Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum.
Calreticulin is a 46-kDa Ca2+-binding chaperone found across a diverse range of species. The protein is involved in the regulation of intracellular Ca2+ homeostasis and endoplasmic reticulum (ER) Ca2+ storage capacity. Calreticulin is also an important molecular chaperone involved in "quality control" within secretory pathways. The protein contains structurally and functionally unique domains with specialized functions. Studies on calreticulin knockout mice indicate that the protein is essential in early cardiac development. The protein also plays an important role in autoimmunity and cancer.
Gelebart
Pascal
P
Canadian Institute of Health Research Membrane Protein Research Group, Department of Biochemistry, University of Alberta, Edmonton, Alta., T6G 2H7C, Canada.
Opas
Michal
M
Michalak
Marek
M
D000818:Animals; D015551:Autoimmunity / Q000502:physiology; D002118:Calcium / Q000378:metabolism*; D037282:Calreticulin / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006321:Heart / Q000196:embryology; D006801:Humans; D051379:Mice; D018345:Mice, Knockout; D018832:Molecular Chaperones / Q000378:metabolism*; D009206:Myocardium / Q000378:metabolism; D009369:Neoplasms / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary
D037282:Calreticulin; D018832:Molecular Chaperones; D002118:Calcium