As a co-chaperone for HSPA5 it is required for proper folding, trafficking or degradation of proteins ( ). Binds directly to both unfolded proteins that are substrates for ERAD and nascent unfolded peptide chains, but dissociates from the HSPA5-unfolded protein complex before folding is completed . May help recruiting HSPA5 and other chaperones to the substrate. Stimulates HSPA5 ATPase activity . It is necessary for maturation and correct trafficking of PKD1 .
Subcellular locations: Endoplasmic reticulum lumen
Associated with the ER membrane in a C-terminally epitope-tagged construct.
Widely expressed.