| Function | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Proposed to act as a co-chaperone in HSP90 complexes such as in unligated steroid receptors heterocomplexes. Different co-chaperones seem to compete for association with HSP90 thus establishing distinct HSP90-co-chaperone-receptor complexes with the potential to exert tissue-specific receptor activity control. May have a preference for estrogen receptor complexes and is not found in glucocorticoid receptor complexes. May be involved in cytoplasmic dynein-dependent movement of the receptor from the cytoplasm to the nucleus. May regulate MYB by inhibiting its DNA-binding activity. Involved in regulation of AHR signaling by promoting the formation of the AHR:ARNT dimer.the function is independent of HSP90 but requires the chaperone activity. Involved in regulation of UV radiation-induced apoptosis. Promotes cell viability in anaplastic lymphoma kinase-positive anaplastic large-cell lymphoma (ALK+ ALCL) cell lines. (Microbial infection) May be involved in hepatitis C virus (HCV) replication and release. |
| Protein Name | Peptidyl-Prolyl Cis-Trans Isomerase DPpiase D40 Kda Peptidyl-Prolyl Cis-Trans IsomeraseCyclophilin-40Cyp-40Cyclophilin-Related ProteinRotamase D |
| Database Links | Reactome: R-HSA-8939211 |
| Cellular Localisation | CytoplasmNucleusNucleolusNucleoplasm |
| Alternative Protein Names | Peptidyl-Prolyl Cis-Trans Isomerase D proteinPpiase D protein40 Kda Peptidyl-Prolyl Cis-Trans Isomerase proteinCyclophilin-40 proteinCyp-40 proteinCyclophilin-Related Protein proteinRotamase D proteinPPID proteinCYP40 proteinCYPD protein |
Information sourced from Uniprot.org
