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Molecular cloning and characterization of rat brain 2′, 3′ ‐cyclic nucleotide 3′ ‐phosphodiesterase isoform 2
Author(s) -
Gravel M.,
DeAngelis D.,
Braun P. E.
Publication year - 1994
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490380302
Subject(s) - gene isoform , complementary dna , biology , peptide sequence , nucleic acid sequence , cyclic nucleotide phosphodiesterase , microbiology and biotechnology , phosphodiesterase , nucleotide , cloning (programming) , molecular cloning , genetics , coding region , sequence motif , amino acid , consensus sequence , sequence alignment , homology (biology) , biochemistry , gene , enzyme , computer science , programming language
We have isolated a cDNA coding for the larger isoform of the rat brain 2′,3′ ‐cyclic nucleotide 3′ ‐phosphodiesterase (CNP2), a protein associated with myelination in the central nervous system (CNS). The complete 420 amino acid sequence was deduced from the nucleotide sequence of the cDNA. Sequence comparisons show that rat CNP shares 96% homology with mouse, 84% with bovine, and 86% with human CNP. Errors in the published sequence of rat CNP1 have now been corrected. Comparisons with other proteins reveal several interesting conserved motifs, including two leucine repeat heptads, and two consensus motifs for phosphorylation in the N‐terminal domain of CNP2.© 1994 Wiley‐Liss, Inc.