Cyclophilin-type peptidyl-prolyl cis-trans isomerase (IPR024936)

Short name: Cyclophilin-type_PPIase

Overlapping homologous superfamilies

Family relationships


Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (EC:, accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [PMID: 14731520, 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 represents the cyclophilin peptidyl-prolyl cis-trans isomerase family. The family includes RING-type E3 ubiquitin-protein ligase PPIL2, which is thought to be an inactive PPIase [PMID: 20676357].

GO terms

Biological Process

No terms assigned in this category.

Molecular Function

GO:0003755 peptidyl-prolyl cis-trans isomerase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.