 The protein is made up of the two folding domains, the leucine zipper-like domain at the N-terminal and an olfactomedin-like domain at the C-terminal.The domain at the N-terminal is known to have 77.6% homology to the myosin heavy chain of "Dictyostelium discoideum" and 25% homology with the cardiac β-myosin heavy chain.The gene encodes three different exons, each consisting of different structural and functional domains.