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Gene and Protein Information | |||||||
Species | TM | P Loops | AA | Chromosomal Location | Gene Symbol | Gene Name | Reference |
Human | 24 | 0 | 2339 | 9q34.3 | CACNA1B | calcium voltage-gated channel subunit alpha1 B | |
Mouse | 24 | 0 | 2327 | 2 16.58 cM | Cacna1b | calcium channel, voltage-dependent, N type, alpha 1B subunit | |
Rat | 24 | 0 | 2336 | 3p13 | Cacna1b | calcium voltage-gated channel subunit alpha1 B |
Previous and Unofficial Names |
CACNL1A5 | CACNN | brain calcium channel III | Cchn1a | α1B | calcium channel |
Database Links | |
Alphafold | Q00975 (Hs), O55017 (Mm), Q02294 (Rn) |
ChEMBL Target | CHEMBL4478 (Hs), CHEMBL3637936 (Mm), CHEMBL5107 (Rn) |
DrugBank Target | Q00975 (Hs) |
Ensembl Gene | ENSG00000148408 (Hs), ENSMUSG00000004113 (Mm), ENSRNOG00000004560 (Rn) |
Entrez Gene | 774 (Hs), 12287 (Mm), 257648 (Rn) |
Human Protein Atlas | ENSG00000148408 (Hs) |
KEGG Gene | hsa:774 (Hs), mmu:12287 (Mm), rno:257648 (Rn) |
OMIM | 601012 (Hs) |
Pharos | Q00975 (Hs) |
RefSeq Nucleotide | NM_000718 (Hs), NM_001042528 (Mm), NM_147141 (Rn) |
RefSeq Protein | NP_000709 (Hs), NP_001035993 (Mm), NP_671482 (Rn) |
UniProtKB | Q00975 (Hs), O55017 (Mm), Q02294 (Rn) |
Wikipedia | CACNA1B (Hs) |
Associated Proteins | ||||||||||||||||||||||
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Associated Protein Comments | ||||||||||||||||||||||
Cav2.2 channels are associated with and regulated by G protein β/γ subunits (reviewed in [9]). |
Functional Characteristics | |
N-type calcium current: High voltage-activated, moderate voltage-dependent inactivation |
Ion Selectivity and Conductance | ||||||
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Voltage Dependence | ||||||||||||||||||||||
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Voltage Dependence Comments | ||||||||||||||||||||||
Activation kinetics and current-voltage relations are affected by Cav2.2 alternative splicing [31,45,58]. Activation and inactivation time courses depend upon the nature of the coexpressed β subunit (slower with β2) [45]. Notable Cav2.2 splice variants that affect channel biophysical properties, modulation and interaction with synaptic proteins are found in refs [17,25,31,45,58]. |
Download all structure-activity data for this target as a CSV file
Gating inhibitors | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Key to terms and symbols | View all chemical structures | Click column headers to sort | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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ω-grammotoxin SIA causes at +100mV shift in the voltage dependence of Cav2.2 containing channels [37]. |
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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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The efficacy of ω-conotoxin MVIIC is highly dependent on [Ba2+]. ω-conotoxin GVIA is routinely used at concentrations of 500nM to 1μM to completely and irreversibly block native and cloned N-type currents. Cilnidipine is a dihydropyridine derivative that blocks both N-type and L-type calcium channels and has been used clinically to treat patients with renal and cardiovascular disease [61,71]. |
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Physiological Consequences of Altering Gene Expression | ||||||||||
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Phenotypes, Alleles and Disease Models | Mouse data from MGI | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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66. Wennemuth G, Westenbroek RE, Xu T, Hille B, Babcock DF. (2000) CaV2.2 and CaV2.3 (N- and R-type) Ca2+ channels in depolarization-evoked entry of Ca2+ into mouse sperm. J Biol Chem, 275 (28): 21210-7. [PMID:10791962]
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