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J Biochem. 2002 Jan;131(1):113-9.

Identification of a novel unconventional myosin from scallop mantle tissue.

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  • 1Muroran Institute of Technology, Department of Applied Chemistry, Muroran, Hokkaido 050-0071, Japan.


We isolated a cDNA encoding a novel unconventional myosin from scallop mantle tissue (scallop unconventional myosin: ScunM) and determined the nucleotide sequence. It comprises 2,739 bp with 5' and 3'-noncoding sequences and has an open reading frame of 2,334 bp that encodes 778 amino acids. While ScunM has a motor domain and a short tail domain without having light chain-binding IQ motifs like myosin XIV, the deduced amino acid sequence exhibits low homology, 30-36%, to known myosins. Phylogenetic analysis of the motor domain suggested that ScunM belongs to a novel unconventional myosin class. ScunM has an insertion of 67 amino acids in the putative actin-binding site (loop2 site). Western blot analysis with an antibody produced against the N-terminal region revealed that ScunM was strongly expressed in the mantle and mantle pallial cell layer of scallop.

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