cyclophilin D (cyclophilin 40, 40 kD peptidyl-prolyl cis-trans isomerase, PPID, CYP40, CYPD)
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Function
- PPIases accelerate the folding of proteins
- catalyzes cis-trans isomerization of proline imidic peptide bonds in oligopeptides
- binds ESR1 (putative)
- less sensitive to inhibition by cyclosporin A than is CYP-18
peptidylproline (omega=180) <--> peptidylproline (omega=0)
Structure
- belongs to the cyclophilin-type PPIase family, PPIase D subfamily
- contains 1 PPIase cyclophilin-type domain contains 3 TPR repeats
Compartment
Expression
widely expressed
More general terms
References
- ↑ Martinus RD et al Role of chaperones in the biogenesis and maintenance of the mitochondrion. FASEB J. 1995 Mar;9(5):371-8. Review. PMID: https://www.ncbi.nlm.nih.gov/pubmed/7896006
- ↑ Wikipedia; note=cyclophilin entry http://en.wikipedia.org/wiki/cyclophilin
- ↑ UniProt http://www.uniprot.org/uniprot/Q08752.html