calnexin; major histocompatibility complex class I antigen-binding protein p88; p90; IP90 (CANX)

Function

• molecular chaperone
• transiently associates with newly synthesized glycoproteins in the endoplasmic reticulum (ER)
• may act in assisting protein assembly &/or in retention within the ER of unassembled protein subunits
• activity of protein disulfide isomerase may coincide with release of glycoprotein from calnexin
• seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins
• possibly responsible for retention in the ER of mutant forms of LDL receptor, CFTR, & alpha-1 antitrypsin leading to familial hypercholesterolemia type II, cystic fibrosis, & juvenile pulmonary emphysema, respectively

Structure

belongs to the calreticulin family

Compartment

• endoplasmic reticulum membrane
• melanosome

More general terms

• Ca+2 binding protein
• chaperonin; chaperone
• phosphoprotein

Database

• Entrez gene: http://www.ncbi.nlm.nih.gov/sites/entrez?db=gene&cmd=Retrieve&dopt=Graphics&list_uids=821
• Kegg: http://www.genome.jp/dbget-bin/www_bget?hsa:821
• OMIM: https://mirror.omim.org/entry/114217
• UniProt: http://www.uniprot.org/uniprot/P27824.html