Identification of a novel unconventional myosin from scallop mantle tissue.
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.
Hasegawa
Yasushi
Y
Muroran Institute of Technology, Department of Applied Chemistry, Muroran, Hokkaido 050-0071, Japan. hasegawa@mmm.muroran-it.ac.jp
Araki
Takahiro
T
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000032:analysis / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008974:Mollusca / Q000737:chemistry / Q000235:genetics*; D016254:Mutagenesis, Insertional; D009218:Myosins / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
D000199:Actins; D018076:DNA, Complementary; D009218:Myosins