The domain within your query sequence starts at position 17 and ends at position 363; the E-value for the Vinculin domain shown below is 5.1e-66.



PFAM accession number:PF01044
Interpro abstract (IPR006077):

Vinculin is a eukaryotic protein that seems to be involved in the attachment of the actin-based microfilaments to the plasma membrane. Vinculin is located at the cytoplasmic side of focal contacts or adhesion plaques [ (PUBMED:2112986) ]. In addition to actin, vinculin interacts with other structural proteins such as talin and alpha-actinins.

Vinculin is a large protein of 116kDa (about a 1000 residues). Structurally the protein consists of an acidic N-terminal domain of about 90kDa separated from a basic C-terminal domain of about 25kDa by a proline-rich region of about 50 residues. The central part of the N-terminal domain consists of a variable number (3 in vertebrates, 2 in Caenorhabditis elegans) of repeats of a 110 amino acids domain.

Alpha-catenins are proteins of about 100kDa which are evolutionary related to vinculin [ (PUBMED:1924379) ]. Catenins are proteins that associate with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Three different types of catenins seem to exist: alpha, beta, and gamma. In terms of their structure the most significant differences are the absence, in alpha-catenin, of the repeated domain and of the proline-rich segment.

GO process:cell adhesion (GO:0007155)
GO function:actin filament binding (GO:0051015)

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Vinculin