DCP2
Function
Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs (PubMed:12218187, PubMed:12417715, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (PubMed:12486012, PubMed:12923261, PubMed:21070968, PubMed:28002401, PubMed:31875550). Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay (PubMed:14527413). Plays a role in replication-dependent histone mRNA degradation (PubMed:18172165). Has higher activity towards mRNAs that lack a poly(A) tail (PubMed:21070968). Has no activity towards a cap structure lacking an RNA moiety (PubMed:21070968). The presence of a N(6)-methyladenosine methylation at the second transcribed position of mRNAs (N(6),2'-O-dimethyladenosine cap; m6A(m)) provides resistance to DCP2-mediated decapping (PubMed:28002401). Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degradation of their transcripts (PubMed:26098573).
Post-translational modifications
Phosphorylated at ser-249 in a MTOR-dependent manner (PubMed:26098573).
Sequence Similarities
Belongs to the Nudix hydrolase family. DCP2 subfamily.
Tissue Specificity
Expressed in brain and testis. Not detected in heart (at protein level).
Cellular localization
- Cytoplasm
- P-body
- Nucleus
- Predominantly cytoplasmic, in processing bodies (PB) (PubMed:15273322). A minor amount is nuclear (PubMed:15273322).
Alternative names
NUDT20, DCP2, m7GpppN-mRNA hydrolase, Nucleoside diphosphate-linked moiety X motif 20, mRNA-decapping enzyme 2, Nudix motif 20, hDpc