Q99KR7 · PPIF_MOUSE
- ProteinPeptidyl-prolyl cis-trans isomerase F, mitochondrial
- GenePpif
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids206 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity).
Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369).
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:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369).
In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440).
Involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (PubMed:19801635, PubMed:21281446).
Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369).
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:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369).
In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440).
Involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (PubMed:19801635, PubMed:21281446).
Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Activity regulation
Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP.
GO annotations
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase F, mitochondrial
- EC number
- Short namesPPIase F
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ99KR7
Proteomes
Organism-specific databases
Subcellular Location
Phenotypes & Variants
Disruption phenotype
Mice are developmentally normal and show no apparent anomalies (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Mitochondria do not undergo cyclosporin A-sensitive mitochondrial permeability transtition (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Cells show resistance to necrotic cell death induced by reactive oxygen species and Ca2+ overload, and animals show a high level of resistance to ischaemia/reperfusion-induced cardiac injury (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Mice show a dramatic reduction in brain infarct size after acute middle cerebral artery occlusion and reperfusion (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Mice lacking Slc25a4/Ant1, Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack Ca2+-induced mitochondrial permeability transition pore (mPTP) formation (PubMed:31489369).
Mitochondria do not undergo cyclosporin A-sensitive mitochondrial permeability transtition (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Cells show resistance to necrotic cell death induced by reactive oxygen species and Ca2+ overload, and animals show a high level of resistance to ischaemia/reperfusion-induced cardiac injury (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Mice show a dramatic reduction in brain infarct size after acute middle cerebral artery occlusion and reperfusion (PubMed:15800626, PubMed:15800627, PubMed:16103352).
Mice lacking Slc25a4/Ant1, Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack Ca2+-induced mitochondrial permeability transition pore (mPTP) formation (PubMed:31489369).
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 11 variants from UniProt as well as other sources including ClinVar and dbSNP.
Chemistry
PTM/Processing
Features
Showing features for transit peptide, chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transit peptide | 1-29 | Mitochondrion | ||||
Sequence: MLALRCGPRLLGLLSGPRSAPLLLSATRT | ||||||
Chain | PRO_0000025490 | 30-206 | Peptidyl-prolyl cis-trans isomerase F, mitochondrial | |||
Sequence: CSDGGARGANSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS | ||||||
Modified residue | 66 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 66 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 85 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 166 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 174 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 189 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 202 | S-nitrosocysteine | ||||
Sequence: C |
Post-translational modification
Acetylated at Lys-166; deacetylated at Lys-166 by SIRT3.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Associates with the mitochondrial membrane ATP synthase F1F0 ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA) (PubMed:19801635).
Interacts with ATP5F1B; ATP5PD and ATP5PO (PubMed:21281446).
Interacts with SLC25A3; the interaction is impaired by CsA (By similarity).
Interacts with BCL2; the interaction is impaired by CsA. Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA (PubMed:22726440).
Interacts with C1QBP (PubMed:20950273).
Interacts with MCUR1 (By similarity).
Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (By similarity).
Interacts with SPG7 (By similarity).
Interacts with ATP5F1B; ATP5PD and ATP5PO (PubMed:21281446).
Interacts with SLC25A3; the interaction is impaired by CsA (By similarity).
Interacts with BCL2; the interaction is impaired by CsA. Interacts with TP53; the association implicates preferentially tetrameric TP53, is induced by oxidative stress and is impaired by CsA (PubMed:22726440).
Interacts with C1QBP (PubMed:20950273).
Interacts with MCUR1 (By similarity).
Component of the mitochondrial permeability transition pore complex (mPTPC), at least composed of SPG7, VDAC1 and PPIF (By similarity).
Interacts with SPG7 (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
XENO | Q99KR7 | A2M P01023 | 3 | EBI-6455001, EBI-640741 | |
XENO | Q99KR7 | DNM2 P50570-2 | 3 | EBI-6455001, EBI-10968534 | |
XENO | Q99KR7 | HTT P42858 | 3 | EBI-6455001, EBI-466029 | |
BINARY | Q99KR7 | Tp53 P02340 | 2 | EBI-6455001, EBI-474016 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 48-204 | PPIase cyclophilin-type | ||||
Sequence: YLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQ |
Sequence similarities
Belongs to the cyclophilin-type PPIase family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length206
- Mass (Da)21,737
- Last updated2001-06-01 v1
- Checksum6E6BFE4D6B064D6F
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC004041 EMBL· GenBank· DDBJ | AAH04041.1 EMBL· GenBank· DDBJ | mRNA |