Peptidyl-prolyl cis-trans isomerase-like 1 (PPIL1)

Peptidyl-prolyl cis-trans isomerase-like 1 (PPIL1) is an enzyme encoded by the PPIL1 gene in humans, belonging to the cyclophilin family of peptidylprolyl isomerases. It catalyzes the cis-trans isomerization of proline residues in peptides, facilitating protein folding and acting as a molecular chaperone. PPIL1 is a component of the spliceosome, the complex responsible for pre-mRNA splicing in eukaryotic cells, and interacts with factors such as SKIP to promote structural rearrangement and activation of the spliceosome during RNA processing. In addition to its enzymatic role, PPIL1 is functionally involved in embryonic brain development, independently of its isomerase activity, and genetic defects in PPIL1 are associated with pontocerebellar hypoplasia. The protein is widely conserved and structurally resembles other cyclophilins, and while it may share interactions typical to its family (such as binding cyclosporin A), it does not currently have specific drugs or established biomarker applications in clinical practice. If further information or structured data is needed, consult authoritative genetic and proteomic databases using the UniProt Q9Y3C6 or NCBI Gene ID 51645 for PPIL1.

Other names

CYPL1PPIasehCyPXCGI-124PCH14rotamase PPIL1cyclophilin-like 1cyclophilin-related gene 1peptidyl-prolyl isomerase (cyclophilin)-like 1UNQ2425/PRO4984

Inhibition of peptidyl-prolyl isomerase activity (for cyclophilins, e.g., by cyclosporin A)