Protein Domain : Calreticulin/calnexin IPR001580

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

1 Child Features

3 Gene Families

639 Genes

4 Ontology Annotations

0 Parent Features

14 Publications

USDA
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