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KCNA5

From Wikipedia, the free encyclopedia
Protein-coding gene in humans

KCNA5
Identifiers
AliasesKCNA5, ATFB7, HCK1, HK2, HPCN1, KV1.5, PCN1, potassium voltage-gated channel subfamily A member 5
External IDsOMIM:176267;MGI:96662;HomoloGene:1683;GeneCards:KCNA5;OMA:KCNA5 - orthologs
Gene location (Human)
Chromosome 12 (human)
Chr.Chromosome 12 (human)[1]
Chromosome 12 (human)
Genomic location for KCNA5
Genomic location for KCNA5
Band12p13.32Start5,043,879bp[1]
End5,046,788bp[1]
Gene location (Mouse)
Chromosome 6 (mouse)
Chr.Chromosome 6 (mouse)[2]
Chromosome 6 (mouse)
Genomic location for KCNA5
Genomic location for KCNA5
Band6 F3|6 61.35 cMStart126,509,514bp[2]
End126,512,375bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • cardiac muscle tissue of right atrium

  • right auricle of heart

  • right coronary artery

  • popliteal artery

  • tibial arteries

  • testicle

  • Epithelium of choroid plexus

  • ascending aorta

  • left coronary artery

  • Descending thoracic aorta
Top expressed in
  • olfactory epithelium

  • epithelium of lens

  • trigeminal nerve

  • retina

  • endocardial cushion

  • olfactory tubercle

  • neural layer of retina

  • renal pelvis

  • nucleus accumbens

  • myocardium of ventricle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo /QuickGO
Orthologs
SpeciesHumanMouse
Entrez

3741

16493

Ensembl

ENSG00000130037

ENSMUSG00000045534

UniProt

P22460

Q61762

RefSeq (mRNA)

NM_002234

NM_145983

RefSeq (protein)

NP_002225

NP_666095

Location (UCSC)Chr 12: 5.04 – 5.05 MbChr 6: 126.51 – 126.51 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Potassium voltage-gated channel, shaker-related subfamily, member 5, also known asKCNA5 orKv1.5, is aprotein that in humans is encoded by theKCNA5gene.[5]

Function

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Potassium channels represent the most complex class of voltage-gated ion channels from both functional and structural standpoints. KCNA5 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, the function of which could restore the restingmembrane potential ofbeta cells after depolarization, thereby contributing to the regulation ofinsulin secretion. This gene isintronless, and the gene is clustered with genesKCNA1 andKCNA6 on chromosome 12.[5] Mutations in this gene have been related to bothatrial fibrillation[6] and sudden cardiac death.[7] KCNA5 are also key players in pulmonary vascular function, where they play a role in setting the resting membrane potential and its involvement during hypoxic pulmonary vasoconstriction.

Interactions

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KCNA5 has been shown tointeract withDLG4,[8][9] PDZ domain-containing proteins such as SAP97,[10] andActinin, alpha 2.[8][11]

See also

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References

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  1. ^abcGRCh38: Ensembl release 89: ENSG00000130037Ensembl, May 2017
  2. ^abcGRCm38: Ensembl release 89: ENSMUSG00000045534Ensembl, 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. ^ab"Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
  6. ^Olson TM, Alekseev AE, Liu XK, Park S, Zingman LV, Bienengraeber M, et al. (July 2006)."Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation".Human Molecular Genetics.15 (14):2185–2191.doi:10.1093/hmg/ddl143.PMID 16772329.
  7. ^Nielsen NH, Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, et al. (March 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients".Biochemical and Biophysical Research Communications.354 (3):776–782.doi:10.1016/j.bbrc.2007.01.048.PMID 17266934.
  8. ^abEldstrom J, Choi WS, Steele DF, Fedida D (July 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism".FEBS Letters.547 (1–3):205–211.Bibcode:2003FEBSL.547..205E.doi:10.1016/S0014-5793(03)00668-9.PMID 12860415.S2CID 34857270.
  9. ^Eldstrom J, Doerksen KW, Steele DF, Fedida D (November 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels".FEBS Letters.531 (3):529–537.Bibcode:2002FEBSL.531..529E.doi:10.1016/S0014-5793(02)03572-X.PMID 12435606.S2CID 40689829.
  10. ^Murata M, Buckett PD, Zhou J, Brunner M, Folco E, Koren G (December 2001)."SAP97 interacts with Kv1.5 in heterologous expression systems".American Journal of Physiology. Heart and Circulatory Physiology.281 (6):H2575 –H2584.doi:10.1152/ajpheart.2001.281.6.H2575.PMID 11709425.S2CID 28915450.
  11. ^Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, et al. (May 2000)."alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells".FEBS Letters.473 (2):188–194.Bibcode:2000FEBSL.473..188M.doi:10.1016/S0014-5793(00)01521-0.PMID 10812072.S2CID 13026110.

Further reading

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External links

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Ligand-gated
Voltage-gated
Constitutively active
Proton-gated
Voltage-gated
Calcium-activated
Inward-rectifier
Tandem pore domain
Voltage-gated
Miscellaneous
Cl:Chloride channel
H+:Proton channel
M+:CNG cation channel
M+:TRP cation channel
H2O (+solutes):Porin
Cytoplasm:Gap junction
By gating mechanism
Ion channel class
see alsodisorders

This article incorporates text from theUnited States National Library of Medicine, which is in thepublic domain.

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