KCND3: Difference between revisions

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{{Infobox_gene}}
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'''Potassium voltage-gated channel subfamily D member 3''' also known as '''K<sub>v</sub>4.3''' is a [[protein]] that in humans is encoded by the ''KCND3'' [[gene]].<ref name="pmid10942109">{{cite journal |vauthors=Postma AV, Bezzina CR, de Vries JF, Wilde AA, Moorman AF, Mannens MM | title = Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3 | journal = Hum Genet | volume = 106 | issue = 6 | pages = 614–9 |date=Aug 2000 | pmid = 10942109 | pmc =  | doi =10.1007/s004390050033  }}</ref><ref name="pmid16382104">{{cite journal |vauthors=Gutman GA, Chandy KG, Grissmer S, Lazdunski M, McKinnon D, Pardo LA, Robertson GA, Rudy B, Sanguinetti MC, Stuhmer W, Wang X | 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 |date=Dec 2005 | pmid = 16382104 | pmc =  | doi = 10.1124/pr.57.4.10 }}</ref><ref name="entrez"/> It contributes to the [[cardiac transient outward potassium current]] (I<sub>to1</sub>), the main contributing current to the [[repolarization|repolarizing]] [[Cardiac action potential#Phase 1|phase 1 of the cardiac action potential]].<ref name=oudit>{{cite journal |vauthors=Oudit GY, Kassiri Z, Sah R, Ramirez RJ, Zobel C, Backx PH |title=The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium |journal=J. Mol. Cell. Cardiol. |volume=33 |issue=5 |pages=851–72 |date=May 2001 |pmid=11343410 |doi=10.1006/jmcc.2001.1376 |url=}}</ref>
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== Function ==
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Voltage-gated potassium ([[voltage-gated potassium channel|K<sub>v</sub>]]) 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).
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K<sub>v</sub>4.3 is 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 member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KCND3 potassium voltage-gated channel, Shal-related subfamily, member 3| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3752| accessdate = }}</ref>


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Clinical significance ==
{{GNF_Protein_box
| image = PBB_Protein_KCND3_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1s1g.
| PDB = {{PDB2|1s1g}}, {{PDB2|2i2r}}, {{PDB2|2nz0}}
| Name = Potassium voltage-gated channel, Shal-related subfamily, member 3
| HGNCid = 6239
| Symbol = KCND3
| AltSymbols =; KCND3L; KCND3S; KSHIVB; KV4.3; MGC142035; MGC142037
| OMIM = 605411
| ECnumber = 
| Homologene = 21036
| MGIid = 1928743
| GeneAtlas_image1 = PBB_GE_KCND3_211827_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_KCND3_211301_at_tn.png
| GeneAtlas_image3 = PBB_GE_KCND3_215014_at_tn.png
| Function = {{GNF_GO|id=GO:0005249 |text = voltage-gated potassium channel activity}} {{GNF_GO|id=GO:0005250 |text = A-type (transient outward) potassium channel activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0030955 |text = potassium ion binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{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 = 3752
    | Hs_Ensembl = ENSG00000171385
    | Hs_RefseqProtein = NP_004971
    | Hs_RefseqmRNA = NM_004980
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 112114807
    | Hs_GenLoc_end = 112333300
    | Hs_Uniprot = Q9UK17
    | Mm_EntrezGene = 56543
    | Mm_Ensembl = ENSMUSG00000040896
    | Mm_RefseqmRNA = NM_001039347
    | Mm_RefseqProtein = NP_001034436
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 105580386
    | Mm_GenLoc_end = 105802058
    | Mm_Uniprot = Q9Z0V1
  }}
}}
'''Potassium voltage-gated channel, Shal-related subfamily, member 3''', also known as '''KCND3''' or '''K<sub>v</sub>4.3''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCND3 potassium voltage-gated channel, Shal-related subfamily, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3752| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Gain of function is believed to cause [[Brugada Syndrome]] although only indirectly shown by mutations in the beta subunit [[KCNE3]] which causes gain of function of K<sub>v</sub>4.3.
{{PBB_Summary
| section_title =
| summary_text = 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 member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene.<ref name="entrez">{{cite web | title = Entrez Gene: KCND3 potassium voltage-gated channel, Shal-related subfamily, member 3| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3752| accessdate = }}</ref>
}}


==See also==
==See also==
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==References==
==References==
{{reflist|2}}
{{reflist|30em}}


==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin|35em}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{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=Serôdio P, Vega-Saenz de Miera E, Rudy B |title=Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain. |journal=J. Neurophysiol. |volume=75 |issue= 5 |pages= 2174–9 |year= 1997 |pmid= 8734615 |doi= }}
*{{cite journal | author=Serôdio P, Vega-Saenz de Miera E, Rudy B |title=Cloning of a novel component of A-type K+ channels operating at subthreshold potentials with unique expression in heart and brain. |journal=J. Neurophysiol. |volume=75 |issue= 5 |pages= 2174-9 |year= 1997 |pmid= 8734615 |doi=  }}
*{{cite journal   |vauthors=Kong W, Po S, Yamagishi T, etal |title=Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing. |journal=Am. J. Physiol. |volume=275 |issue= 6 Pt 2 |pages= H1963–70 |year= 1999 |pmid= 9843794 |doi=  }}
*{{cite journal | author=Kong W, Po S, Yamagishi T, ''et al.'' |title=Isolation and characterization of the human gene encoding Ito: further diversity by alternative mRNA splicing. |journal=Am. J. Physiol. |volume=275 |issue= 6 Pt 2 |pages= H1963-70 |year= 1999 |pmid= 9843794 |doi=  }}
*{{cite journal   |vauthors=Dilks D, Ling HP, Cockett M, etal |title=Cloning and expression of the human kv4.3 potassium channel. |journal=J. Neurophysiol. |volume=81 |issue= 4 |pages= 1974–7 |year= 1999 |pmid= 10200233 |doi=  }}
*{{cite journal | author=Dilks D, Ling HP, Cockett M, ''et al.'' |title=Cloning and expression of the human kv4.3 potassium channel. |journal=J. Neurophysiol. |volume=81 |issue= 4 |pages= 1974-7 |year= 1999 |pmid= 10200233 |doi= }}
*{{cite journal   |vauthors=Isbrandt D, Leicher T, Waldschütz R, etal |title=Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA). |journal=Genomics |volume=64 |issue= 2 |pages= 144–54 |year= 2000 |pmid= 10729221 |doi= 10.1006/geno.2000.6117 }}
*{{cite journal  | author=Isbrandt D, Leicher T, Waldschütz R, ''et al.'' |title=Gene structures and expression profiles of three human KCND (Kv4) potassium channels mediating A-type currents I(TO) and I(SA). |journal=Genomics |volume=64 |issue= 2 |pages= 144-54 |year= 2000 |pmid= 10729221 |doi= 10.1006/geno.2000.6117 }}
*{{cite journal  |vauthors=Deschênes I, Tomaselli GF |title=Modulation of Kv4.3 current by accessory subunits. |journal=FEBS Lett. |volume=528 |issue= 1–3 |pages= 183–8 |year= 2002 |pmid= 12297301 |doi=10.1016/S0014-5793(02)03296-9  }}
*{{cite journal | author=Postma AV, Bezzina CR, de Vries JF, ''et al.'' |title=Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3. |journal=Hum. Genet. |volume=106 |issue= 6 |pages= 614-9 |year= 2000 |pmid= 10942109 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |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 | pmc=139241 }}
*{{cite journal  | author=Deschênes I, Tomaselli GF |title=Modulation of Kv4.3 current by accessory subunits. |journal=FEBS Lett. |volume=528 |issue= 1-3 |pages= 183-8 |year= 2002 |pmid= 12297301 |doi= }}
*{{cite journal  |vauthors=Ren X, Shand SH, Takimoto K |title=Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43564–70 |year= 2003 |pmid= 12928444 |doi= 10.1074/jbc.M302337200 }}
*{{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   |vauthors=Hatano N, Ohya S, Muraki K, etal |title=Two arginines in the cytoplasmic C-terminal domain are essential for voltage-dependent regulation of A-type K+ current in the Kv4 channel subfamily |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5450–9 |year= 2004 |pmid= 14645239 |doi= 10.1074/jbc.M302034200 }}
*{{cite journal | author=Ren X, Shand SH, Takimoto K |title=Effective association of Kv channel-interacting proteins with Kv4 channel is mediated with their unique core peptide. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43564-70 |year= 2003 |pmid= 12928444 |doi= 10.1074/jbc.M302337200 }}
*{{cite journal   |vauthors=Scannevin RH, Wang K, Jow F, etal |title=Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1 |journal=Neuron |volume=41 |issue= 4 |pages= 587–98 |year= 2004 |pmid= 14980207 |doi=10.1016/S0896-6273(04)00049-2  }}
*{{cite journal | author=Hatano N, Ohya S, Muraki K, ''et al.'' |title=Two arginines in the cytoplasmic C-terminal domain are essential for voltage-dependent regulation of A-type K+ current in the Kv4 channel subfamily. |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5450-9 |year= 2004 |pmid= 14645239 |doi= 10.1074/jbc.M302034200 }}
*{{cite journal   |vauthors=Zicha S, Xiao L, Stafford S, etal |title=Transmural expression of transient outward potassium current subunits in normal and failing canine and human hearts |journal=J. Physiol. |volume=561 |issue= Pt 3 |pages= 735–48 |year= 2005 |pmid= 15498806 |doi= 10.1113/jphysiol.2004.075861  | pmc=1665387 }}
*{{cite journal | author=Scannevin RH, Wang K, Jow F, ''et al.'' |title=Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1. |journal=Neuron |volume=41 |issue= 4 |pages= 587-98 |year= 2004 |pmid= 14980207 |doi= }}
*{{cite journal   |vauthors=Frank-Hansen R, Larsen LA, Andersen P, etal |title=Mutations in the genes KCND2 and KCND3 encoding the ion channels Kv4.2 and Kv4.3, conducting the cardiac fast transient outward current (ITO,f), are not a frequent cause of long QT syndrome |journal=Clin. Chim. Acta |volume=351 |issue= 1–2 |pages= 95–100 |year= 2005 |pmid= 15563876 |doi= 10.1016/j.cccn.2004.08.017 }}
*{{cite journal | author=Zicha S, Xiao L, Stafford S, ''et al.'' |title=Transmural expression of transient outward potassium current subunits in normal and failing canine and human hearts. |journal=J. Physiol. (Lond.) |volume=561 |issue= Pt 3 |pages= 735-48 |year= 2005 |pmid= 15498806 |doi= 10.1113/jphysiol.2004.075861 }}
*{{cite journal   |vauthors=Baltaev R, Strutz-Seebohm N, Korniychuk G, etal |title=Regulation of cardiac shal-related potassium channel Kv 4.3 by serum- and glucocorticoid-inducible kinase isoforms in Xenopus oocytes |journal=Pflugers Arch. |volume=450 |issue= 1 |pages= 26–33 |year= 2005 |pmid= 15578212 |doi= 10.1007/s00424-004-1369-z }}
*{{cite journal | author=Frank-Hansen R, Larsen LA, Andersen P, ''et al.'' |title=Mutations in the genes KCND2 and KCND3 encoding the ion channels Kv4.2 and Kv4.3, conducting the cardiac fast transient outward current (ITO,f), are not a frequent cause of long QT syndrome. |journal=Clin. Chim. Acta |volume=351 |issue= 1-2 |pages= 95-100 |year= 2005 |pmid= 15563876 |doi= 10.1016/j.cccn.2004.08.017 }}
*{{cite journal   |vauthors=Radicke S, Cotella D, Graf EM, etal |title=Expression and function of dipeptidyl-aminopeptidase-like protein 6 as a putative β-subunit of human cardiac transient outward current encoded by Kv4.3 |journal=J. Physiol. |volume=565 |issue= Pt 3 |pages= 751–6 |year= 2005 |pmid= 15890703 |doi= 10.1113/jphysiol.2005.087312 | pmc=1464568 }}
*{{cite journal | author=Baltaev R, Strutz-Seebohm N, Korniychuk G, ''et al.'' |title=Regulation of cardiac shal-related potassium channel Kv 4.3 by serum- and glucocorticoid-inducible kinase isoforms in Xenopus oocytes. |journal=Pflugers Arch. |volume=450 |issue= 1 |pages= 26-33 |year= 2005 |pmid= 15578212 |doi= 10.1007/s00424-004-1369-z }}
*{{cite journal   |vauthors=Gregory SG, Barlow KF, McLay KE, etal |title=The DNA sequence and biological annotation of human chromosome 1 |journal=Nature |volume=441 |issue= 7091 |pages= 315–21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal  | author=Radicke S, Cotella D, Graf EM, ''et al.'' |title=Expression and function of dipeptidyl-aminopeptidase-like protein 6 as a putative beta-subunit of human cardiac transient outward current encoded by Kv4.3. |journal=J. Physiol. (Lond.) |volume=565 |issue= Pt 3 |pages= 751-6 |year= 2005 |pmid= 15890703 |doi= 10.1113/jphysiol.2005.087312 }}
*{{cite journal  |vauthors=Lundby A, Olesen SP |title=KCNE3 is an inhibitory subunit of the Kv4.3 potassium channel |journal=Biochem. Biophys. Res. Commun. |volume=346 |issue= 3 |pages= 958–67 |year= 2006 |pmid= 16782062 |doi= 10.1016/j.bbrc.2006.06.004 }}
*{{cite journal | author=Gregory SG, Barlow KF, McLay KE, ''et al.'' |title=The DNA sequence and biological annotation of human chromosome 1. |journal=Nature |volume=441 |issue= 7091 |pages= 315-21 |year= 2006 |pmid= 16710414 |doi= 10.1038/nature04727 }}
*{{cite journal   |vauthors=Ahmed I, Cosen-Binker LI, Leung YM, etal |title=Modulation of the K(v)4.3 channel by syntaxin 1A |journal=Biochem. Biophys. Res. Commun. |volume=358 |issue= 3 |pages= 789–95 |year= 2007 |pmid= 17506992 |doi= 10.1016/j.bbrc.2007.04.182 }}
*{{cite journal  | author=Lundby A, Olesen SP |title=KCNE3 is an inhibitory subunit of the Kv4.3 potassium channel. |journal=Biochem. Biophys. Res. Commun. |volume=346 |issue= 3 |pages= 958-67 |year= 2006 |pmid= 16782062 |doi= 10.1016/j.bbrc.2006.06.004 }}
*{{cite journal  |vauthors=Potapova IA, Cohen IS, Doronin SV |title=Voltage-gated ion channel Kv4.3 is associated with Rap guanine nucleotide exchange factors and regulates angiotensin receptor type 1 signaling to small G-protein Rap |journal=FEBS J. |volume=274 |issue= 17 |pages= 4375–84 |year= 2007 |pmid= 17725712 |doi= 10.1111/j.1742-4658.2007.05966.x }}
*{{cite journal | author=Ahmed I, Cosen-Binker LI, Leung YM, ''et al.'' |title=Modulation of the K(v)4.3 channel by syntaxin 1A. |journal=Biochem. Biophys. Res. Commun. |volume=358 |issue= 3 |pages= 789-95 |year= 2007 |pmid= 17506992 |doi= 10.1016/j.bbrc.2007.04.182 }}
*{{cite journal  | author=Potapova IA, Cohen IS, Doronin SV |title=Voltage-gated ion channel Kv4.3 is associated with Rap guanine nucleotide exchange factors and regulates angiotensin receptor type 1 signaling to small G-protein Rap. |journal=FEBS J. |volume=274 |issue= 17 |pages= 4375-84 |year= 2007 |pmid= 17725712 |doi= 10.1111/j.1742-4658.2007.05966.x }}
}}
}}
{{refend}}
{{refend}}


== External links ==
==External links==
* [https://www.ncbi.nlm.nih.gov/books/NBK1517/  GeneReviews/NIH/NCBI/UW entry on Brugada syndrome]
* {{MeshName|Kv4.3+Potassium+Channel}}
* {{MeshName|Kv4.3+Potassium+Channel}}
{{PDB Gallery|geneid=3752}}
{{Ion channels|g3}}
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Revision as of 06:13, 2 September 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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Wikidata
View/Edit Human

Potassium voltage-gated channel subfamily D member 3 also known as Kv4.3 is a protein that in humans is encoded by the KCND3 gene.[1][2][3] It contributes to the cardiac transient outward potassium current (Ito1), the main contributing current to the repolarizing phase 1 of the cardiac action potential.[4]

Function

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).

Kv4.3 is 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 member includes two isoforms with different sizes, which are encoded by alternatively spliced transcript variants of this gene.[3]

Clinical significance

Gain of function is believed to cause Brugada Syndrome although only indirectly shown by mutations in the beta subunit KCNE3 which causes gain of function of Kv4.3.

See also

References

  1. ↑ Postma AV, Bezzina CR, de Vries JF, Wilde AA, Moorman AF, Mannens MM (Aug 2000). "Genomic organisation and chromosomal localisation of two members of the KCND ion channel family, KCND2 and KCND3". Hum Genet. 106 (6): 614–9. doi:10.1007/s004390050033. PMID 10942109.
  2. ↑ 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.
  3. ↑ 3.0 3.1 "Entrez Gene: KCND3 potassium voltage-gated channel, Shal-related subfamily, member 3".
  4. ↑ Oudit GY, Kassiri Z, Sah R, Ramirez RJ, Zobel C, Backx PH (May 2001). "The molecular physiology of the cardiac transient outward potassium current (I(to)) in normal and diseased myocardium". J. Mol. Cell. Cardiol. 33 (5): 851–72. doi:10.1006/jmcc.2001.1376. PMID 11343410.

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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