CaM is involved in most of the important signaling pathways in the cell.
Most of the characterized Calmodulin binding domains of target proteins are stretches of 16 to 35 amino acids that show a segregation of basic and polar residues on one side of an alpha-helical configuration, and hydrophobic amino acids on the other. In many cases, the CaM-binding domain of target proteins constitutes, or is adjacent to, an autoinhibitory domain. Additional information about these processes can be found at the CaMKII site. CaM localization in the rhabdomere, a microvillar structure in the photoreceptor cell, is disrupted in ninaC mutants. NinaC myosin activity might be regulated by Calmodulin, since the properties of at least some unconventional myosins are affected by Calmodulin association.