PPIC
Sign in to saveAlso known as CYPC, peptidylprolyl isomerase C
Peptidyl-prolyl cis-trans isomerase C (PPIC) is an enzyme that in humans is encoded by the PPIC gene on chromosome 5. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIC participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.
Gene data
PPIC- Name
- peptidylprolyl isomerase C
- Type
- protein-coding
- Position
- 123,022,052–123,036,725 (−)
- Aliases
- CYPC
- Ensembl
- ENSG00000168938
- RefSeq RNA
- NM_000943.5
- RefSeq protein
- NP_000934.1
The protein encoded by this gene is 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. Similar to other PPIases, this protein can bind immunosuppressant cyclosporin A. [provided by RefSeq, Jul 2008].
Gene Ontology
Biological process
Molecular function
via MyGene.info
Gene · Ensembl
peptidylprolyl isomerase C
- Symbol
- PPIC
- Biotype
- Protein coding
- Organism
- Homo sapiens
- Location
- 5:123,022,052-123,036,727
- Strand
- Reverse (−)
- Assembly
- GRCh38
via Ensembl · EMBL-EBI
Wikidata facts
- Image
- Protein PPIC PDB 2esl.png
Show 6 more facts
- HomoloGene ID
- 727
- exact match
- identifiers.org/ncbigene/5480
- genomic end
- 123036725
- genomic start
- 122358945
- cytogenetic location
- 5q23.2
- Commons category
- Peptidyl-prolyl cis-trans isomerase C
Sources (4)
via Wikidata · CC0
~3 min read
Article
6 sectionsContents
- Structure
- Function
- Clinical Significance
- Interactions
- References
- Further reading
Peptidyl-prolyl cis-trans isomerase C (PPIC) is an enzyme that in humans is encoded by the PPIC gene on chromosome 5. As a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, this protein catalyzes the cis-trans isomerization of proline imidic peptide bonds, which allows it to facilitate folding or repair of proteins. In addition, PPIC participates in many biological processes, including mitochondrial metabolism, apoptosis, redox, and inflammation, as well as in related diseases and conditions, such as ischemic reperfusion injury, AIDS, and cancer.
==Structure== Like other cyclophilins, PPIC forms a β-barrel structure with a hydrophobic core. This β-barrel is composed of eight anti-parallel β-strands and capped by two α-helices at the top and bottom. In addition, the β-turns and loops in the strands contribute to the flexibility of the barrel. PPIC in particular is composed of 212 residues and contains a hydrophobic, ER-targeting sequence at the N-terminal. The PPIase domain is homologous to PPIA and can be bound and inhibited by CsA.