PF00262

Calreticulin family

Pfam entry
Member databasePfam
Pfam typefamily
Short nameCalreticulin
ClanConcanavalin
Author Finn RD;0000-0001-8626-2148
Sequence Ontology0100021

Description
Imported from IPR001580

The calreticulin family is a family of calcium-binding ER chaperonesthat includes calreticulin, calnexin and camlegin
[4]
.

Calreticulin (calregulin)
[1]
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
[2]
and calmegin
[3]
.

References
Imported from IPR001580

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

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