Integrin alpha chain, C-terminal cytoplasmic region, conserved site
IPR018184
Definition
Some alpha subunits are cleaved post- translationally to produce a heavy and a light chain linked by a disulphide bond [[cite:PMID:3028640], [cite:PMID: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 PMID:3327687. It has been predicted that these repeats assume the β-propeller fold. The domains contain seven four-stranded β-sheets arranged in a torus around a pseudosymmetry axis PMID:8990162. Integrin ligands and a putative Mg2+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 β-propeller fold) binds the G protein alpha subunit PMID: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 PMID: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 α 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.
16 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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