UniProt functional annotation for P14832

UniProt code: P14832.

Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Taxonomy: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
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. Regulates the meiotic gene program via the Set3C histone deacetylase complex to promote efficient sporulation, and the prolyl-isomerase activity is required for this function. {ECO:0000269|PubMed:11641409, ECO:0000269|PubMed:15643056, ECO:0000269|PubMed:8431466}.
Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0). {ECO:0000269|PubMed:8431466}.
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. {ECO:0000269|PubMed:10899127, ECO:0000269|PubMed:11711434, ECO:0000269|PubMed:15643056}.
Subcellular location: Cytoplasm. Nucleus. Mitochondrion intermembrane space.
Miscellaneous: Present with 86000 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
Similarity: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. {ECO:0000305}.
Similarity: Contains 1 PPIase cyclophilin-type domain. {ECO:0000255|PROSITE-ProRule:PRU00156}.

Annotations taken from UniProtKB at the EBI.