DIL

DIL
SMART accession number:SM01132
Description: The DIL domain has no known function.
Interpro abstract (IPR002710):

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 [(PUBMED:11212352)].

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 [(PUBMED:10931864)]. 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 [(PUBMED:7667878)]. 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 [(PUBMED:10931864), (PUBMED:15684027)].

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 [(PUBMED:12456712)]. The dilute domain of afadin appears to be responsible for actin stress fibre formation [(PUBMED:25712270)].

Family alignment:
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There are 6872 DIL domains in 6863 proteins in SMART's nrdb database.

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