3.0
Summary
| Name |  PPIFView Modifications |
| Full Name | Peptidyl-prolyl cis-trans isomerase F, mitochondrial |
| Synonyms | PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Mitochondrial cyclophilin, CyP-M, Rotamase F | CYP3 |
| Primary ID | P30405 |
| Links |  -  -  |
| Type | protein |
| Relations | 2 |
| Function | PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:26387735). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). |
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phosphorylation