KCND1

KCND1
Identifiers
Aliases	KCND1, KV4.1, potassium voltage-gated channel subfamily D member 1
External IDs	MGI: 96671 HomoloGene: 21035 GeneCards: KCND1
Targeted by Drug
dalfampridine, tetraethylammonium
Gene ontology Molecular function • potassium channel activity • delayed rectifier potassium channel activity • metal ion binding • voltage-gated ion channel activity • ion channel activity • A-type (transient outward) potassium channel activity • voltage-gated potassium channel activity Cellular component • integral component of membrane • cell projection • membrane • cellular component • voltage-gated potassium channel complex • plasma membrane • neuronal cell body • dendrite Biological process • regulation of ion transmembrane transport • ion transport • potassium ion transport • cardiac conduction • transmembrane transport • potassium ion transmembrane transport • transport • protein homooligomerization Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3750	16506
Ensembl	ENSG00000102057	ENSMUSG00000009731
UniProt	Q9NSA2	Q03719
RefSeq (mRNA)	NM_004979	NM_008423
RefSeq (protein)	NP_004970.3	NP_032449.1
Location (UCSC)	Chr X: 48.96 – 48.97 Mb	Chr X: 7.82 – 7.84 Mb
PubMed search
Wikidata
View/Edit Human		View/Edit Mouse

Potassium voltage-gated channel, Shal-related subfamily, member 1 (KCND1), also known as K_v4.1, is a human gene.

Voltage-gated potassium (Kv) channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. Their diverse functions include regulating neurotransmitter release, heart rate, insulin secretion, neuronal excitability, epithelial electrolyte transport, smooth muscle contraction, and cell volume. Four sequence-related potassium channel genes - shaker, shaw, shab, and shal - have been identified in Drosophila, and each has been shown to have human homolog(s). This gene encodes a member of the potassium channel, voltage-gated, shal-related subfamily, members of which form voltage-activated A-type potassium ion channels and are prominent in the repolarization phase of the action potential. This gene is expressed at moderate levels in all tissues analyzed, with lower levels in skeletal muscle.

See also

• Voltage-gated potassium channel

Further reading

• Gutman GA, Chandy KG, Grissmer S, et al. (2006). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels.". Pharmacol. Rev. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. 
• Kurschner C, Yuzaki M (1999). "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein.". J. Neurosci. 19 (18): 7770–80. PMID 10479680. 
• Isbrandt D, Leicher T, Waldschütz R, et al. (2000). "Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA).". Genomics. 64 (2): 144–54. doi:10.1006/geno.2000.6117. PMID 10729221. 
• Nakamura TY, Nandi S, Pountney DJ, et al. (2001). "Different effects of the Ca(2+)-binding protein, KChIP1, on two Kv4 subfamily members, Kv4.1 and Kv4.2.". FEBS Lett. 499 (3): 205–9. doi:10.1016/S0014-5793(01)02560-1. PMID 11423117. 
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. 
• Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039. 
• Jerng HH, Qian Y, Pfaffinger PJ (2005). "Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase 10 (DPP10).". Biophys. J. 87 (4): 2380–96. doi:10.1529/biophysj.104.042358. PMC 1304660. PMID 15454437. 
• Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. 
• Kim SJ, Choi WS, Han JS, et al. (2005). "A novel mechanism for the suppression of a voltage-gated potassium channel by glucose-dependent insulinotropic polypeptide: protein kinase A-dependent endocytosis.". J. Biol. Chem. 280 (31): 28692–700. doi:10.1074/jbc.M504913200. PMID 15955806. 

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