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{{Infobox_gene}}
{{PBB_Controls
'''Potassium voltage-gated channel subfamily D member 2''' is a [[protein]] that in humans is encoded by the ''KCND2'' [[gene]].<ref name="pmid10551270">{{cite journal |vauthors=Zhu XR, Wulf A, Schwarz M, Isbrandt D, Pongs O | title = Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current | journal = Receptors Channels | volume = 6 | issue = 5 | pages = 387–400 |date=December 1999 | pmid = 10551270 | pmc = | doi = }}</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=December 2005 | pmid = 16382104 | pmc =  | doi = 10.1124/pr.57.4.10 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3751| accessdate = }}</ref> 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=851–872 |date=May 2001 |pmid=11343410 |doi=10.1006/jmcc.2001.1376 |url=}}</ref>
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{{GNF_Protein_box
| image = PBB_Protein_KCND2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1nn7.
| PDB = {{PDB2|1nn7}}, {{PDB2|1s6c}}
| Name = Potassium voltage-gated channel, Shal-related subfamily, member 2
| HGNCid = 6238
| Symbol = KCND2
| AltSymbols =; KIAA1044; KV4.2; MGC119702; MGC119703; RK5
| OMIM = 605410
| ECnumber = 
| Homologene = 40828
| MGIid = 102663
| Function = {{GNF_GO|id=GO:0005249 |text = voltage-gated 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:0009986 |text = cell surface}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0043197 |text = dendritic spine}}
  | Process = {{GNF_GO|id=GO:0001508 |text = regulation of action potential}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006813 |text = potassium ion transport}} {{GNF_GO|id=GO:0007268 |text = synaptic transmission}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 3751
    | Hs_Ensembl = ENSG00000184408
    | Hs_RefseqProtein = NP_036413
    | Hs_RefseqmRNA = NM_012281
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 7
    | Hs_GenLoc_start = 119701923
    | Hs_GenLoc_end = 120175148
    | Hs_Uniprot = Q9NZV8
    | Mm_EntrezGene = 16508
    | Mm_Ensembl = ENSMUSG00000060882
    | Mm_RefseqmRNA = NM_019697
    | Mm_RefseqProtein = NP_062671
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 6
    | Mm_GenLoc_start = 21166300
    | Mm_GenLoc_end = 21677343
    | Mm_Uniprot = Q9Z0V2
  }}
}}
'''Potassium voltage-gated channel, Shal-related subfamily, member 2''', also known as '''KCND2''' or '''K<sub>v</sub>4.2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3751| accessdate = }}</ref>


==Description==
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{{PBB_Summary
{{PBB_Summary
| section_title =  
| 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 mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.<ref name="entrez">{{cite web | title = Entrez Gene: KCND2 potassium voltage-gated channel, Shal-related subfamily, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=3751| accessdate = }}</ref>
| 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 mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.<ref name="entrez" />
}}
}}
==Interactions==
KCND2 has been shown to [[Protein-protein interaction|interact]] with [[FLNC (gene)|FLNC]].<ref name=pmid11102480>{{cite journal |last=Petrecca |first=K |authorlink= |author2=Miller D M |author3=Shrier A  |date=December 2000  |title=Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin |journal=J. Neurosci. |volume=20 |issue=23 |pages=8736–44 |publisher= |location = UNITED STATES| issn = | pmid = 11102480 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>


==See also==
==See also==
Line 57: Line 16:


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


==Further reading==
==Further reading==
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{{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  | author=Kong W |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= |name-list-format=vanc| author2=Po S | author3=Yamagishi T | display-authors=| last4=Ashen  | first4=MD  | last5=Stetten  | first5=| last6=Tomaselli  | first6=GF }}
*{{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  | author=Kikuno R |title=Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro |journal=DNA Res. |volume=6 |issue= 3 |pages= 197–205 |year= 1999 |pmid= 10470851 |doi=10.1093/dnares/6.3.197 |name-list-format=vanc| author2=Nagase T  | author3=Ishikawa K  | display-authors=3  | last4=Hirosawa  | first4=| last5=Miyajima  | first5=| last6=Tanaka  | first6=| last7=Kotani | first7=H | last8=Nomura  | first8=| last9=Ohara  | first9=O }}
*{{cite journal  | author=Kikuno R, Nagase T, Ishikawa K, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. |journal=DNA Res. |volume=6 |issue= 3 |pages= 197-205 |year= 1999 |pmid= 10470851 |doi= }}
*{{cite journal  |vauthors=Kurschner C, Yuzaki M |title=Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein |journal=J. Neurosci. |volume=19 |issue= 18 |pages= 7770–80 |year= 1999 |pmid= 10479680 |doi= }}
*{{cite journal | author=Kurschner C, Yuzaki M |title=Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein. |journal=J. Neurosci. |volume=19 |issue= 18 |pages= 7770-80 |year= 1999 |pmid= 10479680 |doi}}
*{{cite journal  | author=An WF |title=Modulation of A-type potassium channels by a family of calcium sensors |journal=Nature |volume=403 |issue= 6769 |pages= 553–556 |year= 2000 |pmid= 10676964 |doi= 10.1038/35000592  |name-list-format=vanc| author2=Bowlby MR | author3=Betty M  | display-authors=3  | last4=Cao  | first4=Jie  | last5=Ling  | first5=Huai-Ping  | last6=Mendoza  | first6=Grace  | last7=Hinson  | first7=Joseph W.  | last8=Mattsson  | first8=Karen I.  | last9=Strassle | first9=Brian W. }}
*{{cite journal | author=Zhu XR, Wulf A, Schwarz M, ''et al.'' |title=Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current. |journal=Recept. Channels |volume=6 |issue= 5 |pages= 387-400 |year= 1999 |pmid= 10551270 |doi=  }}
*{{cite journal  | author=Isbrandt D |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= 144–154 |year= 2000 |pmid= 10729221 |doi= 10.1006/geno.2000.6117 |name-list-format=vanc| author2=Leicher T  | author3=Waldschütz R  | display-authors=3  | last4=Zhu  | first4=| last5=Luhmann  | first5=| last6=Michel  | first6=U  | last7=Sauter  | first7=K  | last8=Pongs  | first8=O }}
*{{cite journal  | author=An WF, Bowlby MR, Betty M, ''et al.'' |title=Modulation of A-type potassium channels by a family of calcium sensors. |journal=Nature |volume=403 |issue= 6769 |pages= 553-6 |year= 2000 |pmid= 10676964 |doi= 10.1038/35000592 }}
*{{cite journal  | author=Postma AV |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= 614–619 |year= 2000 |pmid= 10942109 |doi=10.1007/s004390050033  |name-list-format=vanc| author2=Bezzina CR  | author3=de Vries JF  | display-authors=| last4=Wilde  | first4=Arthur A. M.  | last5=Moorman  | first5=Antoon F. M.  | last6=Mannens  | first6=Marcel M. A. M. }}
*{{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=Petrecca K, Miller DM, Shrier A |title=Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin |journal=J. Neurosci. |volume=20 |issue= 23 |pages= 8736–44 |year= 2001 |pmid= 11102480 |doi=  }}
*{{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  | author=Bähring R |title=Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23888–23894 |year= 2001 |pmid= 11287421 |doi= 10.1074/jbc.M101320200 |name-list-format=vanc| author2=Dannenberg J | author3=Peters HC  | display-authors=3  | last4=Leicher  | first4=| last5=Pongs  | first5=| last6=Isbrandt  | first6=D }}
*{{cite journal  | author=Petrecca K, Miller DM, Shrier A |title=Localization and enhanced current density of the Kv4.2 potassium channel by interaction with the actin-binding protein filamin. |journal=J. Neurosci. |volume=20 |issue= 23 |pages= 8736-44 |year= 2001 |pmid= 11102480 |doi= }}
*{{cite journal  | author=Nakamura TY |title=A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 22 |pages= 12808–12813 |year= 2001 |pmid= 11606724 |doi= 10.1073/pnas.221168498  | pmc=60135 |name-list-format=vanc| author2=Pountney DJ  | author3=Ozaita A  | display-authors=| last4=Nandi  | first4=| last5=Ueda  | first5=| last6=Rudy  | first6=B  | last7=Coetzee  | first7=WA }}
*{{cite journal | author=Bähring R, Dannenberg J, Peters HC, ''et al.'' |title=Conserved Kv4 N-terminal domain critical for effects of Kv channel-interacting protein 2.2 on channel expression and gating. |journal=J. Biol. Chem. |volume=276 |issue= 26 |pages= 23888-94 |year= 2001 |pmid= 11287421 |doi= 10.1074/jbc.M101320200 }}
*{{cite journal  | author=Morohashi Y |title=Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4 |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14965–14975 |year= 2002 |pmid= 11847232 |doi= 10.1074/jbc.M200897200 |name-list-format=vanc| author2=Hatano N  | author3=Ohya S  | display-authors=3  | last4=Takikawa  | first4=| last5=Watabiki  | first5=| last6=Takasugi  | first6=N  | last7=Imaizumi  | first7=Y  | last8=Tomita  | first8=T  | last9=Iwatsubo  | first9=T }}
*{{cite journal  | author=Nakamura TY, Pountney DJ, Ozaita A, ''et al.'' |title=A role for frequenin, a Ca2+-binding protein, as a regulator of Kv4 K+-currents. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 22 |pages= 12808-13 |year= 2001 |pmid= 11606724 |doi= 10.1073/pnas.221168498 }}
*{{cite journal  |vauthors=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= 529–537 |year= 2002 |pmid= 12435606 |doi=10.1016/S0014-5793(02)03572-X  }}
*{{cite journal  | author=Morohashi Y, Hatano N, Ohya S, ''et al.'' |title=Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand protein interacting with presenilin 2 and voltage-gated potassium channel subunit Kv4. |journal=J. Biol. Chem. |volume=277 |issue= 17 |pages= 14965-75 |year= 2002 |pmid= 11847232 |doi= 10.1074/jbc.M200897200 }}
*{{cite journal  | author=Schrader LA |title=PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex |journal=J. Neurosci. |volume=22 |issue= 23 |pages= 10123–33 |year= 2002 |pmid= 12451113 |doi=  |name-list-format=vanc| author2=Anderson AE  | author3=Mayne A  | display-authors=3  | last4=Pfaffinger  | first4=PJ  | last5=Sweatt  | first5=JD  }}
*{{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 |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= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899  | pmc=139241  |name-list-format=vanc| author2=Feingold EA  | author3=Grouse LH  | display-authors=3  | last4=Derge  | first4=JG  | last5=Klausner  | first5=RD  | last6=Collins  | first6=FS  | last7=Wagner  | first7=L  | last8=Shenmen  | first8=CM  | last9=Schuler  | first9=GD }}
*{{cite journal  | author=Schrader LA, Anderson AE, Mayne A, ''et al.'' |title=PKA modulation of Kv4.2-encoded A-type potassium channels requires formation of a supramolecular complex. |journal=J. Neurosci. |volume=22 |issue= 23 |pages= 10123-33 |year= 2002 |pmid= 12451113 |doi=  }}
*{{cite journal  | author=Shin BK |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607–7616 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200  |name-list-format=vanc| author2=Wang H  | author3=Yim AM  | display-authors=3  | last4=Le Naour  | first4=F  | last5=Brichory  | first5=F  | last6=Jang  | first6=JH  | last7=Zhao  | first7=R  | last8=Puravs  | first8=E  | last9=Tra  | first9=J }}
*{{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=Scherer SW |title=Human chromosome 7: DNA sequence and biology |journal=Science |volume=300 |issue= 5620 |pages= 767–772 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423  | pmc=2882961  |name-list-format=vanc| author2=Cheung J  | author3=MacDonald JR  | display-authors=3  | last4=Osborne  | first4=LR  | last5=Nakabayashi  | first5=K  | last6=Herbrick  | first6=JA  | last7=Carson  | first7=AR  | last8=Parker-Katiraee  | first8=L  | last9=Skaug  | first9=J }}
*{{cite journal  | author=Shin BK, Wang H, Yim AM, ''et al.'' |title=Global profiling of the cell surface proteome of cancer cells uncovers an abundance of proteins with chaperone function. |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7607-16 |year= 2003 |pmid= 12493773 |doi= 10.1074/jbc.M210455200 }}
*{{cite journal  | author=Hillier LW |title=The DNA sequence of human chromosome 7 |journal=Nature |volume=424 |issue= 6945 |pages= 157–164 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782  |name-list-format=vanc| author2=Fulton RS  | author3=Fulton LA  | display-authors=3  | last4=Graves  | first4=Tina A.  | last5=Pepin  | first5=Kymberlie H.  | last6=Wagner-Mcpherson  | first6=Caryn  | last7=Layman  | first7=Dan  | last8=Maas  | first8=Jason  | last9=Jaeger  | first9=Sara }}
*{{cite journal | author=Scherer SW, Cheung J, MacDonald JR, ''et al.'' |title=Human chromosome 7: DNA sequence and biology. |journal=Science |volume=300 |issue= 5620 |pages= 767-72 |year= 2003 |pmid= 12690205 |doi= 10.1126/science.1083423 }}
*{{cite journal  |vauthors=Wong W, Schlichter LC |title=Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95 |journal=J. Biol. Chem. |volume=279 |issue= 1 |pages= 444–452 |year= 2004 |pmid= 14559911 |doi= 10.1074/jbc.M304675200 }}
*{{cite journal  | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
*{{cite journal  | author=Kim LA |title=Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2 |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5549–5554 |year= 2004 |pmid= 14623880 |doi= 10.1074/jbc.M311332200 |name-list-format=vanc| author2=Furst J  | author3=Butler MH  | display-authors=3  | last4=Xu  | first4=S  | last5=Grigorieff  | first5=N  | last6=Goldstein  | first6=SA }}
*{{cite journal | author=Wong W, Schlichter LC |title=Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95. |journal=J. Biol. Chem. |volume=279 |issue= 1 |pages= 444-52 |year= 2004 |pmid= 14559911 |doi= 10.1074/jbc.M304675200 }}
*{{cite journal  | author=Kim LA, Furst J, Butler MH, ''et al.'' |title=Ito channels are octomeric complexes with four subunits of each Kv4.2 and K+ channel-interacting protein 2. |journal=J. Biol. Chem. |volume=279 |issue= 7 |pages= 5549-54 |year= 2004 |pmid= 14623880 |doi= 10.1074/jbc.M311332200 }}
}}
}}
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* {{MeshName|KCND2+protein,+human}}
* {{MeshName|KCND2+protein,+human}}


{{membrane-protein-stub}}
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{{Ion channels|g3}}
 
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Revision as of 06:13, 2 September 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

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n/a

RefSeq (protein)

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

Potassium voltage-gated channel subfamily D member 2 is a protein that in humans is encoded by the KCND2 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]

Description

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 mediates a rapidly inactivating, A-type outward potassium current which is not under the control of the N terminus as it is in Shaker channels.[3]

Interactions

KCND2 has been shown to interact with FLNC.[5]

See also

References

  1. Zhu XR, Wulf A, Schwarz M, Isbrandt D, Pongs O (December 1999). "Characterization of human Kv4.2 mediating a rapidly-inactivating transient voltage-sensitive K+ current". Receptors Channels. 6 (5): 387–400. PMID 10551270.
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Further reading

External links

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