{PDOC51126} {PS51126; DILUTE} {BEGIN} ************************* * Dilute domain profile * ************************* The myosin superfamily consists of at least 15 distinct classes of presumed actin-based molecular motors. All members of the superfamily share a similar motor domain and a tail portion which is diagnostic of the class [1]. Class V myosins are actin-based molecular motors that function in relatively long-range movements of many intracellular cargoes including organelles, membrane vesicles, and mRNA [2]. These motors are ubiquitously found in all eukaryotes. Class V myosins are characterised by the presence of a conserved globular domain at the C-terminus of the tail portion: the dilute domain [3]. Myosin V moves via attachment of its amino terminal head (motor) domain to actin cables; its carboxyl terminal dilute domain anchors it to cargoes via attachments to organelle-specific receptors [2,4]. The dilute domain is also found in the afadin family. Afadins are nectin and actin filament-binding proteins that connect nectin to the actin cytoskeleton [5]. The profile we developed covers the whole dilute domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: June 2005 / First entry. [ 1] Oliver T.N., Berg J.S., Cheney R.E. "Tails of unconventional myosins." Cell. Mol. Life Sci. 56:243-257(1999). PubMed=11212352 [ 2] Catlett N.L., Duex J.E., Tang F., Weisman L.S. "Two distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes." J. Cell Biol. 150:513-526(2000). PubMed=10931864 [ 3] Ponting C.P. "AF-6/cno: neither a kinesin nor a myosin, but a bit of both." Trends Biochem. Sci. 20:265-266(1995). PubMed=7667878 [ 4] Pashkova N., Catlett N.L., Novak J.L., Wu G., Lu R., Cohen R.E., Weisman L.S. "Myosin V attachment to cargo requires the tight association of two functional subdomains." J. Cell Biol. 168:359-364(2005). PubMed=15684027; DOI=10.1083/jcb.200407146 [ 5] Takai Y., Nakanishi H. "Nectin and afadin: novel organizers of intercellular junctions." J. Cell Sci. 116:17-27(2003). PubMed=12456712 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}