Search Results
Overview
| Uniprot ID | Q99KR7 |
|---|---|
| Protein Name | Peptidyl-prolyl cis-trans isomerase F, mitochondrial |
| Gene Name | Ppif |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 166 | KTDWLDGKHVVFGHV |
| 174 | HVVFGHVKEGMDVVK |
| 189 | KIESFGSKSGKTSKK |
| 66 | GRVVLELKADVVPKT |
| 72 | LKADVVPKTAENFRA |
| 85 | RALCTGEKGFGYKGS |
| 90 | GEKGFGYKGSTFHRV |
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 F(1)F(0) 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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005757 | mitochondrial permeability transition pore complex |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0016018 | cyclosporin A binding |
| Molecular Function | GO:0004857 | enzyme inhibitor activity |
| Molecular Function | GO:0042277 | peptide binding |
| Molecular Function | GO:0003755 | peptidyl-prolyl cis-trans isomerase activity |
| Biological Process | GO:0008637 | apoptotic mitochondrial changes |
| Biological Process | GO:0006915 | apoptotic process |
| Biological Process | GO:0071243 | cellular response to arsenic-containing substance |
| Biological Process | GO:0071277 | cellular response to calcium ion |
| Biological Process | GO:0070301 | cellular response to hydrogen peroxide |
| Biological Process | GO:0051882 | mitochondrial depolarization |
| Biological Process | GO:1902686 | mitochondrial outer membrane permeabilization involved in programmed cell death |
| Biological Process | GO:0007005 | mitochondrion organization |
| Biological Process | GO:0061061 | muscle structure development |
| Biological Process | GO:0070266 | necroptotic process |
| Biological Process | GO:0043066 | negative regulation of apoptotic process |
| Biological Process | GO:2001243 | negative regulation of intrinsic apoptotic signaling pathway |
| Biological Process | GO:0090324 | negative regulation of oxidative phosphorylation |
| Biological Process | GO:0090201 | negative regulation of release of cytochrome c from mitochondria |
| Biological Process | GO:0012501 | programmed cell death |
| Biological Process | GO:0006457 | protein folding |
| Biological Process | GO:0042981 | regulation of apoptotic process |
| Biological Process | GO:0046902 | regulation of mitochondrial membrane permeability |
| Biological Process | GO:1902445 | regulation of mitochondrial membrane permeability involved in programmed necrotic cell death |
| Biological Process | GO:0002931 | response to ischemia |
| Biological Process | GO:0006979 | response to oxidative stress |
| Biological Process | GO:0098528 | skeletal muscle fiber differentiation |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.