S. cerevisiae Gene CPR1 (YDR155C)
  Description: Cytoplasmic peptidyl-prolyl cis-trans isomerase (cyclophilin), catalyzes the cis-trans isomerization of peptide bonds N-terminal to proline residues binds the drug cyclosporin A
Transcript (Including UTRs)
   Position: sacCer3 chrIV:768,512-769,000 Size: 489 Total Exon Count: 1 Strand: -
Coding Region
   Position: sacCer3 chrIV:768,512-769,000 Size: 489 Coding Exon Count: 1 

Page IndexSequence and LinksUniProtKB CommentsProtein StructureOther SpeciesGO Annotations
mRNA DescriptionsOther NamesMethods
Data last updated at UCSC: 2011-08-29

-  Sequence and Links to Tools and Databases
Genomic Sequence (chrIV:768,512-769,000)mRNAProtein (162 aa)
Gene SorterGenome BrowserOther Species FASTASGDUniProtKB

-  Comments and Description Text from UniProtKB
DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase; Short=PPIase; EC=; AltName: Full=Cyclophilin; Short=CPH; AltName: Full=Cyclosporin A-binding protein; AltName: Full=PPI-II; AltName: Full=Rotamase;
FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Involved in histone deacetylase complexes, suggesting a function in chromatin. Imports fructose-1,6- bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles.
CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline (omega=0).
ENZYME REGULATION: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
SUBUNIT: Interacts with a complex composed of SIN3 and RPD3. Identified in the Set3C complex with HOS2, HST1, SNT1, SIF2, HOS4/YIL112W and SET3.
MISCELLANEOUS: Present with 86000 molecules/cell in log phase SD medium.
SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily.
SIMILARITY: Contains 1 PPIase cyclophilin-type domain.

-  Protein Domain and Structure Information
  InterPro Domains: Graphical view of domain structure
IPR002130 - Cyclophilin-like_PPIase_dom
IPR024936 - Cyclophilin-type_PPIase
IPR020892 - Cyclophilin-type_PPIase_CS

Pfam Domains:
PF00160 - Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD

Protein Data Bank (PDB) 3-D Structure
MuPIT help

- X-ray

- X-ray

ModBase Predicted Comparative 3D Structure on P14832
The pictures above may be empty if there is no ModBase structure for the protein. The ModBase structure frequently covers just a fragment of the protein. You may be asked to log onto ModBase the first time you click on the pictures. It is simplest after logging in to just click on the picture again to get to the specific info on that model.

-  Orthologous Genes in Other Species
  Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.
HumanMouseRatZebrafishD. melanogasterC. elegans
Genome BrowserGenome BrowserGenome BrowserNo orthologGenome BrowserGenome Browser
Gene DetailsGene DetailsGene Details Gene DetailsGene Details
Gene SorterGene SorterGene Sorter Gene SorterGene Sorter