PROSITE documentation PDOC51126
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.

Last update:

June 2005 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

DILUTE, PS51126; Dilute domain profile  (MATRIX)


1AuthorsOliver T.N. Berg J.S. Cheney R.E.
TitleTails of unconventional myosins.
SourceCell. Mol. Life Sci. 56:243-257(1999).
PubMed ID11212352

2AuthorsCatlett N.L. Duex J.E. Tang F. Weisman L.S.
TitleTwo distinct regions in a yeast myosin-V tail domain are required for the movement of different cargoes.
SourceJ. Cell Biol. 150:513-526(2000).
PubMed ID10931864

3AuthorsPonting C.P.
TitleAF-6/cno: neither a kinesin nor a myosin, but a bit of both.
SourceTrends Biochem. Sci. 20:265-266(1995).
PubMed ID7667878

4AuthorsPashkova N. Catlett N.L. Novak J.L. Wu G. Lu R. Cohen R.E. Weisman L.S.
TitleMyosin V attachment to cargo requires the tight association of two functional subdomains.
SourceJ. Cell Biol. 168:359-364(2005).
PubMed ID15684027

5AuthorsTakai Y. Nakanishi H.
TitleNectin and afadin: novel organizers of intercellular junctions.
SourceJ. Cell Sci. 116:17-27(2003).
PubMed ID12456712

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