Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle (By similarity). This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity). Probably by controlling the folding of extracellular matrix protein unc-52/Perlecan, may play a role in the formation of fibrous organelles, a hemidesmosome-like structure attaching muscles to the epidermis (PubMed:20153198). Protects dopaminergic neurons against oxidative stress-induced neurodegeneration (PubMed:29346364). May play a role in protection against ER stress (PubMed:24933177). Plays a role in modulating lifespan, acting by influencing ER calcium homeostasis (PubMed:32905769). By ER stress in an xbp-1-dependent manner (PubMed:24933177). By aging (PubMed:32905769). 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 (By similarity). The interaction with glycans occurs through a binding site in the globular lectin domain. The zinc binding sites are localized to the N-domain. Cleaved by caspase ced-3 in vitro. RNAi-mediated knockdown in a vab-10(e698) mutant background causes 45 percent embryonic lethality. In the surviving animals, causes a 14 percent larval lethality associated with the detachment of muscles from the epidermis. Belongs to the calreticulin family.