UniProt functional annotation for Q12461

UniProt code: Q12461.

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. Acts as a regulatory subunit for TAP42-associated PP2A-like phosphatases modulating their activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2Ai) in presence of ATP and Mg(2+) by dissociating the inactive form from the complex. Acts also inhibitory at high concentrations. Involved in the regulation of cell cycle progression, mitotic spindle formation and bud morphogenesis. {ECO:0000269|PubMed:11134337, ECO:0000269|PubMed:11262194, ECO:0000269|PubMed:12952889, ECO:0000269|PubMed:15447631, ECO:0000269|PubMed:15689491, ECO:0000269|PubMed:16380387}.
 
Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0).
Subunit: Interacts with the phosphatase PP2A catalytic subunits PPH21 and PPH22. Forms a ternary complex with PPH21-TAP42. {ECO:0000269|PubMed:12952889, ECO:0000269|PubMed:15447631, ECO:0000269|PubMed:15689491}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Miscellaneous: Present with 2430 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.

Annotations taken from UniProtKB at the EBI.