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Gene and Protein Information  |
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| Species | TM | P Loops | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
| Human | 24 | 4 | 1873 | 1q32.1 | CACNA1S | calcium voltage-gated channel subunit alpha1 S | 14 |
| Mouse | 24 | 4 | 1880 | 1 59.55 cM | Cacna1s | calcium channel, voltage-dependent, L type, alpha 1S subunit | 8 |
| Rat | 24 | 4 | 1850 | 13 | Cacna1s | calcium voltage-gated channel subunit alpha1 S | 10 |
| Previous and Unofficial Names |
| alpha-1S skeletal muscle L-type Ca2+ channel | CACNL1A3 | HOKPP | ROB1 | voltage-dependent L-type calcium channel subunit alpha-1S | voltage-gated calcium channel subunit alpha Cav1.1 | DHPR alpha1s | fmd | mdg | TTPP1 | CCHL1A3 | HOKPP1 | alpha-1 polypeptide, isoform 3, skeletal muscle | hypoPP | skeletal muscle dihydropyridine receptor | calcium channel |
| Database Links |
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| Alphafold | Q13698 (Hs), Q02789 (Mm), Q02485 (Rn) |
| ChEMBL Target | CHEMBL3805 (Hs), CHEMBL4108 (Rn) |
| DrugBank Target | Q13698 (Hs) |
| Ensembl Gene | ENSG00000081248 (Hs), ENSMUSG00000026407 (Mm), ENSRNOG00000046231 (Rn) |
| Entrez Gene | 779 (Hs), 12292 (Mm), 682930 (Rn) |
| Human Protein Atlas | ENSG00000081248 (Hs) |
| KEGG Gene | hsa:779 (Hs), mmu:12292 (Mm), rno:682930 (Rn) |
| OMIM | 114208 (Hs) |
| Orphanet | ORPHA119157 (Hs) |
| Pharos | Q13698 (Hs) |
| RefSeq Nucleotide | NM_000069 (Hs), NM_014193 (Mm), NM_001081023 (Mm), NM_053873 (Rn) |
| RefSeq Protein | NP_000060 (Hs), NP_001074492 (Mm), NP_055008 (Mm), NP_446325 (Rn) |
| UniProtKB | Q13698 (Hs), Q02789 (Mm), Q02485 (Rn) |
| Wikipedia | CACNA1S (Hs) |
| Selected 3D Structures |
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| Associated Proteins |
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| Functional Characteristics |
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| L-type calcium current: High voltage-activated, very slow voltage dependent inactivation | |
| Ion Selectivity and Conductance |
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| Voltage Dependence |
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Download all structure-activity data for this target as a CSV file 
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| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| BAYK 8644 stimulates currents at μM concentrations but, unlike inhibitory dihydropyridines, does not block charge movement [22,32,40]. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| View species-specific gating inhibitor tables | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Channel Blockers | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Key to terms and symbols | View all chemical structures | Click column headers to sort | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| View species-specific channel blocker tables | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Channel Blocker Comments | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Amlodopine, isradipine, nifedipine, nitrendipine, and nimodipine are examples of dihydropyridine calcium channel antagonists. Verapamil is a phenylalkylamine calcium channel blocker, and diltiazem is a benzothiazepine calcium channel blocker. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Tissue Distribution Comments | ||||||||
| On the protein level Cav1.1 channel expression was demonstrated only in skeletal muscle and mRNA expression has been described by one research group in rat and human brain [48], but these findings have not been reproduced by other groups so far [45]. | ||||||||
| Functional Assays
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| Physiological Functions
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| Physiological Functions Comments | ||||||||
| ECC is absent from dysgenic skeletal muscle cells lacking dihydropyridine receptors (Cav1.1 α1 subunits) and is restored by transfection of these cells with Cav1.1 α1 subunits [44,49]; fast voltage sensor movement of channel triggers opening of ryanodine receptor-mediated calcium release; channel pore opens only slowly and role of calcium entry for physiological function is not clear. | ||||||||
| Physiological Consequences of Altering Gene Expression
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| Phenotypes, Alleles and Disease Models
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Mouse data from MGI | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Clinically-Relevant Mutations and Pathophysiology
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| For details of the mechanism of action of CACNA1S mutations see references [6,30,46]. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Biologically Significant Variants
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52. Tuluc P, Molenda N, Schlick B, Obermair GJ, Flucher BE, Jurkat-Rott K. (2009) A CaV1.1 Ca2+ channel splice variant with high conductance and voltage-sensitivity alters EC coupling in developing skeletal muscle. Biophys J, 96 (1): 35-44. [PMID:19134469]
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55. Wu J, Yan Z, Li Z, Qian X, Lu S, Dong M, Zhou Q, Yan N. (2016) Structure of the voltage-gated calcium channel Ca(v)1.1 at 3.6 Å resolution. Nature, 537 (7619): 191-196. [PMID:27580036]
56. Zhao Y, Huang G, Wu J, Wu Q, Gao S, Yan Z, Lei J, Yan N. (2019) Molecular Basis for Ligand Modulation of a Mammalian Voltage-Gated Ca2+ Channel. Cell, 177 (6): 1495-1506.e12. [PMID:31150622]
