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The mouse muscle creatine kinase cDNA and deduced amino acid sequences: Comparison to evolutionarily related enzymes
Authors:J N Buskin  J B Jaynes  J S Chamberlain  S D Hauschka
Institution:(1) Department of Biochemistry, University of Washington, 98195 Seattle, Washington, USA;(2) Present address: Division of Medical Genetics, Baylor College of Medicine, 77030 Houston, Taxas
Abstract:Summary 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 5prime untranslated regions are more highly conserved than are the 3prime untranslated regions; this may point to some regulatory function in the 5prime region.
Keywords:Creatine kinase  cDNA  Muscle  Guanidino kinase  Nucleotide binding  Kinase
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