Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
- PMID: 2600080
Molecular cloning of the high affinity calcium-binding protein (calreticulin) of skeletal muscle sarcoplasmic reticulum
Abstract
A cDNA clone encoding the high affinity Ca2+-binding protein (HACBP) of rabbit skeletal muscle sarcoplasmic reticulum was isolated and sequenced. The cDNA encoded a protein of 418 amino acids, but a comparison of the deduced amino acid sequence with the NH2-terminal amino acid sequence of the purified protein indicates that a 17-residue NH2-terminal signal sequence was removed during synthesis. This was confirmed by studies of in vitro translation of mRNA encoding the protein. Structural predictions did not reveal any potential transmembrane segments in the protein. The COOH-terminal sequence of the high affinity Ca2+-binding protein, Lys-Asp-Glu-Leu, is the same as that proposed to be an endoplasmic reticulum retention signal (Munro, S., and Pelham, H. R. B. (1987) Cell 48, 899-907). All of these characteristics suggest that the protein is localized in the lumen of the sarcoplasmic reticulum. The mature protein of Mr 46,567 contains 109 acidic and 52 basic amino acids. Structural predictions suggest that the first half of the molecule forms a globular domain of 8 anti-parallel beta-strands with a helix-turn-helix motif at the extreme NH2 terminus. The next one-third of the sequence is proline-rich. This segment can be subdivided into a charged region which contains a 17-amino acid repeat, followed by a proline, serine, and threonine-rich segment extending from Pro-246 to Thr-316. Thirty-seven acidic residues are clustered within 56 amino acids at the COOH terminus of the protein. Although the protein binds 1 mol of Ca2+/mol with high affinity, no "EF-hand" consensus sequence was observed in the protein. The acidic COOH terminus, however, could account for the low affinity, high capacity Ca2+ binding observed in the protein. In agreement with other involved laboratories, we have chosen the name calreticulin for the protein.
Similar articles
-
Molecular cloning of a histidine-rich Ca2+-binding protein of sarcoplasmic reticulum that contains highly conserved repeated elements.J Biol Chem. 1989 Oct 25;264(30):18083-90. J Biol Chem. 1989. PMID: 2808365
-
Molecular cloning and expression of cDNA encoding a lumenal calcium binding glycoprotein from sarcoplasmic reticulum.Proc Natl Acad Sci U S A. 1989 Aug;86(16):6047-51. doi: 10.1073/pnas.86.16.6047. Proc Natl Acad Sci U S A. 1989. PMID: 2762314 Free PMC article.
-
Peripheral membrane proteins of sarcoplasmic and endoplasmic reticulum. Comparison of carboxyl-terminal amino acid sequences.Biochem Cell Biol. 1989 Oct;67(10):696-702. doi: 10.1139/o89-104. Biochem Cell Biol. 1989. PMID: 2686719 Review.
-
Molecular cloning of cDNA encoding human and rabbit forms of the Ca2+ release channel (ryanodine receptor) of skeletal muscle sarcoplasmic reticulum.J Biol Chem. 1990 Feb 5;265(4):2244-56. J Biol Chem. 1990. PMID: 2298749
-
Molecular cloning of cDNA encoding a 55-kDa multifunctional thyroid hormone binding protein of skeletal muscle sarcoplasmic reticulum.J Biol Chem. 1990 Sep 15;265(26):15496-502. J Biol Chem. 1990. PMID: 1697592
Cited by
-
The C1q and gC1qR axis as a novel checkpoint inhibitor in cancer.Front Immunol. 2024 Apr 22;15:1351656. doi: 10.3389/fimmu.2024.1351656. eCollection 2024. Front Immunol. 2024. PMID: 38711524 Free PMC article. Review.
-
Calreticulin: Endoplasmic reticulum Ca2+ gatekeeper.J Cell Mol Med. 2023 Jul 9;28(5):e17839. doi: 10.1111/jcmm.17839. Online ahead of print. J Cell Mol Med. 2023. PMID: 37424156 Free PMC article. Review.
-
The many faces of parasite calreticulin.Front Immunol. 2023 Mar 10;14:1101390. doi: 10.3389/fimmu.2023.1101390. eCollection 2023. Front Immunol. 2023. PMID: 36993959 Free PMC article. Review.
-
Structural and Dynamic Differences between Calreticulin Mutants Associated with Essential Thrombocythemia.Biomolecules. 2023 Mar 10;13(3):509. doi: 10.3390/biom13030509. Biomolecules. 2023. PMID: 36979444 Free PMC article.
-
Transgenic mice encoding modern imaging probes: Properties and applications.Cell Rep. 2022 May 24;39(8):110845. doi: 10.1016/j.celrep.2022.110845. Cell Rep. 2022. PMID: 35613592 Free PMC article. Review.
Publication types
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources
Research Materials
Miscellaneous