UniProt functional annotation for P30405

UniProt code: P30405.

Organism: Homo sapiens (Human).
Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
 
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. {ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:22726440}.
 
Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation: Binds cyclosporin A (CsA). Is displaced by CsA from the mPTP leading to a lower open probability of the mPTP.
Subunit: Believed to associate with the mitochondrial permeability transition pore complex (PTPC). Associates with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase; the association is increased by inorganic phosphate (Pi) and decreased by cyclosporin A (CsA). Interacts with ATP5B; ATP5H and ATP5O. Interacts with SLC25A3; the interaction is impaired by CsA. 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. Interacts with C1QBP. Interacts with MCUR1 (PubMed:26976564). {ECO:0000269|PubMed:18076075, ECO:0000269|PubMed:19228691, ECO:0000269|PubMed:20950273, ECO:0000269|PubMed:22726440, ECO:0000269|PubMed:26976564}.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:10406942}.
Ptm: Deacteylated at Lys-167 by SIRT3. {ECO:0000250}.
Similarity: Belongs to the cyclophilin-type PPIase family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.