Caution:Was originally (PubMed:2332496) thought to be the 52 kDa Ro autoantigen.,Domain:Associates with PDIA3 through the tip of the extended arm formed by the P-domain.,Domain:Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity.,Domain:The interaction with glycans occurs through a binding site in the globular lectin domain.,Domain:The zinc binding sites are localized to the N-domain.,Function: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.,mass spectrometry: PubMed:11149926,online information:Calreticulin,online information:Calreticulin entry,similarity:Belongs to the calreticulin family.,subcellular location:Also found in cell surface (T cells), cytosol and extracellular matrix. Associated with the lytic granules in the cytolytic T-lymphocytes.,subunit:Monomer. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and with NR3C1.,
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