Sequence similarities between chicken intestinal 110-kDa ATPase and myosin I-like enzymes
- Resource Type
- Article
- Authors
- Atkinson, Mark A. L.; Collins, Jimmy H.
- Source
- Journal of Protein Chemistry; August 1989, Vol. 8 Issue: 4 p495-498, 4p
- Subject
- Language
- ISSN
- 02778033
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.