Recombinant Human Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIF)

Uniprot Id

P30405

Target Species

Human

Target Name

PPIF

Target Full Name

Peptidyl-prolyl cis-trans isomerase F, mitochondrial

Target Function

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). 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. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis. Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels. Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis.

Target Subcellular Location

Mitochondrion matrix.

Target Protein Families

Cyclophilin-type PPIase family

Target Synonyms

Cyclophilin 3; cyclophilin D; Cyclophilin F; Cyp D; CyP M; CyP-D; CyP-M; CYP3; CypD; hCyP3; mitochondrial; Mitochondrial cyclophilin; Peptidyl prolyl cis trans isomerase, mitochondral; Peptidyl-prolyl cis-trans isomerase F; Peptidyl-prolyl cis-trans isomerase F, mitochondrial; Peptidylprolyl isomerase F (cyclophilin F); Peptidylprolyl isomerase F; PPIase; PPIase F; Ppif; PPIF_HUMAN; Rotamase; Rotamase F

Target Background

The protein encoded by this gene is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. This protein is part of the mitochondrial permeability transition pore in the inner mitochondrial membrane. Activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death.