CANX

Function

Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse (By similarity).

Post-translational modifications

Phosphorylated at Ser-565 by MAPK3/ERK1. Phosphorylation by MAPK3/ERK1 increases its association with ribosomes (By similarity).

Palmitoylation by DHHC6 leads to the preferential localization to the perinuclear rough ER. It mediates the association of calnexin with the ribosome-translocon complex (RTC) which is required for efficient folding of glycosylated proteins (By similarity).

Ubiquitinated, leading to proteasomal degradation. Probably ubiquitinated by ZNRF4.

Sequence Similarities

Belongs to the calreticulin family.

Cellular localization

• Endoplasmic reticulum membrane
• Single-pass type I membrane protein
• Mitochondrion membrane
• Single-pass type I membrane protein
• Melanosome membrane
• Single-pass type I membrane protein
• The palmitoylated form preferentially localizes to the perinuclear rough ER (By similarity). Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (PubMed:22045338).

Alternative names

Calnexin, pp90, CANX

Database links

swissprot:P24643 entrezGene:403908

Other research areas

• Neuroscience