Sequence similarities between chicken intestinal 110-kDa ATPase and myosin I-like enzymes.
We report the partial amino acid sequence of chicken intestinal microvillar 110-kDa protein that, as a complex with calmodulin, has previously been shown to exhibit myosin-like ATPase and actin-binding activities. The sequence shows a high degree of similarity to the sequence of a novel vertebrate myosin I-like heavy chain encoded by a cDNA isolated from bovine intestine. This confirms that the bovine and chicken proteins are the first examples of Acanthamoeba myosin I-like proteins from higher eukaryotes. Comparison of available structural and functional data leads us to postulate that the myosin I family of proteins result from the fusion of a conserved myosin headlike motor domain, with variable COOH-terminal domains responsible for binding to specific intracellular structures.
Atkinson
M A
MA
Department of Biochemistry, University of Texas Health Center, Tyler 75710.
Collins
J H
JH
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D007422:Intestines / Q000201:enzymology*; D008969:Molecular Sequence Data; D009218:Myosins / Q000032:analysis*
D000251:Adenosine Triphosphatases; D009218:Myosins