Ppif
entrez
105675
canonical
uniprot
Q99KR7
canonical
ensembl
ENSMUSG00000021868
resolver
ensp
ENSMUSP00000022419
resolver
ensp
ENSMUSP00000246770
resolver
enst
ENSMUST00000022419
resolver
genesymbol
Ppif
resolver
uniprot_entry
PPIF_MOUSE
resolver
activity_regulation
ACTIVITY REGULATION: Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP. {ECO:0000250|UniProtKB:P30405}.
uniprot
proteins
amino_acid_sequence
MLALRCGPRLLGLLSGPRSAPLLLSATRTCSDGGARGANSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPAFMCQAGDFTNHNGTGGRSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS
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 (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). {ECO:0000250|UniProtKB:P29117, ECO:0000250|UniProtKB:P30405, ECO:0000269|PubMed:15800626, ECO:0000269|PubMed:15800627, ECO:0000269|PubMed:16103352, ECO:0000269|PubMed:18684715, ECO:0000269|PubMed:19801635, ECO:0000269|PubMed:21281446, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:31489369}.
uniprot
proteins
mass_dalton
21737
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-166; deacetylated at Lys-166 by SIRT3. {ECO:0000269|PubMed:21212461}.; PTM: Benzoylated at Lys-72 and Lys-196. Debenzoylated by SIRT3; inhibiting its cooperation with p53/TP53. {ECO:0000250|UniProtKB:P30405}.
uniprot
proteins
protein_family
Cyclophilin-type PPIase family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15800626
uniprot
proteins
pubmed
15800627
uniprot
proteins
pubmed
16103352
uniprot
proteins
pubmed
18684715
uniprot
proteins
pubmed
19801635
uniprot
proteins
pubmed
20950273
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21212461
uniprot
proteins
pubmed
21281446
uniprot
proteins
pubmed
21930693
uniprot
proteins
pubmed
22726440
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
31489369
uniprot
proteins
sequence_length
206
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P29117}.
uniprot
proteins