v5.1.0.3
Glycine data from LIS
Type | Family |
Description | The calreticulin family is a family of calcium-binding ER chaperonesthat includes calreticulin, calnexin and camlegin [ ].Calreticulin (calregulin) [ ] 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 volvulus antigen RAL-1, calnexin [ ] and calmegin []. |
Short Name | Calret/calnex |