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cyclophilin B (peptidyl-prolyl cis-trans isomerase B, S-cyclophilin, CypB, PPIB, SCYLP, CYP-S)
Function:
- PPIases accelerate the folding of proteins
- catalyzes cis-trans isomerization of proline imidic peptide bonds in oligopeptides
- cyclosporin A binds to & inhibits cyclophilin B
peptidylproline (omega=180) peptidylproline (omega=0)
Structure:
- belongs to the cyclophilin-type PPIase family, PPIase B subfamily
- contains 1 PPIase cyclophilin-type domain
Compartment:
- endoplasmic reticulum lumen, melanosome
Note:
- identified by mass spectrometry in melanosome fractions from stage I to stage IV
Interactions
molecular events
General
chaperonin; chaperone
cyclophilin
Properties
SIZE: entity length = 208 aa
MW = 23 kD
COMPARTMENT: endoplasmic reticulum
MOTIF: signal sequence {1-25}
active site
SITE: 39-196
Prevents secretion from ER {205-208}
Database Correlations
OMIM 123841
MORBIDMAP 123841
UniProt P23284
Entrez Gene 5479
Kegg hsa/hsa04020
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
- UniProt :accession P23284
Component-of
molecular complex