PMID:15998457

Citation	Wang, P and Heitman, J (2005) The cyclophilins. Genome Biol. 6:226
Abstract	Cyclophilins (Enzyme Commission (EC) number 5.1.2.8) belong to a group of proteins that have peptidyl-prolyl cis-trans isomerase activity; such proteins are collectively known as immunophilins and also include the FK-506-binding proteins and the parvulins. Cyclophilins are found in all cells of all organisms studied, in both prokaryotes and eukaryotes; humans have a total of 16 cyclophilin proteins, Arabidopsis up to 29 and Saccharomyces 8. The first member of the cyclophilins to be identified in mammals, cyclophilin A, is the major cellular target for, and thus mediates the actions of, the immunosuppressive drug cyclosporin A. Cyclophilin A forms a ternary complex with cyclosporin A and the calcium-calmodulin-activated serine/threonine-specific protein phosphatase calcineurin; formation of this complex prevents calcineurin from regulating cytokine gene transcription. Recent studies have implicated a diverse array of additional cellular functions for cyclophilins, including roles as chaperones and in cell signaling.
Links	PubMed PMC1175980 Online version:10.1186/gb-2005-6-7-226
Keywords	Animals; Arabidopsis/enzymology; Arabidopsis/genetics; Cyclophilins/chemistry; Cyclophilins/genetics; Cyclophilins/metabolism; Drosophila/enzymology; Drosophila/genetics; Evolution, Molecular; Humans; Protein Folding; Saccharomyces/enzymology; Saccharomyces/genetics
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
PSYA2:Q4FTV6		GO:0003755: peptidyl-prolyl cis-trans isomerase activity	ECO:0000314:		F		Fig 1 shows the cis and trans forms of proline that were catalyzed by cyclophilins and peptidyl-prolyl isomerases.	complete CACAO 9569

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