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Description

Calnexin (UniProt: P27824, also known as IP90, Major histocompatibility complex class I antigen-binding protein p88, p90) is encoded by the CANX gene (Gene ID: 821) in human. Calnexin is a well-conserved, calcium binding, endoplasmic reticulum (ER) resident chaperone protein that associates with newly synthesized, incompletely folded monomeric glycoproteins and promotes their correct folding prior to secretion. It is also reported to target misfolded proteins for degradation. It is anchored to the ER membrane by a transmembrane domain. Calnexin associates with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes and may, therefore, function as a signaling complex regulating thymocyte maturation. Calnexin is synthesized with a signal peptide of 20 amino acids, which is cleaved to generate the mature form. Three isoforms of calnexin have been described that are generated by alternative splicing. Calnexin is shown to be phosphorylated at Ser564 by MAPK3/ERK1, which increases its association with ribosomes.