| Type: | Conserved_site | Name: | Calreticulin/calnexin, conserved site |
| Description: | Synonym(s): Calregulin, CRP55, HACBP Calreticulin [] is a high-capacity calcium-binding protein which is present in most tissues and located at the periphery of the endoplasmic (ER) and the sarcoplamic reticulum (SR) membranes. It probably plays a role in the storage of calcium in the lumen of the ER and SR and it may well have other important functions.Structurally, calreticulin is a protein of about 400 amino acid residues consisting of three domains: An N-terminal, probably globular, domain of about 180 amino acid residues (N-domain).A central domain of about 70 residues (P-domain) which contains three repeats of an acidic 17 amino acid motif. This region binds calcium with a low-capacity, but a high-affinity.A C-terminal domain rich in acidic residues and in lysine (C-domain). This region binds calcium with a high-capacity but a low-affinity.Calreticulin is evolutionarily related to several other calcium-binding proteins, including Onchocerca volvulusantigen RAL-1, calnexin [] and calmegin []. | Short Name: | Calret/calnex_CS |
