Class V myosin, motor domain (IPR036103)

Short name: MYSc_Myo5

Overlapping homologous superfamilies

Domain relationships


Class V myosins have been shown to play a role in both membrane trafficking and RNA transport [PMID: 10722875]. There are two type V myosins in yeast, which appear to have nonoverlapping functions. In Schizosaccharomyces pombe Myo52 is involved in growth polarity and cytokinesis, whereas Myo51 is a component of the cytokinetic actin ring [PMID: 11112691]. Similarly, Saccharomyces cerevisiae Myo2 is essential for polarized growth, most likely through transport of secretory vesicles to the developing bud [PMID: 10931864], while Myo4 has been proposed to transport a mRNA needed to repress mating type switching in daughter cells [PMID: 9288973]. Mice and humans possess three class V myosins (Myo5A, Myo5B, and Myo5C). Possible cargoes for myosin-V in mammals include melanosomes, synaptic vesicles [PMID: 11980908, PMID: 11212351, PMID: 14610051] and organelles in neurons [PMID: 23990471]. Mutations in myo5A cause Griscelli syndrome type-1 (GS1) and neuroectodermal melanolysosomal disease, or Elejalde disease [PMID: 21508232].

This entry represents the motor (head) domain of class V myosins [PMID: 14508494]. The motor domain has ATPase activity and belongs to the larger group of P-loop NTPases.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.