Journal
BEST PRACTICE & RESEARCH CLINICAL ENDOCRINOLOGY & METABOLISM
Volume 27, Issue 3, Pages 285-301Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.beem.2013.02.009
Keywords
alternative splicing; calcium-sensing receptor; glial cells missing-2; Class C G protein-coupled receptor; ligand binding; nine-cysteines domain; 1 alpha,25-dihydroxyvitamin D; proinflammatory cytokines; seven-transmembrane domain; Venus-flytrap domain; transcription
Categories
Funding
- Canadian Institutes of Health Research
- Reseau de recherche en sante buccodentaire et osseuse
- Kidney Foundation of Canada
- Dairy Farmers of Canada
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The calcium-sensing receptor (CaSR) is a G protein-coupled receptor encoded by a single copy gene. The human CASR gene spans similar to 103-kb and has eight exons. Promoters P1 and P2 drive transcription of exons 1A and 1B, respectively, encoding alternative 5'-UTRs that splice to exon 2 encoding the common part of the 5'-UTR. Exons 2-7 encode the CaSR protein of 1078 amino acids. Functional elements responsive to 1,25-dihydroxyvitamin D, proinflammatory cytokines, and glial cells missing-2 are present in the CASR promoters. Evolutionarily, the exon structure, first seen in aquatic vertebrates, is well-conserved with a single linkage disequilibrium haplotype block for protein coding exons 2-7. Structural features of the human CaSR protein are: an N-terminal signal peptide (19 amino acids (aa)); an extracellular domain (600 aa) having a bi-lobed Venus Flytrap (VFT) domain with several Ca2+-binding sites; and a nine-cysteines domain that transduces the activation signal to the 7-transmembrane domain (250 aa) and the C-terminal tail (216 aa). (C) 2013 Elsevier Ltd. All rights reserved.
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