82112330ENSG00000283777ENSG00000127022ENSMUSG00000020368P27824P35564NM_001024649NM_001746NM_001110499NM_001110500NM_007597NP_001350925NP_001350926NP_001350927NP_001350928NP_001350929NP_001350930NP_001103969NP_001103970NP_031623Calnexin (CNX) is a 67kDa integral protein (that appears variously as a 90kDa, 80kDa, or 75kDa band on western blotting depending on the source of the antibody) of the endoplasmic reticulum (ER).

It consists of a large (50 kDa) N-terminal calcium-binding lumenal domain, a single transmembrane helix and a short (90 residues), acidic cytoplasmic tail.

As newly synthesized MHC class I α-chains enter the endoplasmic reticulum, calnexin binds on to them retaining them in a partly folded state.

A prolonged association of calnexin with mutant misfolded PMP22 known to cause Charcot-Marie-Tooth Disease[16] leads to the sequestration, degradation and inability of PMP22 to traffic to the Schwann cell surface for myelination.

[17] The x-ray crystal structure of calnexin revealed a globular lectin domain and a long hydrophobic arm extending out.