Proteins expressed in the endoplasmic reticulum （ER） are tightly regulated by a variety of quality control mechanisms. Terminally misfolded proteins in the ER are retrotranslocated to the cytoplasm and degraded by proteasomes through a mechanism known as ER-associated degradation （ERAD）. EDEM2 （ER degradation-enhancing alpha-mannosidase-like 2） is a 578 amino acid secreted protein that，in conjunction with other EDEM proteins （namely EDEM and EDEM3），is involved in the ERAD pathway of protein degradation. EDEM2，a member of the glycosyl hydrolase 47 family，contains a mannosidase homology domain，an N-terminal cleavable signal sequence and a C-terminal extension that is required for both ER retention and the proper function of EDEM2. Human EDEM2 shares 93% sequence identity with its mouse homolog，suggesting a conserved role between species. Two isoforms of EDEM2 exist due to alternative splicing events.
