Cav1.3

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The correct title of this article is Cav1.3. It features superscript or subscript characters that are substituted or omitted because of technical limitations.


Calcium channel, voltage-dependent, L type, alpha 1D subunit
PDB rendering based on 2be6.
Available structures: 2be6
Identifiers
Symbol(s) CACNA1D; CACH3; CACN4; CACNL1A2; CCHL1A2; Cav1.3
External IDs OMIM: 114206 MGI: 88293 HomoloGene: 578
RNA expression pattern

More reference expression data
Orthologs
Human Mouse
Entrez 776 12289
Ensembl ENSG00000157388 ENSMUSG00000015968
Uniprot Q01668 Q99246
Refseq NM_000720 (mRNA)
NP_000711 (protein)		 NM_028981 (mRNA)
NP_083257 (protein)
Location Chr 3: 53.5 - 53.82 Mb Chr 14: 28.87 - 29.32 Mb
Pubmed search [1] [2]

Cav1.3 also known as the calcium channel, voltage-dependent, L type, alpha 1D subunit (CACNA1D), is a human gene.[1]


Contents

[edit] See also

[edit] References

  1. ^ Entrez Gene: CACNA1D calcium channel, voltage-dependent, L type, alpha 1D subunit.

[edit] Further reading

  • Williams ME, Feldman DH, McCue AF, et al. (1992). "Structure and functional expression of alpha 1, alpha 2, and beta subunits of a novel human neuronal calcium channel subtype.". Neuron 8 (1): 71–84. PMID 1309651. 
  • Seino S, Chen L, Seino M, et al. (1992). "Cloning of the alpha 1 subunit of a voltage-dependent calcium channel expressed in pancreatic beta cells.". Proc. Natl. Acad. Sci. U.S.A. 89 (2): 584–8. PMID 1309948. 
  • Seino S, Yamada Y, Espinosa R, et al. (1992). "Assignment of the gene encoding the alpha 1 subunit of the neuroendocrine/brain-type calcium channel (CACNL1A2) to human chromosome 3, band p14.3.". Genomics 13 (4): 1375–7. PMID 1324226. 
  • Chin HM, Kozak CA, Kim HL, et al. (1992). "A brain L-type calcium channel alpha 1 subunit gene (CCHL1A2) maps to mouse chromosome 14 and human chromosome 3.". Genomics 11 (4): 914–9. PMID 1664412. 
  • Mori Y, Friedrich T, Kim MS, et al. (1991). "Primary structure and functional expression from complementary DNA of a brain calcium channel.". Nature 350 (6317): 398–402. doi:10.1038/350398a0. PMID 1849233. 
  • Yamada Y, Masuda K, Li Q, et al. (1995). "The structures of the human calcium channel alpha 1 subunit (CACNL1A2) and beta subunit (CACNLB3) genes.". Genomics 27 (2): 312–9. doi:10.1006/geno.1995.1048. PMID 7557998. 
  • Puro DG, Hwang JJ, Kwon OJ, Chin H (1996). "Characterization of an L-type calcium channel expressed by human retinal Müller (glial) cells.". Brain Res. Mol. Brain Res. 37 (1-2): 41–8. PMID 8738134. 
  • Yang SN, Larsson O, Bränström R, et al. (1999). "Syntaxin 1 interacts with the L(D) subtype of voltage-gated Ca(2+) channels in pancreatic beta cells.". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10164–9. PMID 10468580. 
  • Bell DC, Butcher AJ, Berrow NS, et al. (2001). "Biophysical properties, pharmacology, and modulation of human, neuronal L-type (alpha(1D), Ca(V)1.3) voltage-dependent calcium currents.". J. Neurophysiol. 85 (2): 816–27. PMID 11160515. 
  • Rosenthal R, Thieme H, Strauss O (2001). "Fibroblast growth factor receptor 2 (FGFR2) in brain neurons and retinal pigment epithelial cells act via stimulation of neuroendocrine L-type channels (Ca(v)1.3).". FASEB J. 15 (6): 970–7. PMID 11292657. 
  • Davare MA, Avdonin V, Hall DD, et al. (2001). "A beta2 adrenergic receptor signaling complex assembled with the Ca2+ channel Cav1.2.". Science 293 (5527): 98–101. doi:10.1126/science.293.5527.98. PMID 11441182. 
  • Namkung Y, Skrypnyk N, Jeong MJ, et al. (2001). "Requirement for the L-type Ca(2+) channel alpha(1D) subunit in postnatal pancreatic beta cell generation.". J. Clin. Invest. 108 (7): 1015–22. PMID 11581302. 
  • Stokes L, Gordon J, Grafton G (2004). "Non-voltage-gated L-type Ca2+ channels in human T cells: pharmacology and molecular characterization of the major alpha pore-forming and auxiliary beta-subunits.". J. Biol. Chem. 279 (19): 19566–73. doi:10.1074/jbc.M401481200. PMID 14981074. 
  • Qu Y, Baroudi G, Yue Y, Boutjdir M (2006). "Novel molecular mechanism involving alpha1D (Cav1.3) L-type calcium channel in autoimmune-associated sinus bradycardia.". Circulation 111 (23): 3034–41. doi:10.1161/CIRCULATIONAHA.104.517326. PMID 15939813. 
  • Baroudi G, Qu Y, Ramadan O, et al. (2006). "Protein kinase C activation inhibits Cav1.3 calcium channel at NH2-terminal serine 81 phosphorylation site.". Am. J. Physiol. Heart Circ. Physiol. 291 (4): H1614–22. doi:10.1152/ajpheart.00095.2006. PMID 16973824. 
  • Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.". Cell 127 (3): 635–48. doi:10.1016/j.cell.2006.09.026. PMID 17081983. 

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v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channel
Na+: Sodium channel
Navα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.9, 7A) • Navβ (1, 2, 3, 4) • Epithelial sodium channel
K+: Potassium channel
Cl-: Chloride channel
Porin
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)
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