Cav1.2

From Wikipedia, the free encyclopedia

The correct title of this article is Ca_v1.2. It features superscript or subscript characters that are substituted or omitted because of technical limitations.

Calcium channel, voltage-dependent, L type, alpha 1C subunit

PDB rendering based on 2be6.

Available structures: 2be6

Identifiers

Symbol(s)

CACNA1C; CACH2; CACN2; CACNL1A1; CCHL1A1; CaV1.2; MGC120730; TS

External IDs

OMIM: 114205 MGI: 103013 HomoloGene: 55484

Gene ontology
Molecular Function:	• ion channel activity • voltage-gated calcium channel activity • calcium ion binding • calmodulin binding
Cellular Component:	• voltage-gated calcium channel complex • postsynaptic density • membrane • integral to membrane
Biological Process:	• ion transport • calcium ion transport • regulation of heart contraction

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_000719 (mRNA)
NP_000710 (protein)

NM_009781 (mRNA)
NP_033911 (protein)

Location

n/a

Chr 6: 118.56 - 119.02 Mb

Pubmed search

[1]

[2]

Calcium channel, voltage-dependent, L type, alpha 1C subunit (also known as Ca_v1.2) is a subunit of L-type voltage-dependent calcium channel encoded by the CACNA1C gene, mutation in which are associated with a variant of Long QT syndrome called Timothy's syndrome and also with Brugada syndrome.

1 See also
2 References
3 Further reading
4 External links

[edit] See also

Calcium channel

[edit] References

[edit] 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.
Soldatov NM (1992). "Molecular diversity of L-type Ca2+ channel transcripts in human fibroblasts.". Proc. Natl. Acad. Sci. U.S.A. 89 (10): 4628–32. PMID 1316612.
Powers PA, Gregg RG, Hogan K (1992). "Linkage mapping of the human gene for the alpha 1 subunit of the cardiac DHP-sensitive Ca2+ channel (CACNL1A1) to chromosome 12p13.2-pter using a dinucleotide repeat.". Genomics 14 (1): 206–7. PMID 1330882.
Sun W, McPherson JD, Hoang DQ, et al. (1993). "Mapping of a human brain voltage-gated calcium channel to human chromosome 12p13-pter.". Genomics 14 (4): 1092–4. PMID 1335957.
Lacerda AE, Kim HS, Ruth P, et al. (1991). "Normalization of current kinetics by interaction between the alpha 1 and beta subunits of the skeletal muscle dihydropyridine-sensitive Ca2+ channel.". Nature 352 (6335): 527–30. doi:10.1038/352527a0. PMID 1650913.
Powers PA, Gregg RG, Lalley PA, et al. (1991). "Assignment of the human gene for the alpha 1 subunit of the cardiac DHP-sensitive Ca2+ channel (CCHL1A1) to chromosome 12p12-pter.". Genomics 10 (3): 835–9. PMID 1653763.
Perez-Reyes E, Wei XY, Castellano A, Birnbaumer L (1990). "Molecular diversity of L-type calcium channels. Evidence for alternative splicing of the transcripts of three non-allelic genes.". J. Biol. Chem. 265 (33): 20430–6. PMID 2173707.
Soldatov NM, Bouron A, Reuter H (1995). "Different voltage-dependent inhibition by dihydropyridines of human Ca2+ channel splice variants.". J. Biol. Chem. 270 (18): 10540–3. PMID 7737988.
Soldatov NM (1994). "Genomic structure of human L-type Ca2+ channel.". Genomics 22 (1): 77–87. doi:10.1006/geno.1994.1347. PMID 7959794.
Tang S, Mikala G, Bahinski A, et al. (1993). "Molecular localization of ion selectivity sites within the pore of a human L-type cardiac calcium channel.". J. Biol. Chem. 268 (18): 13026–9. PMID 8099908.
Schultz D, Mikala G, Yatani A, et al. (1993). "Cloning, chromosomal localization, and functional expression of the alpha 1 subunit of the L-type voltage-dependent calcium channel from normal human heart.". Proc. Natl. Acad. Sci. U.S.A. 90 (13): 6228–32. PMID 8392192.
Perets T, Blumenstein Y, Shistik E, et al. (1996). "A potential site of functional modulation by protein kinase A in the cardiac Ca2+ channel alpha 1C subunit.". FEBS Lett. 384 (2): 189–92. PMID 8612821.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction.". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID 8619474.
Soldatov NM, Zühlke RD, Bouron A, Reuter H (1997). "Molecular structures involved in L-type calcium channel inactivation. Role of the carboxyl-terminal region encoded by exons 40-42 in alpha1C subunit in the kinetics and Ca2+ dependence of inactivation.". J. Biol. Chem. 272 (6): 3560–6. PMID 9013606.
Klöckner U, Mikala G, Eisfeld J, et al. (1997). "Properties of three COOH-terminal splice variants of a human cardiac L-type Ca2+-channel alpha1-subunit.". Am. J. Physiol. 272 (3 Pt 2): H1372–81. PMID 9087614.
Yu W, Andersson B, Worley KC, et al. (1997). "Large-scale concatenation cDNA sequencing.". Genome Res. 7 (4): 353–8. PMID 9110174.
Gao T, Yatani A, Dell'Acqua ML, et al. (1997). "cAMP-dependent regulation of cardiac L-type Ca2+ channels requires membrane targeting of PKA and phosphorylation of channel subunits.". Neuron 19 (1): 185–96. PMID 9247274.
Zühlke RD, Bouron A, Soldatov NM, Reuter H (1998). "Ca2+ channel sensitivity towards the blocker isradipine is affected by alternative splicing of the human alpha1C subunit gene.". FEBS Lett. 427 (2): 220–4. PMID 9607315.
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.
Liu WS, Soldatov NM, Gustavsson I, Chowdhary BP (1999). "Fiber-FISH analysis of the 3'-terminal region of the human L-type Ca2+ channel alpha 1C subunit gene.". Hereditas 129 (2): 169–75. PMID 10022083.

[edit] External links

MeSH CACNA1C+protein,+human

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v • d • e Membrane transport protein: ion channels

Ca²⁺: Calcium channel	Voltage-dependent calcium channel (L-type/Ca_vα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Ca_vα(2.1), Q-type, R-type, T-type, α₂δ-subunits (1, 2), β-subunits (β1, β2, β3, β4), γ-subunits (γ1, γ2, γ3, γ4) Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel

Na⁺: Sodium channel	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Na_vβ (1, 2, 3, 4) • Epithelial sodium channel

K⁺: Potassium channel	Voltage-gated (K_vα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 3.1, 3.4, 4.1, 4.2, 4.3, 6.1, 7.1, 7.2, 7.3, 7.4, 7.5, 9.3, 10.1, 11.1/hERG) • K_vβ (1, 2), Shaker gene, KCNE1) Calcium-activated (BK channel: α1, β1, β2, β3, β4; SK channel: SK1, SK2, SK3, SK4) Inward-rectifier K_ir (1.1, 2.1, 2.2, 2.3, 2.4, GIRK, 3.1, 3.2, 3.3, 3.4, 4.1, 4.2, 5.1, 6.1, 6.2, 7.1) Tandem pore domain K2P (1, 2, 3, 4, 6, 9, 15, 17)

Cl^-: Chloride channel	Cystic fibrosis transmembrane conductance regulator

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) • Voltage-dependent anion channel (1)

Cations: TRP	TRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2) • TRPV (1, 2, 3, 4, 5, 6)

Other/general	Voltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α2, α3, β1, β3, H1, H2, H3, H4) • Stretch-activated ion channel

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Cav1.2

From Wikipedia, the free encyclopedia

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[edit] See also

[edit] References

[edit] Further reading

[edit] External links

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