Cyclophilin-type peptidyl-prolyl cis-trans isomerase, cyclophilin A-like
IPR044666
Definition
Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity ([ec:5.2.1.8]), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [[cite:PMID:14731520], [cite:PMID:2186809]]. They also have protein chaperone-like functions PMID:15998457 and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates PMID:14731520. Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function PMID:21309470. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation PMID:21295323. This entry includes eukaryotic, bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase, Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin [[cite:PMID:8652511], [cite:PMID:8263916]]. This entry also includes proteins that do not have the peptidyl-prolyl cis-trans isomerase activity, such as CWC27 from humans PMID:20676357.
5 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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