[1]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Slow-twitch skeletal muscle;
PubMed=2600080 [NCBI, ExPASy, EBI, Israel, Japan]
Fliegel L.,
Burns K.,
Maclennan D.H.,
Reithmeier R.A.F.,
Michalak M.;
"Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum.";
J. Biol. Chem. 264:21522-21528(1989).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Fast-twitch skeletal muscle;
DOI=10.1016/0006-291X(91)90634-J; PubMed=2059224 [NCBI, ExPASy, EBI, Israel, Japan]
Fliegel L.,
Michalak M.;
"Fast-twitch and slow-twitch skeletal muscles express the same isoform of calreticulin.";
Biochem. Biophys. Res. Commun. 177:979-984(1991).
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[3]
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PROTEIN SEQUENCE OF 18-36.
PubMed=2241926 [NCBI, ExPASy, EBI, Israel, Japan]
Treves S.,
de Mattei M.,
Lanfredi M.,
Villa A.,
Green N.M.,
Maclennan D.H.,
Meldolesi J.,
Pozzan T.;
"Calreticulin is a candidate for a calsequestrin-like function in Ca2(+)-storage compartments (calciosomes) of liver and brain.";
Biochem. J. 271:473-480(1990).
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[4]
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PROTEIN SEQUENCE OF 18-46.
PubMed=2016321 [NCBI, ExPASy, EBI, Israel, Japan]
Milner R.E.,
Baksh S.,
Shemanko C.,
Carpenter M.R.,
Smillie L.,
Vance J.E.,
Opas M.,
Michalak M.;
"Calreticulin, and not calsequestrin, is the major calcium binding protein of smooth muscle sarcoplasmic reticulum and liver endoplasmic reticulum.";
J. Biol. Chem. 266:7155-7165(1991).
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[5]
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PARTIAL PROTEIN SEQUENCE.
TISSUE=Lung;
DOI=10.1021/bi00105a012; PubMed=1911780 [NCBI, ExPASy, EBI, Israel, Japan]
Guan S.,
Falick A.M.,
Williams D.E.,
Cashman J.R.;
"Evidence for complex formation between rabbit lung flavin-containing monooxygenase and calreticulin.";
Biochemistry 30:9892-9900(1991).
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[6]
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FUNCTION.
DOI=10.1093/emboj/18.23.6718; PubMed=10581245 [NCBI, ExPASy, EBI, Israel, Japan]
Saito Y.,
Ihara Y.,
Leach M.R.,
Cohen-Doyle M.F.,
Williams D.B.;
"Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins.";
EMBO J. 18:6718-6729(1999).
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[7]
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ZINC-BINDING DOMAIN.
DOI=10.1016/0014-5793(95)01246-4; PubMed=8521965 [NCBI, ExPASy, EBI, Israel, Japan]
Baksh S.,
Spamer C.,
Heilmann C.,
Michalak M.;
"Identification of the Zn2+ binding region in calreticulin.";
FEBS Lett. 376:53-57(1995).
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[8]
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MUTAGENESIS OF HIS-170.
DOI=10.1074/jbc.M309497200; PubMed=14522955 [NCBI, ExPASy, EBI, Israel, Japan]
Guo L.,
Groenendyk J.,
Papp S.,
Dabrowska M.,
Knoblach B.,
Kay C.,
Parker J.M.,
Opas M.,
Michalak M.;
"Identification of an N-domain histidine essential for chaperone function in calreticulin.";
J. Biol. Chem. 278:50645-50653(2003).
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- FUNCTION: Molecular calcium binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity).
- SUBUNIT: Monomer. Component of an EIF2 complex at least composed of CUGBP1, CALR, CALR3, EIF2S1, EIF2S2, HSP90B1 and HSPA5. Interacts with PDIA3/ERp57 and with NR3C1 (By similarity).
- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen.
- DOMAIN: Can be divided into a N-terminal globular domain, a proline-rich P-domain forming an elongated arm-like structure and a C-terminal acidic domain. The P-domain binds one molecule of calcium with high affinity, whereas the acidic C-domain binds multiple calcium ions with low affinity (By similarity).
- DOMAIN: The interaction with glycans occurs through a binding site in the globular lectin domain (By similarity).
- DOMAIN: The zinc binding sites are localized to the N-domain.
- DOMAIN: Associates with PDIA3 through the tip of the extended arm formed by the P-domain (By similarity).
- SIMILARITY: Belongs to the calreticulin family.
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