Decapping Enzyme 2 (DCP2)

DCP2 is a key component of an mRNA-decapping complex required for removal of the 5-prime cap from mRNA prior to its degradation from the 5-prime end .

Epitope-tagged DCP2 localized to punctate cytoplasmic foci, with some nuclear staining.The deduced protein contains 3 conserved regions: the 109-amino acid Nudix fold and its flanking A and B boxes. The Nudix motif within the fold contains 2 glutamic acids (glu147 and glu148) critical for metal ion coordination and pyrophosphatase activity. Western blot analysis detected endogenous DCP2 at an apparent molecular mass of 45 kD in cytoplasmic fractions of K562 cells. DCP2 predominantly cosedimented with polysomes.