UniProt functional annotation for P62937

UniProt codes: P62937, P05092.

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.
 
Catalytic activity: Peptidylproline (omega=180) = peptidylproline (omega=0).
Enzyme regulation: Binds cyclosporin A (CsA). CsA mediates some of its effects via an inhibitory action on PPIase.
Subunit: Interacts with HIV-1 Capsid protein. {ECO:0000269|PubMed:12218175, ECO:0000269|PubMed:12357034, ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:8513493}.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16527992}. Secreted {ECO:0000269|PubMed:16527992}. Note=Secretion occurs in response to oxidative stress in vascular smooth muscle through a vesicular secretory pathway that involves actin remodeling and myosin II activation, and mediates ERK1/2 activation.
Ptm: Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition. {ECO:0000269|PubMed:19413330, ECO:0000269|PubMed:19608861, ECO:0000269|PubMed:20364129, ECO:0000269|PubMed:22223895, ECO:0000269|PubMed:22814378, ECO:0000269|Ref.12}.
Similarity: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. {ECO:0000305}.
Similarity: Contains 1 PPIase cyclophilin-type domain. {ECO:0000255|PROSITE-ProRule:PRU00156}.

Annotations taken from UniProtKB at the EBI.