Proper protein folding and post-translational modifications are essential for secretory protein export out of the endoplasmic reticulum. This task is accomplished by chaperone proteins such as protein disulfide isomerase (PDI), GRP94, and BiP. A recently characterized protein, designated ERp29, is closely related to these chaperone proteins and appears to be up regulated during ER stress conditions.
ERp29 is a 259-residue protein that is encoded by a gene on chromosome 12 in humans. This soluble protein is localized to the lumen of the endoplasmic reticulum in all mammalian cells. Research has shown that there are two primary domains within ERp29. The first is the C-terminal region that is a novel, all helical, fold that is most likely involved with ERp29 retention to the ER. The second is the N-terminal region that resembles that of PDI's thioredoxin module.
chromosome 12 open reading frame 8; endoplasmic reticulum lumenal protein ERp28; endoplasmic reticulum protein 29; Endoplasmic reticulum protein ERp29; Endoplasmic reticulum resident protein 28; Endoplasmic reticulum resident protein 29; Endoplasmic reticulum resident protein 31; endoplasmic retuclum protein 29; epididymis secretory protein Li 107; ERp28; ERp29; ERp31; protein disulfide isomerase family A, member 9