Tetratricopeptide repeat domain 17 (TTC17)

Tetratricopeptide repeat domain 17 (TTC17) is a large, soluble adaptor protein primarily localized to the endoplasmic reticulum (ER) and contains multiple tetratricopeptide repeat (TPR) motifs[1][2][4]. TTC17 is crucial for efficient secretory protein trafficking, maintenance of Golgi apparatus architecture, and proper ER function—processes critical for protein folding, quality control, and maturation[1][2][4]. TTC17 interacts with several molecular chaperones and cochaperones, is highly N-glycosylated, and is upregulated in response to ER stress[1][4]. Loss of TTC17 leads to broad defects in secretory trafficking, altered glycosylation, and impaired processing of important glycoproteins, including insulin-like growth factor type 1 receptor and clusterin[1][2][4]. Additionally, TTC17 contributes to actin filament polymerization and cilium organization, linking it to disorders of ciliogenesis such as primary ciliary dyskinesia[5][7]. As of now, TTC17 is not considered a classical therapeutic target such as a receptor, enzyme, transporter, or transcription factor.

Other names

Tetratricopeptide repeat protein 17TPR repeat protein 17FLJ10890TTC17