The domain within your query sequence starts at position 1131 and ends at position 1145; the E-value for the Integrin_alpha domain shown below is 4.3e-7.



PFAM accession number:PF00357
Interpro abstract (IPR018184):

Some alpha subunits are cleaved post- translationally to produce a heavy and a light chain linked by a disulphide bond [ (PUBMED:3028640) (PUBMED:2199285) ]. Integrin alpha chains share a conserved sequence which is found at the beginning of the cytoplasmic domain, just after the end of the transmembrane region. Within the N-terminal domain of alpha subunits, seven sequence repeats, each of approximately 60 amino acids, have been found [ (PUBMED:3327687) ]. It has been predicted that these repeats assume the beta-propeller fold. The domains contain seven four-stranded beta-sheets arranged in a torus around a pseudosymmetry axis [ (PUBMED:8990162) ]. Integrin ligands and a putative Mg 2+ ion are predicted to bind to the upper face of the propeller, in a manner analogous to the way in which the trimeric G-protein beta subunit (G beta) (which also has a beta-propeller fold) binds the G protein alpha subunit [ (PUBMED:8990162) ].

Integrin cytoplasmic domains are normally less than 50 amino acids in length, with the beta-subunit sequences exhibiting greater homology to each other than the alpha-subunit sequences [ (PUBMED:12826403) ]. This is consistent with current evidence that the beta subunit is the principal site for binding of cytoskeletal and signalling molecules, whereas the alpha subunit has a regulatory role. The first ten residues of the alpha-subunit cytoplasmic domain appear to form an alpha helix that is terminated by a proline residue. The remainder of the domain is highly acidic in nature and this loops back to contact the membrane-proximal lysine anchor residue.

This entry represents the conserved site of the C-terminal integrin alpha chain.

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