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cyclophilin D (cyclophilin 40, 40 kD peptidyl-prolyl cis-trans isomerase, PPID, CYP40, CYPD)
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: cytoplasm
Expression: widely expressed
General
chaperonin; chaperone
cyclophilin
nuclear protein
Properties
SIZE: MW = 40 kD
COMPARTMENT: cell nucleus
cytoplasm
MOTIF: active site
Database Correlations
OMIM 601753
UniProt Q08752
Entrez Gene 5481
ENZYME 5.2.1.8
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: 7896006
- Wikipedia; note=cyclophilin entry
http://en.wikipedia.org/wiki/cyclophilin
- UniProt :accession Q08752