JavaScript is disabled in your browser. Please enable JavaScript to view this website.

Calr

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 (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.

Associates with PDIA3 through the tip of the extended arm formed by the P-domain.

Function

Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (PubMed:20880849, PubMed:21652723). Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).

Sequence Similarities

Belongs to the calreticulin family.

Cellular localization

Alternative names

Calreticulin, CRP55, Calregulin, Endoplasmic reticulum resident protein 60, HACBP, ERp60, Calr

swissprot:P14211 entrezGene:12317