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Cav1.1 

The correct title of this article is Cav1.1. It features superscript or subscript characters that are substituted or omitted because of technical limitations.
Calcium channel, voltage-dependent, L type, alpha 1S subunit
Identifiers
Symbols CACNA1S; CACNL1A3; CCHL1A3; Cav1.1; HOKPP; MHS5; hypoPP
External IDs OMIM: 114208 MGI: 88294 HomoloGene: 37257
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 779 12292
Ensembl ENSG00000081248 ENSMUSG00000026407
Uniprot Q13698 Q3UPG8
Refseq NM_000069 (mRNA)
NP_000060 (protein)		 XM_001002706 (mRNA)
XP_001002706 (protein)
Location Chr 1: 199.28 - 199.35 Mb Chr 1: 137.87 - 137.94 Mb
Pubmed search [1] [2]

Cav1.1 also known as the calcium channel, voltage-dependent, L type, alpha 1S subunit, (CACNA1S), is a human gene.[1]

This gene encodes one of the five subunits of the slowly inactivating L-type voltage-dependent calcium channel in skeletal muscle cells. Mutations in this gene have been associated with hypokalemic periodic paralysis, thyrotoxic periodic paralysis and malignant hyperthermia susceptibility.[1]

Contents

See also

References

  1. ^ a b "Entrez Gene: CACNA1S calcium channel, voltage-dependent, L type, alpha 1S subunit".

Further reading

  • Catterall WA, Perez-Reyes E, Snutch TP, Striessnig J (2006). "International Union of Pharmacology. XLVIII. Nomenclature and structure-function relationships of voltage-gated calcium channels.". Pharmacol. Rev. 57 (4): 411–25. doi:10.1124/pr.57.4.5. PMID 16382099. 
  • Rotman EI, De Jongh KS, Florio V, et al. (1992). "Specific phosphorylation of a COOH-terminal site on the full-length form of the alpha 1 subunit of the skeletal muscle calcium channel by cAMP-dependent protein kinase.". J. Biol. Chem. 267 (23): 16100–5. PMID 1322891. 
  • Röhrkasten A, Meyer HE, Nastainczyk W, et al. (1988). "cAMP-dependent protein kinase rapidly phosphorylates serine- 687 of the skeletal muscle receptor for calcium channel blockers.". J. Biol. Chem. 263 (30): 15325–9. PMID 2844809. 
  • Tanabe T, Takeshima H, Mikami A, et al. (1987). "Primary structure of the receptor for calcium channel blockers from skeletal muscle.". Nature 328 (6128): 313–8. doi:10.1038/328313a0. PMID 3037387. 
  • Hogan K, Powers PA, Gregg RG (1995). "Cloning of the human skeletal muscle alpha 1 subunit of the dihydropyridine-sensitive L-type calcium channel (CACNL1A3).". Genomics 24 (3): 608–9. doi:10.1006/geno.1994.1677. PMID 7713519. 
  • Elbaz A, Vale-Santos J, Jurkat-Rott K, et al. (1995). "Hypokalemic periodic paralysis and the dihydropyridine receptor (CACNL1A3): genotype/phenotype correlations for two predominant mutations and evidence for the absence of a founder effect in 16 caucasian families.". Am. J. Hum. Genet. 56 (2): 374–80. PMID 7847370. 
  • Boerman RH, Ophoff RA, Links TP, et al. (1995). "Mutation in DHP receptor alpha 1 subunit (CACLN1A3) gene in a Dutch family with hypokalaemic periodic paralysis.". J. Med. Genet. 32 (1): 44–7. PMID 7897626. 
  • Gregg RG, Couch F, Hogan K, Powers PA (1993). "Assignment of the human gene for the alpha 1 subunit of the skeletal muscle DHP-sensitive Ca2+ channel (CACNL1A3) to chromosome 1q31-q32.". Genomics 15 (1): 107–12. doi:10.1006/geno.1993.1017. PMID 7916735. 
  • Jurkat-Rott K, Lehmann-Horn F, Elbaz A, et al. (1995). "A calcium channel mutation causing hypokalemic periodic paralysis.". Hum. Mol. Genet. 3 (8): 1415–9. PMID 7987325. 
  • Ptácek LJ, Tawil R, Griggs RC, et al. (1994). "Dihydropyridine receptor mutations cause hypokalemic periodic paralysis.". Cell 77 (6): 863–8. PMID 8004673. 
  • Drouet B, Garcia L, Simon-Chazottes D, et al. (1994). "The gene coding for the alpha 1 subunit of the skeletal dihydropyridine receptor (Cchl1a3 = mdg) maps to mouse chromosome 1 and human 1q32.". Mamm. Genome 4 (9): 499–503. PMID 8118099. 
  • Iles DE, Segers B, Olde Weghuis D, et al. (1994). "Refined localization of the alpha 1-subunit of the skeletal muscle L-type voltage-dependent calcium channel (CACNL1A3) to human chromosome 1q32 by in situ hybridization.". Genomics 19 (3): 561–3. PMID 8188298. 
  • O'Brien RO, Taske NL, Hansbro PM, et al. (1996). "Exclusion of defects in the skeletal muscle specific regions of the DHPR alpha 1 subunit as frequent causes of malignant hyperthermia.". J. Med. Genet. 32 (11): 913–4. PMID 8592342. 
  • Hogan K, Gregg RG, Powers PA (1997). "The structure of the gene encoding the human skeletal muscle alpha 1 subunit of the dihydropyridine-sensitive L-type calcium channel (CACNL1A3).". Genomics 31 (3): 392–4. doi:10.1006/geno.1996.0066. PMID 8838325. 
  • Robinson RL, Monnier N, Wolz W, et al. (1997). "A genome wide search for susceptibility loci in three European malignant hyperthermia pedigrees.". Hum. Mol. Genet. 6 (6): 953–61. PMID 9175745. 
  • Monnier N, Procaccio V, Stieglitz P, Lunardi J (1997). "Malignant-hyperthermia susceptibility is associated with a mutation of the alpha 1-subunit of the human dihydropyridine-sensitive L-type voltage-dependent calcium-channel receptor in skeletal muscle.". Am. J. Hum. Genet. 60 (6): 1316–25. PMID 9199552. 
  • Meyers MB, Puri TS, Chien AJ, et al. (1998). "Sorcin associates with the pore-forming subunit of voltage-dependent L-type Ca2+ channels.". J. Biol. Chem. 273 (30): 18930–5. PMID 9668070. 
  • Morrill JA, Brown RH, Cannon SC (1999). "Gating of the L-type Ca channel in human skeletal myotubes: an activation defect caused by the hypokalemic periodic paralysis mutation R528H.". J. Neurosci. 18 (24): 10320–34. PMID 9852570. 
  • Protasi F, Paolini C, Nakai J, et al. (2003). "Multiple regions of RyR1 mediate functional and structural interactions with alpha(1S)-dihydropyridine receptors in skeletal muscle.". Biophys. J. 83 (6): 3230–44. PMID 12496092. 
  • Carsana A, Fortunato G, De Sarno C, et al. (2003). "Identification of new polymorphisms in the CACNA1S gene.". Clin. Chem. Lab. Med. 41 (1): 20–2. PMID 12636044. 

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v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channel
L-type/Cavα (1.1, 1.2, 1.3, 1.4) • N-type/Cavα2.2 • P-type/Cavα(2.1) • Q-type/Cavα2.1 • R-type/Cavα2.3 • T-type/Cavα(3.2)
α2δ-subunits (1, 2) • β-subunits (β1, β2, β3, β4) • γ-subunits (γ1, γ2, γ3, γ4)
Cation channels of sperm • Two-pore channel (1, 2)
Ligand-gated
Na+: Sodium channel
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) • Navβ (1, 2, 3, 4)
Other
K+: Potassium channel
Kvα (1-6) (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.10, 2.1, 2.2, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 4.3, 5.1, 6.1, 6.2, 6.3, 6.4)
Kvα (7-12) (7.1, 7.2, 7.3, 7.4, 7.5, 8.1, 8.2, 9.1, 9.2, 9.3, 10.1, 10.2, 11.1/hERG, 11.2, 11.3, 12.1, 12.2, 12.3)
Kvβ (1, 2, 3) • KCNIP (1, 2, 3, 4) • minK/ISK • MiRP (1, 2, 3) • Shaker gene
Kir (1.1, 2.1, 2.2, 2.3, 2.4) • GIRK/Kir (3.1, 3.2, 3.3, 3.4) • Kir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)
K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)
M+: TRP cation channel
TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (1, 2, 3) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)
Cl-: Chloride channel
CFTR • CLCA (1, 2, 3, 4) • CLCN (1, 2, 3, 4, 5, 6, 7, KA, KB) • CLIC (1, 2, 3, 4, 5, 6, L1) • CLNS (1A, 1B)
Cyclic nucleotide-gated
α1, α2, α3, α4, β1, β3, H1, H2, H3, H4
Porin
Other/general
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