KCNA2

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Potassium voltage-gated channel, shaker-related subfamily, member 2
Protein KCNA2 PDB 1dsx.png
PDB rendering based on 1dsx.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols KCNA2 ; HBK5; HK4; HUKIV; KV1.2; MK2; NGK1; RBK2
External IDs OMIM176262 MGI96659 HomoloGene21034 IUPHAR: Kv1.2 ChEMBL: 2086 GeneCards: KCNA2 Gene
RNA expression pattern
PBB GE KCNA2 208564 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 3737 16490
Ensembl ENSG00000177301 ENSMUSG00000040724
UniProt P16389 P63141
RefSeq (mRNA) NM_001204269 NM_008417
RefSeq (protein) NP_001191198 NP_032443
Location (UCSC) Chr 1:
111.14 – 111.17 Mb
Chr 3:
107.1 – 107.11 Mb
PubMed search [1] [2]

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.[1][2]

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.[2]

Interactions[edit]

KCNA2 has been shown to interact with KCNA4,[3] DLG4,[4] PTPRA,[5] KCNAB2,[3][6] RHOA[7] and Cortactin.[8]

See also[edit]

References[edit]

  1. ^ Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X (Dec 2005). "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. 
  2. ^ a b "Entrez Gene: KCNA2 potassium voltage-gated channel, shaker-related subfamily, member 2". 
  3. ^ a b Coleman, S K; Newcombe J; Pryke J; Dolly J O (Aug 1999). "Subunit composition of Kv1 channels in human CNS". J. Neurochem. (UNITED STATES) 73 (2): 849–58. doi:10.1046/j.1471-4159.1999.0730849.x. ISSN 0022-3042. PMID 10428084. 
  4. ^ Eldstrom, Jodene; Doerksen Kyle W; Steele David F; Fedida David (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Lett. (Netherlands) 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. ISSN 0014-5793. PMID 12435606. 
  5. ^ Tsai, W; Morielli A D; Cachero T G; Peralta E G (Jan 1999). "Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity". EMBO J. (ENGLAND) 18 (1): 109–18. doi:10.1093/emboj/18.1.109. ISSN 0261-4189. PMC 1171107. PMID 9878055. 
  6. ^ Nakahira, K; Shi G; Rhodes K J; Trimmer J S (Mar 1996). "Selective interaction of voltage-gated K+ channel beta-subunits with alpha-subunits". J. Biol. Chem. (UNITED STATES) 271 (12): 7084–9. doi:10.1074/jbc.271.12.7084. ISSN 0021-9258. PMID 8636142. 
  7. ^ Cachero, T G; Morielli A D; Peralta E G (Jun 1998). "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel". Cell (UNITED STATES) 93 (6): 1077–85. doi:10.1016/S0092-8674(00)81212-X. ISSN 0092-8674. PMID 9635436. 
  8. ^ Hattan, David; Nesti Edmund; Cachero Teresa G; Morielli Anthony D (Oct 2002). "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin". J. Biol. Chem. (United States) 277 (41): 38596–606. doi:10.1074/jbc.M205005200. ISSN 0021-9258. PMID 12151401. 

Further reading[edit]

External links[edit]

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