KCND1

KCND1
Identifiers
AliasesKCND1, KV4.1, potassium voltage-gated channel subfamily D member 1
External IDsMGI: 96671 HomoloGene: 21035 GeneCards: KCND1
Gene location (Human)
Chr.X chromosome (human)[1]
BandXp11.23Start48,961,378 bp[1]
End48,971,569 bp[1]
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez

3750

16506

Ensembl

ENSG00000102057

ENSMUSG00000009731

UniProt

Q9NSA2

Q03719

RefSeq (mRNA)

NM_004979

NM_008423

RefSeq (protein)

NP_004970

NP_032449

Location (UCSC)Chr X: 48.96 – 48.97 MbChr X: 7.82 – 7.84 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Potassium voltage-gated channel, Shal-related subfamily, member 1 (KCND1), also known as Kv4.1, is a human gene.[5]

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.[5]

See also

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000102057 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000009731 - Ensembl, May 2017
  3. ↑ "Human PubMed Reference:".
  4. ↑ "Mouse PubMed Reference:".
  5. 1 2 "Entrez Gene: KCND1 potassium voltage-gated channel, Shal-related subfamily, member 1".

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.


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