Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export.
Specificity
Natural and recombinant Human Calreticulin
Subcellular Location
Endoplasmic reticulum lumen Cytoplasm cytosol Secreted extracellular space extracellular matrix Cell surface Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes.
Monomer. Component of an EIF2 complex at least composed of CELF1/CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 (By similarity). Interacts with NR3C1 and TRIM21. Interacts with GABARAP.