Description: Homo sapiens peptidylprolyl isomerase A (cyclophilin A) (PPIA), mRNA. RefSeq Summary (NM_021130): This gene encodes a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family. PPIases catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerate the folding of proteins. The encoded protein is a cyclosporin binding-protein and may play a role in cyclosporin A-mediated immunosuppression. The protein can also interact with several HIV proteins, including p55 gag, Vpr, and capsid protein, and has been shown to be necessary for the formation of infectious HIV virions. Multiple pseudogenes that map to different chromosomes have been reported. [provided by RefSeq, Jul 2008]. Transcript (Including UTRs) Position: hg19 chr7:44,836,241-44,842,716 Size: 6,476 Total Exon Count: 5 Strand: + Coding Region Position: hg19 chr7:44,836,324-44,841,021 Size: 4,698 Coding Exon Count: 5
ID:PPIA_HUMAN DESCRIPTION: RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; EC=184.108.40.206; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-binding protein; AltName: Full=Rotamase A; 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. INTERACTION: Q72497:gag (xeno); NbExp=6; IntAct=EBI-437708, EBI-1036263; Q16849:PTPRN; NbExp=3; IntAct=EBI-437708, EBI-728153; O00267:SUPT5H; NbExp=2; IntAct=EBI-437708, EBI-710464; SUBCELLULAR LOCATION: Cytoplasm. Secreted. 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. SIMILARITY: Belongs to the cyclophilin-type PPIase family. PPIase A subfamily. SIMILARITY: Contains 1 PPIase cyclophilin-type domain. WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/ppia/"; WEB RESOURCE: Name=Wikipedia; Note=Cyclophilin entry; URL="http://en.wikipedia.org/wiki/Cyclophilin";
Genetic Association Studies of Complex Diseases and Disorders
Genetic Association Database (archive): PPIA CDC HuGE Published Literature: PPIA
The RNAfold program from the Vienna RNA Package is used to perform the secondary structure predictions and folding calculations. The estimated folding energy is in kcal/mol. The more negative the energy, the more secondary structure the RNA is likely to have.
ModBase Predicted Comparative 3D Structure on P62937
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Orthologous Genes in Other Species
Orthologies between human, mouse, and rat are computed by taking the best BLASTP hit, and filtering out non-syntenic hits. For more distant species reciprocal-best BLASTP hits are used. Note that the absence of an ortholog in the table below may reflect incomplete annotations in the other species rather than a true absence of the orthologous gene.