| Description | This entry represents the catalytic domain of CNP, which catalyses the hydrolysis of nucleoside 2',3'-cyclic monophosphates to nucleoside 2'-monophosphates [ ].This entry includes the eukaryotic protein 2',3'-cyclic nucleotide 3'-phosphodiesterase (CNPase) [ ]. CNPase is one of the earliest myelin-related proteins expressed in differentiating oligodendrocytes and Schwann cells. CNPase is abundant in the central nervous system and in oligodendrocytes []. This protein is also found in mammalian photoreceptor cells, testis and lymphocytes. It may participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin []. CNP selectively cleaves 2',3'-cyclic nucleotides to produce 2'-nucleotides. Although physiologically relevant substrates with 2',3'-cyclic termini are still unknown, numerous cyclic phosphate containing RNAs occur transiently within eukaryotic cells. Other known protein families capable of hydrolysing 2',3'-cyclic nucleotides include tRNA ligases and plant cyclic phosphodiesterases. The catalytic domains from all these proteins contain two tetra-peptide motifs H-X-T/S-X, where X is usually a hydrophobic residue. Mutation of either histidine in CNPase abolishes enzymatic activity []. | Name | Cyclic nucleotide phosphodiesterase, catalytic domain |
| Short Name | CNPase_cat | Type | Domain |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
