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      Cloning and mRNA expression of human unconventional myosin-IC. A homologue of amoeboid myosins-I with a single IQ motif and an SH3 domain.

      Journal of Molecular Biology
      Acanthamoeba, chemistry, Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Dictyostelium, Humans, Molecular Sequence Data, Myosins, genetics, RNA, Messenger, biosynthesis, Sequence Homology, Amino Acid

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          Abstract

          The complete deduced amino acid sequence and mRNA expression of human unconventional myosin-IC (HuncM-IC) are described. Sequencing of overlapping cDNA clones reveals a message of 4666 nucleotides with a single open reading frame predicted to encode a 127 kDa protein of 1109 amino acids. HuncM-IC is composed of three discrete regions: a characteristic N-terminal myosin head with predicted actin and ATP-binding sites; a neck domain with an "IQ motif", predicted to bind a single light chain; and a C-terminal tail with a putative membrane-binding site. In addition, the tail contains an src-homology 3 domain. The presence of a single IQ motif and an src-homology 3 domain is reminiscent of "long-tailed" myosins-I from amoeboid organisms, a supposition confirmed by multiple sequence alignment. Northern blot analysis of human tissues shows that HuncM-IC is ubiquitously expressed, with the highest levels in kidney, prostate, colon, liver and ovary. The results show that "amoeboid" myosins-I are not restricted to amoeboid organisms, rather they are expressed in the metazoa as well.

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