PPIF
entrez
10105
canonical
uniprot
P30405
canonical
ensembl
ENSG00000108179
resolver
ensp
ENSP00000225174
resolver
ensp
ENSP00000396388
resolver
genesymbol
PPIF
resolver
genesymbol_syn
CYP3
resolver
hgnc
HGNC:9259
resolver
uniprot
Q2YDB7
resolver
uniprot
Q5W131
resolver
uniprot_entry
PPIF_HUMAN
resolver
uniprot_sec
Q2YDB7
resolver
uniprot_sec
Q5W131
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by cyclosporin A (CsA) (PubMed:20676357). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP. {ECO:0000269|PubMed:20676357}.
uniprot
proteins
amino_acid_sequence
MLALRCGSRWLGLLSVPRSVPLRLPAARACSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS
uniprot
proteins
ec_number
5.2.1.8
uniprot
proteins
function
FUNCTION: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (PubMed:20676357). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:26387735). 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:26387735). 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 (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (PubMed:19228691). {ECO:0000250|UniProtKB:Q99KR7, ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20676357, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26387735}.
uniprot
proteins
mass_dalton
22040
uniprot
proteins
mutagenesis
MUTAGEN 73; /note="K->A: Abolished debenzoylation by SIRT3; when associated with A-197."; /evidence="ECO:0000269|PubMed:39524354"; MUTAGEN 197; /note="K->A: Abolished debenzoylation by SIRT3; when associated with A-73."; /evidence="ECO:0000269|PubMed:39524354"; MUTAGEN 203; /note="C->S: Blocks Ca(2+)-induced mPTP opening and reduces hydrogen peroxide-induced cell death."; /evidence="ECO:0000269|PubMed:21930693
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-167; deacetylated at Lys-167 by SIRT3. {ECO:0000250|UniProtKB:Q99KR7}.; PTM: Benzoylated at Lys-73 and Lys-197 (PubMed:39524354). Debenzoylated by SIRT3; inhibiting its cooperation with p53/TP53 (PubMed:39524354). {ECO:0000269|PubMed:39524354}.
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
pubmed
10406942
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15858260
uniprot
proteins
pubmed
1744118
uniprot
proteins
pubmed
18076075
uniprot
proteins
pubmed
19228691
uniprot
proteins
pubmed
20676357
uniprot
proteins
pubmed
20950273
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21904027
uniprot
proteins
pubmed
21930693
uniprot
proteins
pubmed
22726440
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26387735
uniprot
proteins
pubmed
26976564
uniprot
proteins
pubmed
39524354
uniprot
proteins
sequence_length
207
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:10406942}.
uniprot
proteins