Peptidyl-prolyl cis-trans isomerase F, mitochondrial
Name | Peptidyl-prolyl cis-trans isomerase F, mitochondrial |
---|---|
Synonyms | 5.2.1.8 Cyclophilin D Cyclophilin F CyP-D CyP-M CYP3 CypD Mitochondrial cyclophilin PPIase F Rotamase F |
Gene Name | PPIF |
Organism | Human |
Amino acid sequence | >lcl|BSEQ0002777|Peptidyl-prolyl cis-trans isomerase F, mitochondrial MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLG RVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSI YGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDV VKKIESFGSKSGRTSKKIVITDCGQLS |
Number of residues | 207 |
Molecular Weight | 22040.09 |
Theoretical pI | 9.95 |
GO Classification |
Functions
peptidyl-prolyl cis-trans isomerase activity cyclosporin A binding Processes
cellular response to hydrogen peroxide negative regulation of ATPase activity negative regulation of intrinsic apoptotic signaling pathway regulation of mitochondrial membrane permeability positive regulation of release of cytochrome c from mitochondria negative regulation of oxidative phosphorylation apoptotic mitochondrial changes negative regulation of oxidative phosphorylation uncoupler activity regulation of mitochondrial membrane permeability involved in programmed necrotic cell death protein peptidyl-prolyl isomerization regulation of proton-transporting ATPase activity, rotational mechanism response to ischemia protein folding negative regulation of release of cytochrome c from mitochondria necroptotic process cellular response to arsenic-containing substance negative regulation of apoptotic process cellular response to calcium ion regulation of necrotic cell death Components
mitochondrion membrane mitochondrial inner membrane mitochondrial matrix |
General Function | Peptidyl-prolyl cis-trans isomerase activity |
Specific 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. |
Transmembrane Regions | |
GenBank Protein ID | 181274 |
UniProtKB ID | P30405 |
UniProtKB Entry Name | PPIF_HUMAN |
Cellular Location | Mitochondrion matrix |
Gene sequence | >lcl|BSEQ0021846|Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIF) ATGCTGGCGCTGCGCTGCGGCTCCCGCTGGCTCGGCCTGCTCTCCGTCCCGCGCTCCGTG CCGCTGCGCCTCCCCGCGGCCCGCGCCTGCAGCAAGGGCTCCGGCGACCCGTCCTCTTCC TCCTCCTCCGGGAACCCGCTCGTGTACCTGGACGTGGACGCCAACGGGAAGCCGCTCGGC CGCGTGGTGCTGGAGCTGAAGGCAGATGTCGTCCCAAAGACAGCTGAGAACTTCAGAGCC CTGTGCACTGGTGAGAAGGGCTTCGGCTACAAAGGCTCCACCTTCCACAGGGTGATCCCT TCCTTCATGTGCCAGGCGGGCGACTTCACCAACCACAATGGCACAGGCGGGAAGTCCATC TACGGAAGCCGCTTTCCTGACGAGAACTTTACACTGAAGCACGTGGGGCCAGGTGTCCTG TCCATGGCTAATGCTGGTCCTAACACCAACGGCTCCCAGTTCTTCATCTGCACCATAAAG ACAGACTGGTTGGATGGCAAGCATGTTGTGTTCGGTCACGTCAAAGAGGGCATGGACGTC GTGAAGAAAATAGAATCTTTCGGCTCTAAGAGTGGGAGGACATCCAAGAAGATTGTCATC ACAGACTGTGGCCAGTTGAGCTAA |
GenBank Gene ID | M80254 |
GeneCard ID | None |
GenAtlas ID | PPIF |
HGNC ID | HGNC:9259 |
Chromosome Location | 10 |
Locus | 10q22-q23 |
References |
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Related FRC
FRCD ID | Name | Exact Mass | Structure |
---|---|---|---|
Cyclosporin |
1202.635 |
||
L-Proline |
115.132 |