Calreticulin/calnexin
Short name | Calret/calnex |
Overlapping homologous superfamilies | |
family relationships |
Description
* 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.
References
1.Calreticulin. Michalak M, Milner RE, Burns K, Opas M. Biochem. J. 285 ( Pt 3), 681-92, (1992). View articlePMID: 1497605
2.Calnexin: a membrane-bound chaperone of the endoplasmic reticulum. Bergeron JJ, Brenner MB, Thomas DY, Williams DB. Trends Biochem. Sci. 19, 124-8, (1994). View articlePMID: 8203019
3.Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. Watanabe D, Yamada K, Nishina Y, Tajima Y, Koshimizu U, Nagata A, Nishimune Y. J. Biol. Chem. 269, 7744-9, (1994). View articlePMID: 8126001
4.Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum. Di Jeso B, Ulianich L, Pacifico F, Leonardi A, Vito P, Consiglio E, Formisano S, Arvan P. Biochem. J. 370, 449-58, (2003). View articlePMID: 12401114
GO terms
biological process
molecular function
cellular component
Cross References
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