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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Potassium voltage-gated channel, shaker-related subfamily, member 5''', also known as '''KCNA5''' or '''K<sub>v</sub>1.5''', is a [[protein]] that in humans is encoded by the ''KCNA5'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741| accessdate = }}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Potassium voltage-gated channel, shaker-related subfamily, member 5
| HGNCid = 6224
| Symbol = KCNA5
| AltSymbols =; HK2; HCK1; HPCN1; KV1.5; MGC117058; MGC117059; PCN1
| OMIM = 176267
| ECnumber = 
| Homologene = 1683
| MGIid = 96662
| GeneAtlas_image1 = PBB_GE_KCNA5_206762_at_tn.png
| Function = {{GNF_GO|id=GO:0005251 |text = delayed rectifier potassium channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0008076 |text = voltage-gated potassium channel complex}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3741
    | Hs_Ensembl = ENSG00000130037
    | Hs_RefseqProtein = NP_002225
    | Hs_RefseqmRNA = NM_002234
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 12
    | Hs_GenLoc_start = 5023346
    | Hs_GenLoc_end = 5026210
    | Hs_Uniprot = P22460
    | Mm_EntrezGene = 16493
    | Mm_Ensembl = ENSMUSG00000045534
    | Mm_RefseqmRNA = NM_145983
    | Mm_RefseqProtein = NP_666095
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 126498974
    | Mm_GenLoc_end = 126500782
    | Mm_Uniprot = Q9Z1R6
  }}
}}
'''Potassium voltage-gated channel, shaker-related subfamily, member 5''', also known as '''KCNA5''' or '''K<sub>v</sub>1.5''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
[[Potassium channel]]s 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 resting [[membrane potential]] of [[beta cell]]s after depolarization, thereby contributing to the regulation of [[insulin]] secretion. This gene is [[intron]]less, and the gene is clustered with genes [[Kv1.1|KCNA1]] and [[KCNA6]] on chromosome 12.<ref name="entrez" /> Mutations in this gene have been related to both [[atrial fibrillation]] <ref name=pmid16772329>{{cite journal | vauthors = Olson TM, Alekseev AE, Liu XK, Park S, Zingman LV, Bienengraeber M, Sattiraju S, Ballew JD, Jahangir A, Terzic A | title = Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation | journal = Human Molecular Genetics | volume = 15 | issue = 14 | pages = 2185–91 | date = Jul 2006 | pmid = 16772329 | doi = 10.1093/hmg/ddl143 }}</ref> and sudden cardiac death.<ref name=pmid17266934>{{cite journal | vauthors = Nielsen NH, Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, Bentzen BH, Sigurd B, Larsen LA, Andersen PS, Haunsø S, Kjeldsen K, Grunnet M, Christiansen M, Olesen SP | title = Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients | journal = Biochemical and Biophysical Research Communications | volume = 354 | issue = 3 | pages = 776–82 | date = Mar 2007 | pmid = 17266934 | doi = 10.1016/j.bbrc.2007.01.048 }}</ref> 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.
{{PBB_Summary
| section_title =
| summary_text = Potassium channels represent the most complex class of voltage-gated ino 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, the function of which could restore the resting membrane potential of beta cells after depolarization and thereby contribute to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.<ref name="entrez">{{cite web | title = Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3741| accessdate = }}</ref>
}}


==See also==
== Interactions ==
 
KCNA5 has been shown to [[Protein-protein interaction|interact]] with [[DLG4]]<ref name=pmid12860415>{{cite journal | vauthors = Eldstrom J, Choi WS, Steele DF, Fedida D | title = SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism | journal = FEBS Letters | volume = 547 | issue = 1-3 | pages = 205–11 | date = Jul 2003 | pmid = 12860415 | doi = 10.1016/S0014-5793(03)00668-9 }}</ref><ref name=pmid12435606>{{cite journal | vauthors = Eldstrom J, Doerksen KW, Steele DF, Fedida D | title = N-terminal PDZ-binding domain in Kv1 potassium channels | journal = FEBS Letters | volume = 531 | issue = 3 | pages = 529–37 | date = Nov 2002 | pmid = 12435606 | doi = 10.1016/S0014-5793(02)03572-X }}</ref> and [[Actinin, alpha 2]].<ref name=pmid12860415/><ref name=pmid10812072>{{cite journal | vauthors = Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D | title = alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells | journal = FEBS Letters | volume = 473 | issue = 2 | pages = 188–94 | date = May 2000 | pmid = 10812072 | doi = 10.1016/S0014-5793(00)01521-0 }}</ref>
 
== See also ==
* [[Voltage-gated potassium channel]]
* [[Voltage-gated potassium channel]]


==References==
== References ==
{{reflist|2}}
{{reflist}}


==Further reading==
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stühmer W, Wang X | title = International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels | journal = Pharmacological Reviews | volume = 57 | issue = 4 | pages = 473–508 | date = Dec 2005 | pmid = 16382104 | doi = 10.1124/pr.57.4.10 }}
| citations =
* {{cite journal | vauthors = Curran ME, Landes GM, Keating MT | title = Molecular cloning, characterization, and genomic localization of a human potassium channel gene | journal = Genomics | volume = 12 | issue = 4 | pages = 729–37 | date = Apr 1992 | pmid = 1349297 | doi = 10.1016/0888-7543(92)90302-9 }}
*{{cite journal | author=Gutman GA, Chandy KG, Grissmer S, ''et al.'' |title=International Union of Pharmacology. LIII. Nomenclature and molecular relationships of voltage-gated potassium channels. |journal=Pharmacol. Rev. |volume=57 |issue= 4 |pages= 473-508 |year= 2006 |pmid= 16382104 |doi= 10.1124/pr.57.4.10 }}
* {{cite journal | vauthors = Philipson LH, Hice RE, Schaefer K, LaMendola J, Bell GI, Nelson DJ, Steiner DF | title = Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 88 | issue = 1 | pages = 53–7 | date = Jan 1991 | pmid = 1986382 | pmc = 50746 | doi = 10.1073/pnas.88.1.53 }}
*{{cite journal | author=Curran ME, Landes GM, Keating MT |title=Molecular cloning, characterization, and genomic localization of a human potassium channel gene. |journal=Genomics |volume=12 |issue= 4 |pages= 729-37 |year= 1992 |pmid= 1349297 |doi= }}
* {{cite journal | vauthors = Tamkun MM, Knoth KM, Walbridge JA, Kroemer H, Roden DM, Glover DM | title = Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle | journal = FASEB Journal | volume = 5 | issue = 3 | pages = 331–7 | date = Mar 1991 | pmid = 2001794 | doi =  }}
*{{cite journal | author=Philipson LH, Hice RE, Schaefer K, ''et al.'' |title=Sequence and functional expression in Xenopus oocytes of a human insulinoma and islet potassium channel. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=88 |issue= 1 |pages= 53-7 |year= 1991 |pmid= 1986382 |doi= }}
* {{cite journal | vauthors = Mays DJ, Foose JM, Philipson LH, Tamkun MM | title = Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue | journal = The Journal of Clinical Investigation | volume = 96 | issue = 1 | pages = 282–92 | date = Jul 1995 | pmid = 7615797 | pmc = 185199 | doi = 10.1172/JCI118032 }}
*{{cite journal | author=Tamkun MM, Knoth KM, Walbridge JA, ''et al.'' |title=Molecular cloning and characterization of two voltage-gated K+ channel cDNAs from human ventricle. |journal=FASEB J. |volume=5 |issue= 3 |pages= 331-7 |year= 1991 |pmid= 2001794 |doi=  }}
* {{cite journal | vauthors = Crumb WJ, Wible B, Arnold DJ, Payne JP, Brown AM | title = Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity | journal = Molecular Pharmacology | volume = 47 | issue = 1 | pages = 181–90 | date = Jan 1995 | pmid = 7838127 | doi =  }}
*{{cite journal | author=Mays DJ, Foose JM, Philipson LH, Tamkun MM |title=Localization of the Kv1.5 K+ channel protein in explanted cardiac tissue. |journal=J. Clin. Invest. |volume=96 |issue= 1 |pages= 282-92 |year= 1995 |pmid= 7615797 |doi= }}
* {{cite journal | vauthors = Phromchotikul T, Browne DL, Curran ME, Keating MT, Litt M | title = Dinucleotide repeat polymorphism at the KCNA5 locus | journal = Human Molecular Genetics | volume = 2 | issue = 9 | pages = 1512 | date = Sep 1993 | pmid = 8242092 | doi = 10.1093/hmg/2.9.1512-a }}
*{{cite journal | author=Crumb WJ, Wible B, Arnold DJ, ''et al.'' |title=Blockade of multiple human cardiac potassium currents by the antihistamine terfenadine: possible mechanism for terfenadine-associated cardiotoxicity. |journal=Mol. Pharmacol. |volume=47 |issue= 1 |pages= 181-90 |year= 1995 |pmid= 7838127 |doi=  }}
* {{cite journal | vauthors = Albrecht B, Weber K, Pongs O | title = Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13 | journal = Receptors & Channels | volume = 3 | issue = 3 | pages = 213–20 | year = 1996 | pmid = 8821794 | doi =  }}
*{{cite journal | author=Phromchotikul T, Browne DL, Curran ME, ''et al.'' |title=Dinucleotide repeat polymorphism at the KCNA5 locus. |journal=Hum. Mol. Genet. |volume=2 |issue= 9 |pages= 1512 |year= 1993 |pmid= 8242092 |doi= }}
* {{cite journal | vauthors = Holmes TC, Fadool DA, Ren R, Levitan IB | title = Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain | journal = Science | volume = 274 | issue = 5295 | pages = 2089–91 | date = Dec 1996 | pmid = 8953041 | doi = 10.1126/science.274.5295.2089 }}
*{{cite journal | author=Albrecht B, Weber K, Pongs O |title=Characterization of a voltage-activated K-channel gene cluster on human chromosome 12p13. |journal=Recept. Channels |volume=3 |issue= 3 |pages= 213-20 |year= 1996 |pmid= 8821794 |doi=  }}
* {{cite journal | vauthors = Lacerda AE, Roy ML, Lewis EW, Rampe D | title = Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart | journal = Molecular Pharmacology | volume = 52 | issue = 2 | pages = 314–22 | date = Aug 1997 | pmid = 9271355 | doi =  }}
*{{cite journal | author=Holmes TC, Fadool DA, Ren R, Levitan IB |title=Association of Src tyrosine kinase with a human potassium channel mediated by SH3 domain. |journal=Science |volume=274 |issue= 5295 |pages= 2089-91 |year= 1997 |pmid= 8953041 |doi= }}
* {{cite journal | vauthors = Kääb S, Dixon J, Duc J, Ashen D, Näbauer M, Beuckelmann DJ, Steinbeck G, McKinnon D, Tomaselli GF | title = Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density | journal = Circulation | volume = 98 | issue = 14 | pages = 1383–93 | date = Oct 1998 | pmid = 9760292 | doi = 10.1161/01.cir.98.14.1383 }}
*{{cite journal | author=Lacerda AE, Roy ML, Lewis EW, Rampe D |title=Interactions of the nonsedating antihistamine loratadine with a Kv1.5-type potassium channel cloned from human heart. |journal=Mol. Pharmacol. |volume=52 |issue= 2 |pages= 314-22 |year= 1997 |pmid= 9271355 |doi=  }}
* {{cite journal | vauthors = Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D | title = alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells | journal = FEBS Letters | volume = 473 | issue = 2 | pages = 188–94 | date = May 2000 | pmid = 10812072 | doi = 10.1016/S0014-5793(00)01521-0 }}
*{{cite journal | author=Kääb S, Dixon J, Duc J, ''et al.'' |title=Molecular basis of transient outward potassium current downregulation in human heart failure: a decrease in Kv4.3 mRNA correlates with a reduction in current density. |journal=Circulation |volume=98 |issue= 14 |pages= 1383-93 |year= 1998 |pmid= 9760292 |doi= }}
* {{cite journal | vauthors = Peretz A, Gil-Henn H, Sobko A, Shinder V, Attali B, Elson A | title = Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon | journal = The EMBO Journal | volume = 19 | issue = 15 | pages = 4036–45 | date = Aug 2000 | pmid = 10921884 | pmc = 306594 | doi = 10.1093/emboj/19.15.4036 }}
*{{cite journal | author=Maruoka ND, Steele DF, Au BP, ''et al.'' |title=alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells. |journal=FEBS Lett. |volume=473 |issue= 2 |pages= 188-94 |year= 2000 |pmid= 10812072 |doi= }}
* {{cite journal | vauthors = Nitabach MN, Llamas DA, Araneda RC, Intile JL, Thompson IJ, Zhou YI, Holmes TC | title = A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 98 | issue = 2 | pages = 705–10 | date = Jan 2001 | pmid = 11149959 | pmc = 14652 | doi = 10.1073/pnas.031446198 }}
*{{cite journal | author=Peretz A, Gil-Henn H, Sobko A, ''et al.'' |title=Hypomyelination and increased activity of voltage-gated K(+) channels in mice lacking protein tyrosine phosphatase epsilon. |journal=EMBO J. |volume=19 |issue= 15 |pages= 4036-45 |year= 2000 |pmid= 10921884 |doi= 10.1093/emboj/19.15.4036 }}
* {{cite journal | vauthors = Cukovic D, Lu GW, Wible B, Steele DF, Fedida D | title = A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2 | journal = FEBS Letters | volume = 498 | issue = 1 | pages = 87–92 | date = Jun 2001 | pmid = 11389904 | doi = 10.1016/S0014-5793(01)02505-4 }}
*{{cite journal | author=Nitabach MN, Llamas DA, Araneda RC, ''et al.'' |title=A mechanism for combinatorial regulation of electrical activity: Potassium channel subunits capable of functioning as Src homology 3-dependent adaptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 2 |pages= 705-10 |year= 2001 |pmid= 11149959 |doi= 10.1073/pnas.031446198 }}
* {{cite journal | vauthors = Kurata HT, Soon GS, Eldstrom JR, Lu GW, Steele DF, Fedida D | title = Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels | journal = The Journal of Biological Chemistry | volume = 277 | issue = 32 | pages = 29045–53 | date = Aug 2002 | pmid = 12021261 | doi = 10.1074/jbc.M111470200 }}
*{{cite journal | author=Cukovic D, Lu GW, Wible B, ''et al.'' |title=A discrete amino terminal domain of Kv1.5 and Kv1.4 potassium channels interacts with the spectrin repeats of alpha-actinin-2. |journal=FEBS Lett. |volume=498 |issue= 1 |pages= 87-92 |year= 2001 |pmid= 11389904 |doi= }}
* {{cite journal | vauthors = Williams CP, Hu N, Shen W, Mashburn AB, Murray KT | title = Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 302 | issue = 2 | pages = 545–50 | date = Aug 2002 | pmid = 12130714 | doi = 10.1124/jpet.102.033357 }}
*{{cite journal | author=Kurata HT, Soon GS, Eldstrom JR, ''et al.'' |title=Amino-terminal determinants of U-type inactivation of voltage-gated K+ channels. |journal=J. Biol. Chem. |volume=277 |issue= 32 |pages= 29045-53 |year= 2002 |pmid= 12021261 |doi= 10.1074/jbc.M111470200 }}
* {{cite journal | vauthors = Eldstrom J, Doerksen KW, Steele DF, Fedida D | title = N-terminal PDZ-binding domain in Kv1 potassium channels | journal = FEBS Letters | volume = 531 | issue = 3 | pages = 529–37 | date = Nov 2002 | pmid = 12435606 | doi = 10.1016/S0014-5793(02)03572-X }}
*{{cite journal | author=Williams CP, Hu N, Shen W, ''et al.'' |title=Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit. |journal=J. Pharmacol. Exp. Ther. |volume=302 |issue= 2 |pages= 545-50 |year= 2002 |pmid= 12130714 |doi= 10.1124/jpet.102.033357 }}
* {{cite journal | vauthors = Zhang S, Kurata HT, Kehl SJ, Fedida D | title = Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition | journal = The Journal of General Physiology | volume = 121 | issue = 3 | pages = 215–25 | date = Mar 2003 | pmid = 12601085 | pmc = 2217332 | doi = 10.1085/jgp.20028760 }}
*{{cite journal | author=Eldstrom J, Doerksen KW, Steele DF, Fedida D |title=N-terminal PDZ-binding domain in Kv1 potassium channels. |journal=FEBS Lett. |volume=531 |issue= 3 |pages= 529-37 |year= 2002 |pmid= 12435606 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal  | author=Zhang S, Kurata HT, Kehl SJ, Fedida D |title=Rapid induction of P/C-type inactivation is the mechanism for acid-induced K+ current inhibition. |journal=J. Gen. Physiol. |volume=121 |issue= 3 |pages= 215-25 |year= 2003 |pmid= 12601085 |doi=  }}
}}
{{refend}}
{{refend}}


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* {{MeshName|KCNA5+protein,+human}}
* {{MeshName|KCNA5+protein,+human}}


{{Ion channels|g3}}
[[Category:Ion channels]]
{{NLM content}}
{{membrane-protein-stub}}
{{membrane-protein-stub}}
{{NLM content}}
{{Ion channels}}
[[Category:Ion channels]]
{{WikiDoc Sources}}

Latest revision as of 01:47, 27 October 2017

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Potassium voltage-gated channel, shaker-related subfamily, member 5, also known as KCNA5 or Kv1.5, is a protein that in humans is encoded by the KCNA5 gene.[1]

Function

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 resting membrane potential of beta cells after depolarization, thereby contributing to the regulation of insulin secretion. This gene is intronless, and the gene is clustered with genes KCNA1 and KCNA6 on chromosome 12.[1] Mutations in this gene have been related to both atrial fibrillation [2] and sudden cardiac death.[3] 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

KCNA5 has been shown to interact with DLG4[4][5] and Actinin, alpha 2.[4][6]

See also

References

  1. ↑ 1.0 1.1 "Entrez Gene: KCNA5 potassium voltage-gated channel, shaker-related subfamily, member 5".
  2. ↑ Olson TM, Alekseev AE, Liu XK, Park S, Zingman LV, Bienengraeber M, Sattiraju S, Ballew JD, Jahangir A, Terzic A (Jul 2006). "Kv1.5 channelopathy due to KCNA5 loss-of-function mutation causes human atrial fibrillation". Human Molecular Genetics. 15 (14): 2185–91. doi:10.1093/hmg/ddl143. PMID 16772329.
  3. ↑ Nielsen NH, Winkel BG, Kanters JK, Schmitt N, Hofman-Bang J, Jensen HS, Bentzen BH, Sigurd B, Larsen LA, Andersen PS, Haunsø S, Kjeldsen K, Grunnet M, Christiansen M, Olesen SP (Mar 2007). "Mutations in the Kv1.5 channel gene KCNA5 in cardiac arrest patients". Biochemical and Biophysical Research Communications. 354 (3): 776–82. doi:10.1016/j.bbrc.2007.01.048. PMID 17266934.
  4. ↑ 4.0 4.1 Eldstrom J, Choi WS, Steele DF, Fedida D (Jul 2003). "SAP97 increases Kv1.5 currents through an indirect N-terminal mechanism". FEBS Letters. 547 (1–3): 205–11. doi:10.1016/S0014-5793(03)00668-9. PMID 12860415.
  5. ↑ Eldstrom J, Doerksen KW, Steele DF, Fedida D (Nov 2002). "N-terminal PDZ-binding domain in Kv1 potassium channels". FEBS Letters. 531 (3): 529–37. doi:10.1016/S0014-5793(02)03572-X. PMID 12435606.
  6. ↑ Maruoka ND, Steele DF, Au BP, Dan P, Zhang X, Moore ED, Fedida D (May 2000). "alpha-actinin-2 couples to cardiac Kv1.5 channels, regulating current density and channel localization in HEK cells". FEBS Letters. 473 (2): 188–94. doi:10.1016/S0014-5793(00)01521-0. PMID 10812072.

Further reading

External links

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

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