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KCNA2

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(Redirected from Kv1.2 potassium channel)
KCNA2
Identifiers
AliasesKCNA2, HBK5, HK4, HUKIV, KV1.2, MK2, NGK1, RBK2, EIEE32, potassium voltage-gated channel subfamily A member 2, DEE32
External IDsOMIM: 176262; MGI: 96659; HomoloGene: 21034; GeneCards: KCNA2; OMA:KCNA2 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001204269
NM_004974

NM_008417

RefSeq (protein)

NP_001191198
NP_004965

NP_032443

Location (UCSC)Chr 1: 110.52 – 110.63 MbChr 3: 107.01 – 107.02 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Potassium voltage-gated channel subfamily A member 2 also known as Kv1.2 is a protein that in humans is encoded by the KCNA2 gene.[5][6]

Function

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Potassium 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, shaker-related subfamily. This member contains six membrane-spanning domains with a shaker-type repeat in the fourth segment. It belongs to the delayed rectifier class, members of which allow nerve cells to efficiently repolarize following an action potential. The coding region of this gene is intronless, and the gene is clustered with genes KCNA3 and KCNA10 on chromosome 1.[6]

Interactions

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KCNA2 has been shown to interact with KCNA4,[7] DLG4,[8] PTPRA,[9] KCNAB2,[7][10] RHOA[11] and Cortactin.[12]

Clinical

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Mutations in this gene have been associated with hereditary spastic paraplegia.[13]

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000177301Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000040724Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X (December 2005). "International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels". Pharmacological Reviews. 57 (4): 473–508. doi:10.1124/pr.57.4.10. PMID 16382104. S2CID 219195192.
  6. ^ a b "Entrez Gene: KCNA2 potassium voltage-gated channel, shaker-related subfamily, member 2".
  7. ^ a b Coleman SK, Newcombe J, Pryke J, Dolly JO (August 1999). "Subunit composition of Kv1 channels in human CNS". Journal of Neurochemistry. 73 (2): 849–58. doi:10.1046/j.1471-4159.1999.0730849.x. PMID 10428084.
  8. ^ Eldstrom J, Doerksen KW, Steele DF, Fedida D (November 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters. 531 (3): 529–37. Bibcode:2002FEBSL.531..529E. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606. S2CID 40689829.
  9. ^ Tsai W, Morielli AD, Cachero TG, Peralta EG (January 1999). "Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity". The EMBO Journal. 18 (1): 109–18. doi:10.1093/emboj/18.1.109. PMC 1171107. PMID 9878055.
  10. ^ Nakahira K, Shi G, Rhodes KJ, Trimmer JS (March 1996). "Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits". The Journal of Biological Chemistry. 271 (12): 7084–9. doi:10.1074/jbc.271.12.7084. PMID 8636142.
  11. ^ Cachero TG, Morielli AD, Peralta EG (June 1998). "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel". Cell. 93 (6): 1077–85. doi:10.1016/S0092-8674(00)81212-X. PMID 9635436. S2CID 13943167.
  12. ^ Hattan D, Nesti E, Cachero TG, Morielli AD (October 2002). "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin". The Journal of Biological Chemistry. 277 (41): 38596–606. doi:10.1074/jbc.M205005200. PMID 12151401.
  13. ^ Helbig KL, Hedrich UB, Shinde DN, Krey I, Teichmann AC, Hentschel J, Schubert J, Chamberlin AC, Huether R, Lu HM, Alcaraz WA, Tang S, Jungbluth C, Dugan SL, Vainionpää L, Karle KN, Synofzik M, Schöls L, Schüle R, Lehesjoki AE, Helbig I, Lerche H, Lemke JR (October 2016). "A recurrent mutation in KCNA2 as a novel cause of hereditary spastic paraplegia and ataxia". Annals of Neurology. 80 (4): 638–642. doi:10.1002/ana.24762. PMC 5129488. PMID 27543892.

Further reading

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