CaBP2 is a rat homolog of ERp72 with proteindisulfide isomerase activity

Abstract

Ca-binding protein 2 (CaBP2) has been described previously as an intracisternal calcium-binding microsomal glycoprotein. We report now the primary sequence of this protein as deduced from the corresponding cDNA. The protein possesses a C-terminal -KEEL retention sequence and three repeats of the thioredoxin-like motive -EFYAPNCGHCK-, and represents the rat homolog of ERp72. In contrast to earlier reports on ERp72, CaBP2 possesses significant proteindisulfide isomerase activity. Furthermore, in contrast to ERp72, CaBP2 is a glycoporotein containing O-linked glycans. The amount of CaBP2 in H-35 Reuber hepatoma cells increases in parallel with that of immunoglobin heavy-chain-binding protein under conditions which lead to impaired glycosylation, while the amount of calreticulin, another KDEL-containing glycoprotein, remains almost unchanged.