Ca_v1.3

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

PDB rendering based on 2be6.

Available structures
PDB	2be6

Identifiers

Symbols

CACNA1D; CACH3; CACN4; CACNL1A2; CCHL1A2; Cav1.3

External IDs

OMIM: 114206 MGI: 88293 HomoloGene: 578 IUPHAR: Ca_v1.3 GeneCards: CACNA1D Gene

Gene Ontology
Molecular function	• voltage-gated ion channel activity • voltage-gated calcium channel activity
Cellular component	• plasma membrane • voltage-gated calcium channel complex • integral to membrane
Biological process	• energy reserve metabolic process • ion transport • calcium ion transport • axon guidance • regulation of insulin secretion • regulation of calcium ion transport via voltage-gated calcium channel activity • transmembrane transport
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 3:
53.53 – 53.85 Mb

Chr 14:
30.85 – 31.3 Mb

PubMed search

[1]

[2]

Ca_v1.3 also known as the calcium channel, voltage-dependent, L type, alpha 1D subunit (CACNA1D), is a human gene.^[1]

1 See also
2 References
3 Further reading
4 External links

References

^ "Entrez Gene: CACNA1D calcium channel, voltage-dependent, L type, alpha 1D subunit". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=776.

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. doi:10.1016/0896-6273(92)90109-Q. 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. doi:10.1073/pnas.89.2.584. PMC 48283. PMID 1309948. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=48283.
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. doi:10.1016/0888-7543(92)90078-7. 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. doi:10.1016/0888-7543(91)90014-6. 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. doi:10.1016/0169-328X(96)80478-5. PMID 8738134.
Yang SN, Larsson O, Bränström R, et al. (1999). "Syntaxin 1 interacts with the LD subtype of voltage-gated Ca2+ channels in pancreatic β cells". Proc. Natl. Acad. Sci. U.S.A. 96 (18): 10164–9. doi:10.1073/pnas.96.18.10164. PMC 17860. PMID 10468580. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=17860.
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. doi:10.1096/fj.00-0188com. 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 Ca2+ channel α1D subunit in postnatal pancreatic β cell generation". J. Clin. Invest. 108 (7): 1015–22. doi:10.1172/JCI13310. PMC 200955. PMID 11581302. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=200955.
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.

External links

MeSH CACNA1D+protein,+human

PDB gallery

2be6: 2.0 A crystal structure of the CaV1.2 IQ domain-Ca/CaM complex

Membrane transport protein: ion channels (TC 1A)

Ca²⁺: Calcium channel

Voltage-gated	L-type/Ca_vα (1.1, 1.2, 1.3, 1.4) · N-type/Ca_vα2.2 · P-type/Ca_vα(2.1) · Q-type/Ca_vα2.1 · R-type/Ca_vα2.3 · T-type/Ca_vα(3.1, 3.2, 3.3) α₂δ-subunits (1, 2) · β-subunits (β1, β2, β3, β4) · γ-subunits (γ1, γ2, γ3, γ4) Cation channels of sperm (1, 2, 3, 4) · Two-pore channel (1, 2)

Ligand-gated	Inositol trisphosphate receptor (1, 2, 3) · Ryanodine receptor (1, 2, 3)

Na⁺: Sodium channel

Constitutively active	Epithelial sodium channel (α, β, γ, δ)

Proton gated	Amiloride-sensitive cation channel (1, 2, 3, 4)

Voltage-gated	Na_vα (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8, 1.9, 7A) · Na_vβ (1, 2, 3, 4)

K⁺: Potassium channel

Voltage-gated	K_vα1-6 (1.1, 1.2, 1.3, 1.4, 1.5, 1.6, 1.7, 1.8) · (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) K_vα7-12 (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) K_vβ (1, 2, 3) · KCNIP (1, 2, 3, 4) · minK/ISK · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene

Calcium-activated	BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3, SK4) · K_Ca (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1)

Inward-rectifier	K_ATP · K_ir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/K_ir (3.1, 3.2, 3.3, 3.4) · K_ir (4.1, 4.2, 5.1, 6.1, 6.2, 7.1)

Tandem pore domain	K2P (1, 2, 3, 4, 5, 6, 7, 9, 10, 12, 13, 15, 16, 17, 18)

Other

Cl^-: Chloride channel	ANO1 · Bestrophin (1, 2) · 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)

H⁺: Voltage-gated	HVCN1

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) · TRPN · TRPP (1, 2) · TRPV (1, 2, 3, 4, 5, 6)

Cyclic nucleotide-gated (FC)	α (1, 2, 3, 4) · β (1, 2, 3) · HCN (1, 2, 3, 4)

Porin	Aquaporin (1, 2, 3, 4, 5, 7, 8, 9) · Voltage-dependent anion channel (1, 2, 3) · General bacterial porin family

Gap junction	Connexin: A (GJA1, GJA3, GJA4, GJA5, GJA8, GJA9, GJA10) · B (GJB1, GJB2, GJB3, GJB4, GJB5, GJB6, GJB7) · C (GJC1, GJC2, GJC3) · D (GJD2, GJD3, GJD4)) Innexin

General	Ligand-gated ion channel · Voltage-gated ion channel · Stretch-activated ion channel

see also disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

Cav1.3

Contents

See also

References

Further reading

External links

Ca_v1.3