPPVPEDATPTRPMYKRLTSEELFSAFKNPPAGEVARPTLPDMSPAVNGLDTLAVLGICTPLKPGASLNEFSGAPQNCPMISEEAGSPADPSAEIGFAMPMDLKQPVVTSDHPWQHHKISDSSAPPQTLESHQGWLDTQLVNTIMHSPNHPLPPTSNSPATPTAVLGHLIGKPIQPQAILPQAATPTALGSAEKPKSSRISLSDNSAFKAISSTQKQSIPKATAAPPSTEKTRSASLSGSSQVVGKPARNLFNSVVSPVSSGIQSIQGDGGAWEDVWFREQLAATTTAGTSISSLAASNQELAMINREETPIEDPYFKQQAYQKAQKAQSLIPACSQWTNSIKLDIDYVVGPLSFWMQQFSTKSPVSGTGPQLP |
Proteomic databases
PTM databases
Expression
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 25-57 | Polar residues | ||||
Sequence: QKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQ | ||||||
Region | 25-148 | Disordered | ||||
Sequence: QKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQPSTSKPKKNEKRKKAVAQAPASAPAPGPEEKKKQPKRASVGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGPR | ||||||
Compositional bias | 97-147 | Polar residues | ||||
Sequence: VGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGP | ||||||
Domain | 238-366 | Nudix hydrolase | ||||
Sequence: STVPTYGAILVDPEMDHVVLVQSYFAKGKNWGFPKGKINQAEPPRDAAIRETFEETGFDFGIYSEKEKKFQRFINDGMVRLYLVKNVPKDFNFQPQTRKEIRKIEWFKIDDLPTDKTDELPAYLQGNKF | ||||||
Motif | 273-294 | Nudix box | ||||
Sequence: GKINQAEPPRDAAIRETFEETG | ||||||
Region | 556-576 | Disordered | ||||
Sequence: IMHSPNHPLPPTSNSPATPTA | ||||||
Region | 623-655 | Disordered | ||||
Sequence: ISSTQKQSIPKATAAPPSTEKTRSASLSGSSQV |
Sequence similarities
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
O62255-2
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Nameb
- Length786
- Mass (Da)87,369
- Last updated2008-09-02 v4
- Checksum45753599CA77D9B9
O62255-1
- Namea
- Differences from canonical
- 2-25: EISTENWCKKPKNRSIFSKNISFQ → ASNSTNSK
O62255-3
- Namec
- Differences from canonical
- 1-100: Missing
O62255-4
- Named
- Differences from canonical
- 1-190: Missing
Sequence caution
Features
Showing features for sequence conflict, alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 1-25 | in Ref. 2; ACE88255 | ||||
Sequence: MEISTENWCKKPKNRSIFSKNISFQ → MASNSTNSK | ||||||
Alternative sequence | VSP_060859 | 1-100 | in isoform c | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_060858 | 1-190 | in isoform d | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_014286 | 2-25 | in isoform a | |||
Sequence: EISTENWCKKPKNRSIFSKNISFQ → ASNSTNSK | ||||||
Compositional bias | 25-57 | Polar residues | ||||
Sequence: QKQNKSTEEPPSSVQKLLASLQQAQNKSDLSEQ | ||||||
Compositional bias | 97-147 | Polar residues | ||||
Sequence: VGARMQQQAENARISQTKRPRQVSTSKGSSRNTTAPEQQNYQQQQQQYKGP | ||||||
Sequence conflict | 214-786 | in Ref. 2; ACE88255 | ||||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DQ143943 EMBL· GenBank· DDBJ | AAZ73241.1 EMBL· GenBank· DDBJ | mRNA | ||
EU760346 EMBL· GenBank· DDBJ | ACE88255.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
BX284604 EMBL· GenBank· DDBJ | CAB05204.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL021488 EMBL· GenBank· DDBJ | CAB05204.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284604 EMBL· GenBank· DDBJ | CAB05206.4 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL021488 EMBL· GenBank· DDBJ | CAB05206.4 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284604 EMBL· GenBank· DDBJ | CDR32703.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX284604 EMBL· GenBank· DDBJ | CDR32704.1 EMBL· GenBank· DDBJ | Genomic DNA |