Names & Taxonomy

Uniprot ID:
P30405
Entry Name:
PPIF_HUMAN
Status:
reviewed
Protein Names:
Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Mitochondrial cyclophilin) (CyP-M) (Rotamase F)
Gene Names:
PPIF CYP3
Gene Names Primary:
PPIF
Organism:
Homo sapiens (Human)

Structure

Length:
207
Sequence:
MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS
Proteomes:
UP000005640

Subcellular location

Subcellular Location:
Mitochondrion matrix

Function

Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. 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 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.
Catalytic Activity:
Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme Regulation:
ENZYME REGULATION: Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP.
Cross Reference Drug Bank:
DB00091 DB00172
Gene Ontology Go:
membrane
mitochondrial inner membrane
mitochondrial matrix
cyclosporin A binding
peptidyl-prolyl cis-trans isomerase activity
apoptotic mitochondrial changes
cellular response to arsenic-containing substance
cellular response to calcium ion
cellular response to hydrogen peroxide
necroptotic process
negative regulation of apoptotic process
negative regulation of ATPase activity
negative regulation of intrinsic apoptotic signaling pathway
negative regulation of oxidative phosphorylation
negative regulation of oxidative phosphorylation uncoupler activity
negative regulation of release of cytochrome c from mitochondria
positive regulation of release of cytochrome c from mitochondria
protein folding
regulation of mitochondrial membrane permeability
regulation of mitochondrial membrane permeability involved in programmed necrotic cell death
regulation of necrotic cell death
regulation of proton-transporting ATPase activity, rotational mechanism
response to ischemia
Gene Ontology Biological Process:
apoptotic mitochondrial changes
cellular response to arsenic-containing substance
cellular response to calcium ion
cellular response to hydrogen peroxide
necroptotic process
negative regulation of apoptotic process
negative regulation of ATPase activity
negative regulation of intrinsic apoptotic signaling pathway
negative regulation of oxidative phosphorylation
negative regulation of oxidative phosphorylation uncoupler activity
negative regulation of release of cytochrome c from mitochondria
positive regulation of release of cytochrome c from mitochondria
protein folding
regulation of mitochondrial membrane permeability
regulation of mitochondrial membrane permeability involved in programmed necrotic cell death
regulation of necrotic cell death
regulation of proton-transporting ATPase activity, rotational mechanism
response to ischemia
Gene Ontology Molecular Function:
cyclosporin A binding
peptidyl-prolyl cis-trans isomerase activity
Gene Ontology Cellular Component:
membrane
mitochondrial inner membrane
mitochondrial matrix
Keywords:
3D-structure
Acetylation
Alternative splicing
Apoptosis
Complete proteome
Cyclosporin
Isomerase
Mitochondrion
Necrosis
Reference proteome
Rotamase
S-nitrosylation
Transit peptide
Interacts With:
Q9NYB9; Q8N9N5; Q96DZ9; P04637

Publication

PubMed ID:
1744118 14702039 15164054 15489334 10406942 19228691 21269460 20950273 21930693 22726440 25944712 15858260 18076075 21904027