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Publication : The mouse muscle creatine kinase cDNA and deduced amino acid sequences: comparison to evolutionarily related enzymes.

First Author  Buskin JN Year  1985
Journal  J Mol Evol Volume  22
Issue  4 Pages  334-41
PubMed ID  3003372 Mgi Jnum  J:8175
Mgi Id  MGI:56644 Doi  10.1007/BF02115689
Citation  Buskin JN, et al. (1985) The mouse muscle creatine kinase cDNA and deduced amino acid sequences: comparison to evolutionarily related enzymes. J Mol Evol 22(4):334-41
abstractText  The nucleotide sequence of cloned DNA corresponding to full-length mouse muscle creatine kinase mRNA has been determined. This 1415 base pair DNA sequence and the deduced 381 amino acid sequence of the protein have been compared to creatine kinase sequences from other vertebrate species and to invertebrate guanidino kinase sequences. These comparisons show that the vertebrate muscle creatine kinases constitute a remarkably conserved protein family with a unit evolutionary period of 30. The creatine kinases also retain marked sequence similarity with the more distantly related invertebrate guanidino kinases. A portion of the sequence, presumably part of the ATP binding site, shows similarity to other nucleotide binding proteins with diverse functions. Comparisons of the untranslated regions of the creatine kinase cDNA sequences show that the 5' untranslated regions are more highly conserved than are the 3' untranslated regions; this may point to some regulatory function in the 5' region.
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