SCN10A

sodium channel, voltage-gated, type X, alpha subunit
Available structures PDB 1byy
Identifiers
Symbols	SCN10A; PN3; SNS; hPN3
External IDs	OMIM: 604427 MGI: 108029 HomoloGene: 21300 IUPHAR: Nav1.8 GeneCards: SCN10A Gene
Gene Ontology Molecular function • voltage-gated ion channel activity • voltage-gated potassium channel activity • ion channel activity • protein binding • calcium ion binding • voltage-gated calcium channel activity • voltage-gated sodium channel activity • sodium ion binding Cellular component • membrane • integral to membrane • voltage-gated sodium channel complex • voltage-gated calcium channel complex • voltage-gated potassium channel complex Biological process • potassium ion transport • sensory perception • calcium ion transport • ion transport • sodium ion transport Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6336	20264
Ensembl	ENSG00000185313	ENSMUSG00000034533
UniProt	Q9Y5Y9	Q6QIY3
RefSeq (mRNA)	NM_006514	NM_009134
RefSeq (protein)	NP_006505	NP_033160
Location (UCSC)	Chr 3: 38.71 – 38.81 Mb	Chr 9: 119.52 – 119.6 Mb
PubMed search	[1]	[2]
This box: view · protein which in humans is encoded by the SCN10A gene.[1] Nav1.8 is a sodium channel subunit.[2][3][4] Function This subtype of voltage-gated sodium channel is expressed in nociceptors and has been proposed as a target for the development of new analgesics.[5] References ^ "Entrez Gene: sodium channel". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6336.  ^ Rabert DK, Koch BD, Ilnicka M, Obernolte RA, Naylor SL, Herman RC, Eglen RM, Hunter JC, Sangameswaran L (November 1998). "A tetrodotoxin-resistant voltage-gated sodium channel from human dorsal root ganglia, hPN3/SCN10A". Pain 78 (2): 107–14. doi:10.1016/S0304-3959(98)00120-1. PMID 9839820.  ^ Plummer NW, Meisler MH (April 1999). "Evolution and diversity of mammalian sodium channel genes". Genomics 57 (2): 323–31. doi:10.1006/geno.1998.5735. PMID 10198179.  ^ Catterall WA, Goldin AL, Waxman SG (December 2005). "International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels". Pharmacol. Rev. 57 (4): 397–409. doi:10.1124/pr.57.4.4. PMID 16382098.  ^ Cummins TR, Sheets PL, Waxman SG (October 2007). "Voltage-gated sodium channel blockers for the treatment of chronic pain". Pain 131 (3): 243–57. PMID 19442207.  Further reading Malik-Hall M, Poon WY, Baker MD, et al. (2003). "Sensory neuron proteins interact with the intracellular domains of sodium channel NaV1.8.". Brain Res. Mol. Brain Res. 110 (2): 298–304. doi:10.1016/S0169-328X(02)00661-7. PMID 12591166.  Yamaoka K, Inoue M, Miyazaki K, et al. (2009). "Synthetic Ciguatoxins Selectively Activate Nav1.8-derived Chimeric Sodium Channels Expressed in HEK293 Cells". J. Biol. Chem. 284 (12): 7597–605. doi:10.1074/jbc.M806481200. PMC 2658054. PMID 19164297. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2658054.  Choi JS, Hudmon A, Waxman SG, Dib-Hajj SD (2006). "Calmodulin regulates current density and frequency-dependent inhibition of sodium channel Nav1.8 in DRG neurons". J. Neurophysiol. 96 (1): 97–108. doi:10.1152/jn.00854.2005. PMID 16598065.  Liu CJ, Priest BT, Bugianesi RM, et al. (2006). "A high-capacity membrane potential FRET-based assay for NaV1.8 channels". Assay and drug development technologies 4 (1): 37–48. doi:10.1089/adt.2006.4.37. PMID 16506887.  Browne LE, Blaney FE, Yusaf SP, et al. (2009). "Structural Determinants of Drugs Acting on the Nav1.8 Channel". J. Biol. Chem. 284 (16): 10523–36. doi:10.1074/jbc.M807569200. PMC 2667739. PMID 19233853. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2667739.  Rabert DK, Koch BD, Ilnicka M, et al. (1998). "A tetrodotoxin-resistant voltage-gated sodium channel from human dorsal root ganglia, hPN3/SCN10A". Pain 78 (2): 107–14. doi:10.1016/S0304-3959(98)00120-1. PMID 9839820.  Plummer NW, Meisler MH (1999). "Evolution and diversity of mammalian sodium channel genes". Genomics 57 (2): 323–31. doi:10.1006/geno.1998.5735. PMID 10198179.  Catterall WA, Goldin AL, Waxman SG (2005). "International Union of Pharmacology. XLVII. Nomenclature and structure-function relationships of voltage-gated sodium channels". Pharmacol. Rev. 57 (4): 397–409. doi:10.1124/pr.57.4.4. PMID 16382098.

Na+: Sodium channel
Constitutively active Epithelial sodium channel (α, β, γ, δ) Proton gated Amiloride-sensitive cation channel (1, 2, 3, 4) Voltage-gated 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)

K+: Potassium channel
Voltage-gated Kvα1-6 (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) Kvα7-12 (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 · minK/ISK-like · MiRP (1, 2, 3) · Shaker gene Calcium-activated BK channel (α1, β1, β2, β3, β4) · SK channel (SK1, SK2, SK3, SK4) · KCa (1.1, 2.1, 2.2, 2.3, 3.1, 4.1, 4.2, 5.1) Inward-rectifier KATP · Kir (1.1, 2.1, 2.2, 2.3, 2.4, 2.6) · GIRK/Kir (3.1, 3.2, 3.3, 3.4) · Kir (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) · 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