Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14. Interacts with CALM and F-actin (PubMed:11940582). Interacts (via SH3 domain) with SYNJ1, DNM1 and DNM2 (PubMed:17257598). Interacts with ARL14EP (PubMed:21458045). Interacts with CARMIL1 (PubMed:19846667). Colocalizes with F-actin (By similarity). In cultured podocytes, it localizes close to and is associated with the cytoplasmic membrane, with enrichment at the lamellipodia tips. Colocalizes with cytoplasmic vesicles, including endocytic clathrin-coated vesicles. Colocalizes with dynamin at cytoplasmic vesicles. Expressed in the immune system. In the kidney, predominantly expressed in the glomerulus, including podocytes. The disease is caused by variants affecting the gene represented in this entry. Belongs to the TRAFAC class myosin-kinesin ATPase superfamily. Myosin family. Represents an unconventional myosin. This protein should not be confused with the conventional myosin-1 (MYH1).