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peptidyl-prolyl cis-trans isomerase-like 1 (PPIase, rotamase, PPIL1, CYPL1, CGI-124, UNQ2425/PRO4984)
Function:
1) PPIases accelerate the folding of proteins
2) catalyzes cis-trans isomerization of proline imidic peptide bonds in oligopeptides
3) role in pre-mRNA splicing, component of spliceosome C complex
peptidylproline (omega=180) peptidylproline (omega=0)
Inhibition:
- inhibited by Cyclosporin A
Kinetic parameters:
- KM=230 uM for N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilid
Structure:
- belongs to the cyclophilin-type PPIase family, PPIL1 subfamily
- contains 1 PPIase cyclophilin-type domain
Expression:
- ubiquitous, most abundant in heart & skeletal muscle
General
peptidyl-prolyl cis/trans isomerase (PPIase) or rotamase
Properties
SIZE: MW = 18 kD
entity length = 166 aa
MOTIF: active site
SITE: 10-164
MOTIF: Cyclosporin A binding {54-65}
Cyclosporin A binding {70-71}
Cyclosporin A binding {99-104}
Cyclosporin A binding {109-113}
binding site
SITE: 119-119
FOR-BINDING-OF: Cyclosporin A
binding site
SITE: 125-125
FOR-BINDING-OF: Cyclosporin A
Database Correlations
OMIM 601301
UniProt Q9Y3C6
Pfam PF00160
ENZYME 5.2.1.8
References
UniProt :accession Q9Y3C6
Component-of
spliceosome C complex