Endoplasmic reticulum protein 27 (ERP27)

Endoplasmic reticulum protein 27 (ERP27) is a non-catalytic member of the protein disulfide isomerase (PDI) family, localized in the endoplasmic reticulum. Structurally, it consists of two thioredoxin-like domains homologous to the non-catalytic b and b′ domains of PDI, but it lacks the active site for redox catalysis and is therefore not involved in thiol-disulfide oxidoreduction[1][3][5]. ERP27 contains an N-terminal signal sequence, two TRX-like domains, and a C-terminal ER-retention sequence[5]. It binds unfolded proteins via a hydrophobic pocket in its C-terminal domain and may function as a molecular chaperone by binding substrate proteins and possibly recruiting other PDI-like proteins such as PDIA3 (ERp57)[5][3][4]. ERP27 is believed to participate in the unfolded protein response, but its specific biological function remains largely uncharacterized[1][5][3]. There is currently no evidence supporting a therapeutic role, disease-specific targeting, or clinical use of ERP27 as a drug target.

Other names

Endoplasmic reticulum resident protein 27C12orf46UNQ781/PRO1575ER protein 27ERp27FLJ32115PDIA8Inactive protein disulfide-isomerase 27protein disulfide isomerase family A member 8endoplasmic reticulum protein 27 kDa