Recombinant Human SEP15 protein

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The SEP15 protein also known as Selenoprotein F has a molecular mass of approximately 15 kDa. It plays a mechanical role as a thiol-disulfide oxidoreductase enzyme participating in the formation and isomerization of disulfide bonds within proteins. SEP15 is found mainly in the endoplasmic reticulum (ER) and shows a higher expression level in liver prostate kidney and colon tissues. Its function is strongly linked to the presence of the rare amino acid selenocysteine which is essential for its activity.

Biological function summary

SEP15 influences protein folding and maintenance of redox homeostasis within the endoplasmic reticulum. As part of the UDP-glucose:glycoprotein glucosyltransferase complex it ensures proper protein folding and glycosylation. This role underlies its involvement in quality control of proteins preventing accumulation of misfolded proteins that could be harmful to cells. Its presence is significant in stress response mechanisms helping cells manage oxidative stress conditions.

Pathways

Several studies connect SEP15 to the ER stress signaling pathways and the antioxidant response. In the ER stress response it works alongside proteins like ERO1 and PDI helping ensure proper protein disulfide bond formation. Within antioxidant pathways SEP15 acts in coordination with Se-dependent glutathione peroxidases which protect cells against oxidative damage by reducing peroxides.

SEP15 relates to cancer and neurological disorders. Its malfunction or altered expression can affect tumor development and progression especially in colon cancer where it is often downregulated. Additionally because SEP15 contributes to neuron protection under oxidative stress dysfunction in SEP15 may link to neurodegenerative diseases. This relation further connects to other selenoproteins like GPX1 and GPX4 which play protective roles against oxidative damage in cellular environments.