PPIF
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).
Post-translational modifications
Acetylated at Lys-167; deacetylated at Lys-167 by SIRT3.
Sequence Similarities
Belongs to the cyclophilin-type PPIase family.
Cellular localization
- Mitochondrion matrix
Alternative names
CYP3, PPIF, PPIase F, Cyclophilin D, Cyclophilin F, Mitochondrial cyclophilin, Rotamase F, CyP-D, CypD, CyP-M