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Potassium voltage-gated channel subfamily D member 2 (RK5) (Shal1) (Voltage-gated potassium channel subunit Kv4.2)

 KCND2_RAT               Reviewed;         630 AA.
Q63881; Q00090; Q99249;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
29-SEP-2021, entry version 173.
RecName: Full=Potassium voltage-gated channel subfamily D member 2;
AltName: Full=RK5 {ECO:0000303|PubMed:1705709, ECO:0000303|PubMed:1722463};
AltName: Full=Shal1 {ECO:0000303|PubMed:1840649};
AltName: Full=Voltage-gated potassium channel subunit Kv4.2 {ECO:0000303|PubMed:9093524};
Name=Kcnd2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Hippocampus;
PubMed=1840649; DOI=10.1016/0896-6273(91)90299-f;
Baldwin T.J., Tsaur M.-L., Lopez G.A., Jan Y.N., Jan L.Y.;
"Characterization of a mammalian cDNA for an inactivating voltage-sensitive
K+ channel.";
Neuron 7:471-483(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Heart;
PubMed=1705709; DOI=10.1073/pnas.88.5.1798;
Roberds S.L., Tamkun M.M.;
"Cloning and tissue-specific expression of five voltage-gated potassium
channel cDNAs expressed in rat heart.";
Proc. Natl. Acad. Sci. U.S.A. 88:1798-1802(1991).
[3]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=1722463; DOI=10.1016/0014-5793(91)81420-d;
Blair T.A., Roberds S.L., Tamkun M.M., Hartshorne R.P.;
"Functional characterization of RK5, a voltage-gated K+ channel cloned from
the rat cardiovascular system.";
FEBS Lett. 295:211-213(1991).
[4]
FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=9093524; DOI=10.1016/s0008-6363(96)00221-0;
Yeola S.W., Snyders D.J.;
"Electrophysiological and pharmacological correspondence between Kv4.2
current and rat cardiac transient outward current.";
Cardiovasc. Res. 33:540-547(1997).
[5]
FUNCTION, ACTIVITY REGULATION, AND SUBCELLULAR LOCATION.
PubMed=9058605;
Sanguinetti M.C., Johnson J.H., Hammerland L.G., Kelbaugh P.R.,
Volkmann R.A., Saccomano N.A., Mueller A.L.;
"Heteropodatoxins: peptides isolated from spider venom that block Kv4.2
potassium channels.";
Mol. Pharmacol. 51:491-498(1997).
[6]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9070739; DOI=10.1016/s0306-4522(96)00561-1;
Alonso G., Widmer H.;
"Clustering of KV4.2 potassium channels in postsynaptic membrane of rat
supraoptic neurons: an ultrastructural study.";
Neuroscience 77:617-621(1997).
[7]
PHOSPHORYLATION AT THR-38 AND SER-552 BY PKACA.
PubMed=10681507; DOI=10.1074/jbc.275.8.5337;
Anderson A.E., Adams J.P., Qian Y., Cook R.G., Pfaffinger P.J.,
Sweatt J.D.;
"Kv4.2 phosphorylation by cyclic AMP-dependent protein kinase.";
J. Biol. Chem. 275:5337-5346(2000).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10860776; DOI=10.1006/jmcc.2000.1172;
Takeuchi S., Takagishi Y., Yasui K., Murata Y., Toyama J., Kodama I.;
"Voltage-gated K(+)Channel, Kv4.2, localizes predominantly to the
transverse-axial tubular system of the rat myocyte.";
J. Mol. Cell. Cardiol. 32:1361-1369(2000).
[9]
PHOSPHORYLATION AT THR-602; THR-607 AND SER-616.
PubMed=11080179; DOI=10.1046/j.1471-4159.2000.0752277.x;
Adams J.P., Anderson A.E., Varga A.W., Dineley K.T., Cook R.G.,
Pfaffinger P.J., Sweatt J.D.;
"The A-type potassium channel Kv4.2 is a substrate for the mitogen-
activated protein kinase ERK.";
J. Neurochem. 75:2277-2287(2000).
[10]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INTERACTION WITH FILAMIN.
PubMed=11102480; DOI=10.1523/jneurosci.20-23-08736.2000;
Petrecca K., Miller D.M., Shrier A.;
"Localization and enhanced current density of the Kv4.2 potassium channel
by interaction with the actin-binding protein filamin.";
J. Neurosci. 20:8736-8744(2000).
[11]
INTERACTION WITH KCNIP1; KCNIP2 AND KCNIP3, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=10676964; DOI=10.1038/35000592;
An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
"Modulation of A-type potassium channels by a family of calcium sensors.";
Nature 403:553-556(2000).
[12]
INTERACTION WITH KCNIP3, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF
SER-552, PHOSPHORYLATION AT SER-552, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=12451113; DOI=10.1523/jneurosci.22-23-10123.2002;
Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.;
"PKA modulation of Kv4.2-encoded A-type potassium channels requires
formation of a supramolecular complex.";
J. Neurosci. 22:10123-10133(2002).
[13]
INTERACTION WITH KCNIP4, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11847232; DOI=10.1074/jbc.m200897200;
Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N.,
Imaizumi Y., Tomita T., Iwatsubo T.;
"Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand
protein interacting with presenilin 2 and voltage-gated potassium channel
subunit Kv4.";
J. Biol. Chem. 277:14965-14975(2002).
[14]
MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4, AND SUBCELLULAR
LOCATION.
PubMed=11923279; DOI=10.1074/jbc.m109412200;
Wong W., Newell E.W., Jugloff D.G.M., Jones O.T., Schlichter L.C.;
"Cell surface targeting and clustering interactions between heterologously
expressed PSD-95 and the Shal voltage-gated potassium channel, Kv4.2.";
J. Biol. Chem. 277:20423-20430(2002).
[15]
INTERACTION WITH KCNIP4.
PubMed=11805342; DOI=10.1073/pnas.022509299;
Holmqvist M.H., Cao J., Hernandez-Pineda R., Jacobson M.D., Carroll K.I.,
Sung M.A., Betty M., Ge P., Gilbride K.J., Brown M.E., Jurman M.E.,
Lawson D., Silos-Santiago I., Xie Y., Covarrubias M., Rhodes K.J.,
Distefano P.S., An W.F.;
"Elimination of fast inactivation in Kv4 A-type potassium channels by an
auxiliary subunit domain.";
Proc. Natl. Acad. Sci. U.S.A. 99:1035-1040(2002).
[16]
PHOSPHORYLATION AT SER-552, AND SUBCELLULAR LOCATION.
PubMed=12829703; DOI=10.1074/jbc.m306142200;
Shibata R., Misonou H., Campomanes C.R., Anderson A.E., Schrader L.A.,
Doliveira L.C., Carroll K.I., Sweatt J.D., Rhodes K.J., Trimmer J.S.;
"A fundamental role for KChIPs in determining the molecular properties and
trafficking of Kv4.2 potassium channels.";
J. Biol. Chem. 278:36445-36454(2003).
[17]
SUBCELLULAR LOCATION, DENDRITIC TARGETING REGION, MUTAGENESIS OF
481-LEU--LEU-482, AND FUNCTION.
PubMed=12592409; DOI=10.1038/nn1020;
Rivera J.F., Ahmad S., Quick M.W., Liman E.R., Arnold D.B.;
"An evolutionarily conserved dileucine motif in Shal K+ channels mediates
dendritic targeting.";
Nat. Neurosci. 6:243-250(2003).
[18]
INTERACTION WITH DPP6.
PubMed=12575952; DOI=10.1016/s0896-6273(02)01185-6;
Nadal M.S., Ozaita A., Amarillo Y., Vega-Saenz de Miera E., Ma Y., Mo W.,
Goldberg E.M., Misumi Y., Ikehara Y., Neubert T.A., Rudy B.;
"The CD26-related dipeptidyl aminopeptidase-like protein DPPX is a critical
component of neuronal A-type K+ channels.";
Neuron 37:449-461(2003).
[19]
SUBUNIT, ZINC-BINDING, SUBCELLULAR LOCATION, FUNCTION, AND MUTAGENESIS OF
HIS-105; CYS-111; CYS-132 AND CYS-133.
PubMed=12754210; DOI=10.1074/jbc.m304268200;
Strang C., Kunjilwar K., DeRubeis D., Peterson D., Pfaffinger P.J.;
"The role of Zn2+ in Shal voltage-gated potassium channel formation.";
J. Biol. Chem. 278:31361-31371(2003).
[20]
MUTAGENESIS OF 627-VAL--LEU-630, INTERACTION WITH DLG4, AND SUBCELLULAR
LOCATION.
PubMed=14559911; DOI=10.1074/jbc.m304675200;
Wong W., Schlichter L.C.;
"Differential recruitment of Kv1.4 and Kv4.2 to lipid rafts by PSD-95.";
J. Biol. Chem. 279:444-452(2004).
[21]
FUNCTION, INTERACTION WITH KCNIP3, AND SUBCELLULAR LOCATION.
PubMed=15485870; DOI=10.1074/jbc.m409721200;
Kunjilwar K., Strang C., DeRubeis D., Pfaffinger P.J.;
"KChIP3 rescues the functional expression of Shal channel tetramerization
mutants.";
J. Biol. Chem. 279:54542-54551(2004).
[22]
INTERACTION WITH KCNIP1 AND KCNIP3.
PubMed=15356203; DOI=10.1523/jneurosci.0776-04.2004;
Rhodes K.J., Carroll K.I., Sung M.A., Doliveira L.C., Monaghan M.M.,
Burke S.L., Strassle B.W., Buchwalder L., Menegola M., Cao J., An W.F.,
Trimmer J.S.;
"KChIPs and Kv4 alpha subunits as integral components of A-type potassium
channels in mammalian brain.";
J. Neurosci. 24:7903-7915(2004).
[23]
INTERACTION WITH KCNIP1, AND MUTAGENESIS OF 7-ALA--PHE-11; GLU-71; ASP-73;
PHE-74 AND GLU-79.
PubMed=14980207; DOI=10.1016/s0896-6273(04)00049-2;
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W.,
Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M.,
Stahl M., Malakian K., Somers W., Mosyak L., Bowlby M.R., Chanda P.,
Rhodes K.J.;
"Two N-terminal domains of Kv4 K(+) channels regulate binding to and
modulation by KChIP1.";
Neuron 41:587-598(2004).
[24]
DOMAIN, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KCNIP2.
PubMed=15452711; DOI=10.1007/s00424-004-1328-8;
Pourrier M., Herrera D., Caballero R., Schram G., Wang Z., Nattel S.;
"The Kv4.2 N-terminal restores fast inactivation and confers KChlP2
modulatory effects on N-terminal-deleted Kv1.4 channels.";
Pflugers Arch. 449:235-247(2004).
[25]
REVIEW.
PubMed=15858231; DOI=10.1385/cbb:42:2:167;
Cox R.H.;
"Molecular determinants of voltage-gated potassium currents in vascular
smooth muscle.";
Cell Biochem. Biophys. 42:167-195(2005).
[26]
INTERACTION WITH DPP6 AND DPP10, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15671030; DOI=10.1074/jbc.m410613200;
Zagha E., Ozaita A., Chang S.Y., Nadal M.S., Lin U., Saganich M.J.,
McCormack T., Akinsanya K.O., Qi S.Y., Rudy B.;
"DPP10 modulates Kv4-mediated A-type potassium channels.";
J. Biol. Chem. 280:18853-18861(2005).
[27]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15736227; DOI=10.1002/cne.20443;
Strassle B.W., Menegola M., Rhodes K.J., Trimmer J.S.;
"Light and electron microscopic analysis of KChIP and Kv4 localization in
rat cerebellar granule cells.";
J. Comp. Neurol. 484:144-155(2005).
[28]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16207878; DOI=10.1523/jneurosci.2858-05.2005;
Yuan W., Burkhalter A., Nerbonne J.M.;
"Functional role of the fast transient outward K+ current IA in pyramidal
neurons in (rat) primary visual cortex.";
J. Neurosci. 25:9185-9194(2005).
[29]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
PubMed=16123112; DOI=10.1113/jphysiol.2005.087858;
Jerng H.H., Kunjilwar K., Pfaffinger P.J.;
"Multiprotein assembly of Kv4.2, KChIP3 and DPP10 produces ternary channel
complexes with ISA-like properties.";
J. Physiol. (Lond.) 568:767-788(2005).
[30]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNIP2, AND DOMAIN.
PubMed=16820361; DOI=10.1074/jbc.m604843200;
Han W., Nattel S., Noguchi T., Shrier A.;
"C-terminal domain of Kv4.2 and associated KChIP2 interactions regulate
functional expression and gating of Kv4.2.";
J. Biol. Chem. 281:27134-27144(2006).
[31]
FUNCTION.
PubMed=17026528; DOI=10.1111/j.1471-4159.2006.04185.x;
Lauver A., Yuan L.L., Jeromin A., Nadin B.M., Rodriguez J.J., Davies H.A.,
Stewart M.G., Wu G.Y., Pfaffinger P.J.;
"Manipulating Kv4.2 identifies a specific component of hippocampal
pyramidal neuron A-current that depends upon Kv4.2 expression.";
J. Neurochem. 99:1207-1223(2006).
[32]
REVIEW.
PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
Baranauskas G.;
"Ionic channel function in action potential generation: current
perspective.";
Mol. Neurobiol. 35:129-150(2007).
[33]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17582333; DOI=10.1016/j.neuron.2007.05.026;
Kim J., Jung S.C., Clemens A.M., Petralia R.S., Hoffman D.A.;
"Regulation of dendritic excitability by activity-dependent trafficking of
the A-type K+ channel subunit Kv4.2 in hippocampal neurons.";
Neuron 54:933-947(2007).
[34]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=18371079; DOI=10.1111/j.1460-9568.2008.06141.x;
Kollo M., Holderith N., Antal M., Nusser Z.;
"Unique clustering of A-type potassium channels on different cell types of
the main olfactory bulb.";
Eur. J. Neurosci. 27:1686-1699(2008).
[35]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-552, AND MUTAGENESIS OF
SER-552.
PubMed=18650329; DOI=10.1523/jneurosci.1951-08.2008;
Hammond R.S., Lin L., Sidorov M.S., Wikenheiser A.M., Hoffman D.A.;
"Protein kinase A mediates activity-dependent Kv4.2 channel trafficking.";
J. Neurosci. 28:7513-7519(2008).
[36]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MISCELLANEOUS.
PubMed=18276729; DOI=10.1113/jphysiol.2007.150540;
Amarillo Y., De Santiago-Castillo J.A., Dougherty K., Maffie J., Kwon E.,
Covarrubias M., Rudy B.;
"Ternary Kv4.2 channels recapitulate voltage-dependent inactivation
kinetics of A-type K+ channels in cerebellar granule neurons.";
J. Physiol. (Lond.) 586:2093-2106(2008).
[37]
REVIEW.
PubMed=18357523; DOI=10.1007/s11064-008-9650-8;
Covarrubias M., Bhattacharji A., De Santiago-Castillo J.A., Dougherty K.,
Kaulin Y.A., Na-Phuket T.R., Wang G.;
"The neuronal Kv4 channel complex.";
Neurochem. Res. 33:1558-1567(2008).
[38]
SUBCELLULAR LOCATION, INTERACTION WITH DPP6 AND KCNIP2, PHOSPHORYLATION AT
SER-548; SER-552; SER-572 AND SER-575, IDENTIFICATION BY MASS SPECTROMETRY,
AND MUTAGENESIS OF SER-552.
PubMed=19441798; DOI=10.1021/bi802316m;
Seikel E., Trimmer J.S.;
"Convergent modulation of Kv4.2 channel alpha subunits by structurally
distinct DPPX and KChIP auxiliary subunits.";
Biochemistry 48:5721-5730(2009).
[39]
FUNCTION, SUBUNIT, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19901547; DOI=10.4161/chan.3.6.10216;
Jerng H.H., Dougherty K., Covarrubias M., Pfaffinger P.J.;
"A novel N-terminal motif of dipeptidyl peptidase-like proteins produces
rapid inactivation of KV4.2 channels by a pore-blocking mechanism.";
Channels 3:448-461(2009).
[40]
INTERACTION WITH DLG1.
PubMed=19213956; DOI=10.1161/circresaha.108.191007;
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
Coulombe A., Jeromin A., Hatem S.N.;
"Kv4 potassium channels form a tripartite complex with the anchoring
protein SAP97 and CaMKII in cardiac myocytes.";
Circ. Res. 104:758-769(2009).
[41]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=19279261; DOI=10.1523/jneurosci.4767-08.2009;
Kaulin Y.A., De Santiago-Castillo J.A., Rocha C.A., Nadal M.S., Rudy B.,
Covarrubias M.;
"The dipeptidyl-peptidase-like protein DPP6 determines the unitary
conductance of neuronal Kv4.2 channels.";
J. Neurosci. 29:3242-3251(2009).
[42]
SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH PKA; CAV3; AKAP6 AND KCND3,
AND TISSUE SPECIFICITY.
PubMed=20224290; DOI=10.4161/chan.4.3.11479;
Alday A., Urrutia J., Gallego M., Casis O.;
"Alpha1-adrenoceptors regulate only the caveolae-located subpopulation of
cardiac K(V)4 channels.";
Channels 4:168-178(2010).
[43]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=20045463; DOI=10.1016/j.mcn.2009.12.005;
Lin L., Sun W., Wikenheiser A.M., Kung F., Hoffman D.A.;
"KChIP4a regulates Kv4.2 channel trafficking through PKA phosphorylation.";
Mol. Cell. Neurosci. 43:315-325(2010).
[44]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22098631; DOI=10.1111/j.1460-9568.2011.07907.x;
Kerti K., Lorincz A., Nusser Z.;
"Unique somato-dendritic distribution pattern of Kv4.2 channels on
hippocampal CA1 pyramidal cells.";
Eur. J. Neurosci. 35:66-75(2012).
[45]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-552; SER-572 AND
SER-575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14 different rat
organs and tissues.";
Nat. Commun. 3:876-876(2012).
[46]
INDUCTION BY HYPOXIA, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=25352783; DOI=10.3389/fncel.2014.00329;
Liu Y.Q., Huang W.X., Sanchez R.M., Min J.W., Hu J.J., He X.H., Peng B.W.;
"Regulation of Kv4.2 A-type potassium channels in HEK-293 cells by
hypoxia.";
Front. Cell. Neurosci. 8:329-329(2014).
[47]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24037673; DOI=10.1002/cne.23435;
Rainnie D.G., Hazra R., Dabrowska J., Guo J.D., Li C.C., Dewitt S.,
Muly E.C.;
"Distribution and functional expression of Kv4 family alpha subunits and
associated KChIP beta subunits in the bed nucleus of the stria
terminalis.";
J. Comp. Neurol. 522:609-625(2014).
[48]
INTERACTION WITH KCNIP4.
PubMed=24811166; DOI=10.1074/jbc.m114.563452;
Kitazawa M., Kubo Y., Nakajo K.;
"The stoichiometry and biophysical properties of the Kv4 potassium channel
complex with K+ channel-interacting protein (KChIP) subunits are variable,
depending on the relative expression level.";
J. Biol. Chem. 289:17597-17609(2014).
[49]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24793047; DOI=10.1007/s00424-014-1521-3;
Rudakova E., Wagner M., Frank M., Volk T.;
"Localization of Kv4.2 and KChIP2 in lipid rafts and modulation of outward
K(+) currents by membrane cholesterol content in rat left ventricular
myocytes.";
Pflugers Arch. 467:299-309(2015).
[50]
FUNCTION, PHOSPHORYLATION AT SER-438, AND SUBCELLULAR LOCATION.
PubMed=24404150; DOI=10.1371/journal.pone.0084086;
Labno A., Warrier A., Wang S., Zhang X.;
"Local plasticity of dendritic excitability can be autonomous of synaptic
plasticity and regulated by activity-based phosphorylation of Kv4.2.";
PLoS ONE 9:E84086-E84086(2014).
[51]
SPECIFIC INHIBITION BY SCORPION TOXIN.
PubMed=27346450; DOI=10.1016/j.toxicon.2016.06.014;
Pucca M.B., Cerni F.A., Cordeiro F.A., Peigneur S., Cunha T.M., Tytgat J.,
Arantes E.C.;
"Ts8 scorpion toxin inhibits the Kv4.2 channel and produces nociception in
vivo.";
Toxicon 119:244-252(2016).
[52]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 42-146 IN COMPLEX WITH ZINC IONS,
AND MUTAGENESIS OF LEU-66 AND ARG-93.
PubMed=12835418; DOI=10.1073/pnas.1432840100;
Nanao M.H., Zhou W., Pfaffinger P.J., Choe S.;
"Determining the basis of channel-tetramerization specificity by X-ray
crystallography and a sequence-comparison algorithm: family values
(FamVal).";
Proc. Natl. Acad. Sci. U.S.A. 100:8670-8675(2003).
[53]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-30, FUNCTION, INTERACTION WITH
KCNIP1; KCNIP2 AND KCNIP3, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF
TRP-8 AND PHE-11, AND DOMAIN.
PubMed=14980206; DOI=10.1016/s0896-6273(04)00045-5;
Zhou W., Qian Y., Kunjilwar K., Pfaffinger P.J., Choe S.;
"Structural insights into the functional interaction of KChIP1 with Shal-
type K(+) channels.";
Neuron 41:573-586(2004).
-!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
potassium transport in excitable membranes, primarily in the brain, but
also in rodent heart (PubMed:1840649, PubMed:1722463, PubMed:9093524,
PubMed:9058605, PubMed:10676964, PubMed:12592409, PubMed:12754210,
PubMed:16207878, PubMed:16123112, PubMed:19279261, PubMed:25352783,
PubMed:14980206). Mediates the major part of the dendritic A-type
current I(SA) in brain neurons (PubMed:16207878, PubMed:17026528). This
current is activated at membrane potentials that are below the
threshold for action potentials. It regulates neuronal excitability,
prolongs the latency before the first spike in a series of action
potentials, regulates the frequency of repetitive action potential
firing, shortens the duration of action potentials and regulates the
back-propagation of action potentials from the neuronal cell body to
the dendrites. Contributes to the regulation of the circadian rhythm of
action potential firing in suprachiasmatic nucleus neurons, which
regulates the circadian rhythm of locomotor activity (By similarity).
Functions downstream of the metabotropic glutamate receptor GRM5 and
plays a role in neuronal excitability and in nociception mediated by
activation of GRM5 (By similarity). Mediates the transient outward
current I(to) in rodent heart left ventricle apex cells, but not in
human heart, where this current is mediated by another family member
(PubMed:9093524, PubMed:9058605). Forms tetrameric potassium-selective
channels through which potassium ions pass in accordance with their
electrochemical gradient. The channel alternates between opened and
closed conformations in response to the voltage difference across the
membrane (PubMed:1840649, PubMed:1722463, PubMed:9093524,
PubMed:10676964, PubMed:12451113, PubMed:12592409, PubMed:12754210,
PubMed:15452711, PubMed:16207878, PubMed:16820361, PubMed:25352783,
PubMed:14980206). Can form functional homotetrameric channels and
heterotetrameric channels that contain variable proportions of KCND2
and KCND3; channel properties depend on the type of pore-forming alpha
subunits that are part of the channel (PubMed:25352783). In vivo,
membranes probably contain a mixture of heteromeric potassium channel
complexes (PubMed:12451113, PubMed:16123112). Interaction with specific
isoforms of the regulatory subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4
strongly increases expression at the cell surface and thereby increases
channel activity; it modulates the kinetics of channel activation and
inactivation, shifts the threshold for channel activation to more
negative voltage values, shifts the threshold for inactivation to less
negative voltages and accelerates recovery after inactivation
(PubMed:12451113, PubMed:15452711, PubMed:16123112, PubMed:16820361,
PubMed:20045463, PubMed:14980206). Likewise, interaction with DPP6 or
DPP10 promotes expression at the cell membrane and regulates both
channel characteristics and activity (PubMed:15671030, PubMed:16123112,
PubMed:19441798, PubMed:19901547, PubMed:19279261).
{ECO:0000250|UniProtKB:Q9Z0V2, ECO:0000269|PubMed:10676964,
ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:12451113,
ECO:0000269|PubMed:12592409, ECO:0000269|PubMed:12754210,
ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15452711,
ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:16123112,
ECO:0000269|PubMed:16207878, ECO:0000269|PubMed:16820361,
ECO:0000269|PubMed:17026528, ECO:0000269|PubMed:1722463,
ECO:0000269|PubMed:17582333, ECO:0000269|PubMed:1840649,
ECO:0000269|PubMed:19279261, ECO:0000269|PubMed:19441798,
ECO:0000269|PubMed:19901547, ECO:0000269|PubMed:24404150,
ECO:0000269|PubMed:25352783, ECO:0000269|PubMed:9058605,
ECO:0000269|PubMed:9093524, ECO:0000305}.
-!- ACTIVITY REGULATION: Inhibited by 5 mM 4-aminopyridine (4-AP)
(PubMed:1840649, PubMed:1722463, PubMed:9093524). Not inhibited by
dendrotoxins and by tetraethylammonium (TEA) (PubMed:1722463).
Inhibited by 10 mM flecainide and 20 mM quinidine (PubMed:9093524).
Inhibited by the heteropodatoxins HpTx(1), HpTx(2), and HpTx(3)
(PubMed:9058605). {ECO:0000269|PubMed:1722463,
ECO:0000269|PubMed:1840649, ECO:0000269|PubMed:9058605,
ECO:0000269|PubMed:9093524}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few msec
(PubMed:1722463, PubMed:9093524). After that, they inactivate
rapidly, i.e within about 50-100 msec (PubMed:1722463,
PubMed:9093524). The voltage-dependence of activation and
inactivation and other channel characteristics vary depending on the
experimental conditions, the expression system and the presence or
absence of ancillary subunits (PubMed:19901547, PubMed:19279261).
Homotetrameric channels have a unitary conductance of about 4 pS when
expressed in a heterologous system (PubMed:19279261). For the
activation of homotetrameric channels expressed in xenopus oocytes,
the voltage at half-maximal amplitude is about -10 mV
(PubMed:12451113). The time constant for inactivation is about 20
msec (PubMed:12451113). For inactivation, the voltage at half-maximal
amplitude is -62 mV (PubMed:12451113). The time constant for recovery
after inactivation is about 70 msec (PubMed:12451113).
{ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:1722463,
ECO:0000269|PubMed:19279261, ECO:0000269|PubMed:19901547,
ECO:0000269|PubMed:9093524, ECO:0000305|PubMed:15858231};
-!- SUBUNIT: Homotetramer or heterotetramer with KCND1 or KCND3
(PubMed:12754210, PubMed:15485870, PubMed:20224290, PubMed:25352783).
Associates with the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and
KCNIP4 (PubMed:10676964, PubMed:12451113, PubMed:11847232,
PubMed:11805342, PubMed:15485870, PubMed:15356203, PubMed:15452711,
PubMed:16820361, PubMed:20045463, PubMed:24811166, PubMed:14980206).
Interacts with DPP6, DPP10, DLG4 and DLG1 (PubMed:11923279,
PubMed:12575952, PubMed:14559911, PubMed:15671030, PubMed:19213956). In
vivo, probably exists as heteromeric complex containing variable
proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2, KCNIP3, KCNIP4,
DPP6 and DPP10 (PubMed:16123112, PubMed:19901547). The tetrameric
channel can associate with up to four regulatory subunits, such as
KCNIP2 or KCNIP4 (By similarity). Interaction with KCNIP3 promotes
tetramerization and formation of a functional potassium channel
(PubMed:15485870). Interaction with four KCNIP4 chains does not reduce
interaction with DPP10 (By similarity). Probably part of a complex
consisting of KCNIP1, KCNIP2 isoform 3 and KCND2 (By similarity).
Interacts with FLNA and FLNC (PubMed:11102480). Interacts with
NCS1/FREQ (By similarity). Identified in a complex with cAMP-dependent
protein kinase (PKA), CAV3, AKAP6 and KCND3 in cardiac myocytes
(PubMed:20224290). {ECO:0000250|UniProtKB:Q9NZV8,
ECO:0000250|UniProtKB:Q9Z0V2, ECO:0000269|PubMed:10676964,
ECO:0000269|PubMed:11102480, ECO:0000269|PubMed:11805342,
ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:11923279,
ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:12575952,
ECO:0000269|PubMed:12754210, ECO:0000269|PubMed:14559911,
ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:14980207,
ECO:0000269|PubMed:15356203, ECO:0000269|PubMed:15452711,
ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:15671030,
ECO:0000269|PubMed:16123112, ECO:0000269|PubMed:16207878,
ECO:0000269|PubMed:16820361, ECO:0000269|PubMed:19213956,
ECO:0000269|PubMed:20224290, ECO:0000269|PubMed:24811166,
ECO:0000269|PubMed:25352783, ECO:0000305|PubMed:19441798,
ECO:0000305|PubMed:19901547}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10676964,
ECO:0000269|PubMed:10860776, ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:11847232, ECO:0000269|PubMed:12451113,
ECO:0000269|PubMed:12592409, ECO:0000269|PubMed:12754210,
ECO:0000269|PubMed:12829703, ECO:0000269|PubMed:14559911,
ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15452711,
ECO:0000269|PubMed:15485870, ECO:0000269|PubMed:15671030,
ECO:0000269|PubMed:15736227, ECO:0000269|PubMed:16123112,
ECO:0000269|PubMed:16820361, ECO:0000269|PubMed:1722463,
ECO:0000269|PubMed:17582333, ECO:0000269|PubMed:18371079,
ECO:0000269|PubMed:1840649, ECO:0000269|PubMed:18650329,
ECO:0000269|PubMed:20045463, ECO:0000269|PubMed:22098631,
ECO:0000269|PubMed:24793047, ECO:0000269|PubMed:25352783,
ECO:0000269|PubMed:9070739, ECO:0000269|PubMed:9093524}; Multi-pass
membrane protein {ECO:0000305}. Cell projection, dendrite
{ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:12592409, ECO:0000269|PubMed:15736227,
ECO:0000269|PubMed:16207878, ECO:0000269|PubMed:17582333,
ECO:0000269|PubMed:18371079, ECO:0000269|PubMed:20224290,
ECO:0000269|PubMed:22098631, ECO:0000269|PubMed:24037673,
ECO:0000269|PubMed:24404150, ECO:0000269|PubMed:9070739}. Cell
junction, synapse {ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:15736227, ECO:0000269|PubMed:17582333,
ECO:0000269|PubMed:9070739}. Perikaryon {ECO:0000269|PubMed:10676964,
ECO:0000269|PubMed:15736227, ECO:0000269|PubMed:16207878,
ECO:0000269|PubMed:18371079, ECO:0000269|PubMed:22098631,
ECO:0000269|PubMed:9070739}. Cell junction, synapse, postsynaptic cell
membrane {ECO:0000269|PubMed:15736227, ECO:0000269|PubMed:9070739}.
Cell projection, dendritic spine {ECO:0000269|PubMed:17582333,
ECO:0000269|PubMed:18650329, ECO:0000269|PubMed:22098631,
ECO:0000269|PubMed:24037673, ECO:0000269|PubMed:9070739}. Cell
membrane, sarcolemma {ECO:0000269|PubMed:10860776}. Cell junction
{ECO:0000269|PubMed:18371079}. Membrane, caveola
{ECO:0000269|PubMed:20224290}. Note=In neurons, primarily detected on
dendrites, dendritic spines and on the neuron cell body, but not on
axons (PubMed:9070739, PubMed:17582333, PubMed:16207878,
PubMed:22098631). Localized preferentially at the dendrites of
pyramidal cells in the hippocampus CA1 layer (PubMed:22098631).
Detected at GABAergic synapses (By similarity). Detected at cell
junctions that are distinct from synaptic cell contacts
(PubMed:18371079). Detected in lipid rafts (PubMed:14559911,
PubMed:20224290, PubMed:24793047). Detected primarily at the
endoplasmic reticulum or Golgi when expressed by itself
(PubMed:12829703, PubMed:12754210, PubMed:16820361, PubMed:19441798,
PubMed:14980206). Interaction with KCNIP1, KCNIP2, KCNIP3 or KCNIP4
promotes expression at the cell membrane (PubMed:12829703,
PubMed:15485870, PubMed:20045463, PubMed:14980206). Interaction with
DPP6 or DPP10 promotes expression at the cell membrane
(PubMed:19441798). Internalized from the cell membrane by clathrin-
dependent endocytosis in response to activation of AMPA-selective
glutamate receptors and PKA-mediated phosphorylation at Ser-552
(PubMed:17582333, PubMed:18650329). Redistributed from dendritic spines
to the main dendritic shaft in response to activation of AMPA-selective
glutamate receptors and activation of PKA (PubMed:17582333,
PubMed:18650329). {ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:12754210, ECO:0000269|PubMed:14559911,
ECO:0000269|PubMed:14980206, ECO:0000269|PubMed:15485870,
ECO:0000269|PubMed:16207878, ECO:0000269|PubMed:16820361,
ECO:0000269|PubMed:17582333, ECO:0000269|PubMed:18650329,
ECO:0000269|PubMed:19441798, ECO:0000269|PubMed:20045463,
ECO:0000269|PubMed:20224290, ECO:0000269|PubMed:22098631,
ECO:0000269|PubMed:24793047, ECO:0000269|PubMed:9070739, ECO:0000305}.
-!- TISSUE SPECIFICITY: Detected in brain cortex, hippocampus, dentate
gyrus, thalamus and cerebellum (PubMed:16123112). Detected in neurons
from the primary visual cortex (PubMed:16207878). Detected in the
supraoptic nucleus in hypothalamus, in hippocampus and the habenular
nucleus of the thalamus (PubMed:9070739). Detected in the bed nucleus
of the stria terminalis (PubMed:24037673). Detected in dendritic fields
in the hippocampus CA1 layer, in stratum radiatum, stratum oriens,
stratum lacunosum-moleculare and stratum pyramidale (PubMed:10676964,
PubMed:22098631). Detected in dendritic fields in the hippocampus CA3
layer and in dentate gyrus (PubMed:10676964). Detected in the
cerebellum granule cell layer, where it localizes at synapses
(PubMed:11102480, PubMed:10676964, PubMed:15736227). Detected in the
main olfactory bulb, especially in the granule cell layer and the
external plexiform layer, but also the mitral layer (PubMed:18371079).
Detected in heart atrium and ventricle (PubMed:10860776). Detected in
heart left ventricle (at protein level) (PubMed:24793047). Highly
expressed in heart and throughout the brain, with similar levels in
cortex and hypothalamus, and much higher levels in hippocampus, dentate
gyrus and the habenular nucleus of the thalamus. Detected in brain, and
at lower levels in heart atrium and ventricle (PubMed:1705709).
Detected in neurons from the bed nucleus of the stria terminalis
(PubMed:24037673). Detected in aorta, cardiac and smooth muscle.
{ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:15736227, ECO:0000269|PubMed:16123112,
ECO:0000269|PubMed:16207878, ECO:0000269|PubMed:1705709,
ECO:0000269|PubMed:18371079, ECO:0000269|PubMed:1840649,
ECO:0000269|PubMed:22098631, ECO:0000269|PubMed:24793047,
ECO:0000269|PubMed:9070739}.
-!- INDUCTION: Down-regulated in response to hypoxia lasting about 15 min,
a treatment that leads to spontaneous convulsive seizures in these
pups. {ECO:0000269|PubMed:25352783}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
characterized by a series of positively charged amino acids at every
third position. Channel opening and closing is effected by a
conformation change that affects the position and orientation of the
voltage-sensor paddle formed by S3 and S4 within the membrane. A
transmembrane electric field that is positive inside would push the
positively charged S4 segment outwards, thereby opening the pore, while
a field that is negative inside would pull the S4 segment inwards and
close the pore. Changes in the position and orientation of S4 are then
transmitted to the activation gate formed by the inner helix bundle via
the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The N-terminal cytoplasmic region can mediate N-type
inactivation by physically blocking the channel (PubMed:15452711). This
probably does not happen in vivo, where the N-terminal region mediates
interaction with regulatory subunits, such as KCNIP1 and KCNIP2
(PubMed:16820361, PubMed:18357523, PubMed:14980206). The zinc binding
sites in the N-terminal domain are important for tetramerization and
assembly of a functional channel complex (PubMed:12754210). Most
likely, the channel undergoes closed-state inactivation, where a subtle
conformation change would render the protein less sensitive to
activation. {ECO:0000250|UniProtKB:Q9NZV8, ECO:0000269|PubMed:12754210,
ECO:0000269|PubMed:16820361, ECO:0000305|PubMed:14980206,
ECO:0000305|PubMed:15452711, ECO:0000305|PubMed:18357523}.
-!- DOMAIN: The C-terminal cytoplasmic region is important for normal
expression at the cell membrane and modulates the voltage-dependence of
channel activation and inactivation. It is required for interaction
with KCNIP2, and probably other family members as well.
{ECO:0000269|PubMed:16820361}.
-!- PTM: Phosphorylation at Ser-438 in response to MAPK activation is
increased in stimulated dendrites (PubMed:24404150). Interaction with
KCNIP2 and DPP6 propomtes phosphorylation by PKA at Ser-552
(PubMed:19441798). Phosphorylation at Ser-552 has no effect on
interaction with KCNIP3, but is required for the regulation of channel
activity by KCNIP3 (PubMed:12451113). Phosphorylation at Ser-552 leads
to KCND2 internalization (PubMed:17582333). Phosphorylated by MAPK in
response to signaling via the metabotropic glutamate receptor GRM5 (By
similarity). Phosphorylation at Ser-616 is required for the down-
regulation of neuronal A-type currents in response to signaling via
GRM5 (By similarity). {ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:17582333,
ECO:0000269|PubMed:19441798, ECO:0000269|PubMed:24404150}.
-!- MISCELLANEOUS: The transient neuronal A-type potassium current called
I(SA) is triggered at membrane potentials that are below the threshold
for action potentials. It inactivates rapidly and recovers rapidly from
inactivation. It regulates the firing of action potentials and plays a
role in synaptic integration and plasticity. Potassium channels
containing KCND2 account for about 80% of the neuronal A-type potassium
current. In contrast, the potassium channel responsible for the cardiac
I(to) current differs between species; it is mediated by KCND2 in
rodents. In human and other non-rodents KCND3 may play an equivalent
role. {ECO:0000269|PubMed:9093524, ECO:0000305|PubMed:17917103,
ECO:0000305|PubMed:18357523}.
-!- MISCELLANEOUS: Is specifically and reversibly inhibited by the scorpion
toxin Ts8 (AC P69940). {ECO:0000269|PubMed:27346450}.
-!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA40929.1; Type=Frameshift; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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EMBL; S64320; AAB19939.1; -; mRNA.
EMBL; M59980; AAA40929.1; ALT_FRAME; mRNA.
PIR; I57681; I57681.
PIR; JU0271; JU0271.
RefSeq; NP_113918.2; NM_031730.2.
PDB; 1NN7; X-ray; 2.10 A; A=42-146.
PDB; 1S6C; X-ray; 2.00 A; B=1-30.
PDBsum; 1NN7; -.
PDBsum; 1S6C; -.
SMR; Q63881; -.
BioGRID; 249292; 2.
CORUM; Q63881; -.
IntAct; Q63881; 3.
STRING; 10116.ENSRNOP00000039227; -.
BindingDB; Q63881; -.
ChEMBL; CHEMBL1075227; -.
DrugCentral; Q63881; -.
GuidetoPHARMACOLOGY; 553; -.
iPTMnet; Q63881; -.
PhosphoSitePlus; Q63881; -.
PaxDb; Q63881; -.
PRIDE; Q63881; -.
ABCD; Q63881; 3 sequenced antibodies.
GeneID; 65180; -.
KEGG; rno:65180; -.
UCSC; RGD:68393; rat.
CTD; 3751; -.
RGD; 68393; Kcnd2.
eggNOG; KOG4390; Eukaryota.
InParanoid; Q63881; -.
OrthoDB; 469107at2759; -.
PhylomeDB; Q63881; -.
EvolutionaryTrace; Q63881; -.
PRO; PR:Q63881; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0098982; C:GABA-ergic synapse; ISO:RGD.
GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
GO; GO:0099055; C:integral component of postsynaptic membrane; IDA:SynGO.
GO; GO:0099060; C:integral component of postsynaptic specialization membrane; ISO:RGD.
GO; GO:0031226; C:intrinsic component of plasma membrane; ISO:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0097038; C:perinuclear endoplasmic reticulum; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IDA:RGD.
GO; GO:0044853; C:plasma membrane raft; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IDA:RGD.
GO; GO:0045211; C:postsynaptic membrane; IDA:UniProtKB.
GO; GO:0034705; C:potassium channel complex; IDA:RGD.
GO; GO:0042383; C:sarcolemma; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; IDA:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IDA:UniProtKB.
GO; GO:0005216; F:ion channel activity; IDA:RGD.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0005267; F:potassium channel activity; IDA:RGD.
GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
GO; GO:1905030; F:voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential; IMP:SynGO.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0001508; P:action potential; IMP:RGD.
GO; GO:0086001; P:cardiac muscle cell action potential; IMP:UniProtKB.
GO; GO:0035690; P:cellular response to drug; IEP:RGD.
GO; GO:0071456; P:cellular response to hypoxia; IDA:UniProtKB.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:RGD.
GO; GO:0045475; P:locomotor rhythm; ISO:RGD.
GO; GO:0019228; P:neuronal action potential; ISO:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:RGD.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 3.30.710.10; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003975; K_chnl_volt-dep_Kv4.
InterPro; IPR004055; K_chnl_volt-dep_Kv4.2.
InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
InterPro; IPR021645; Shal-type_N.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF11879; DUF3399; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11601; Shal-type; 1.
PRINTS; PR01517; KV42CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01497; SHALCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Cell projection; Ion channel;
Ion transport; Membrane; Metal-binding; Phosphoprotein;
Postsynaptic cell membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Synapse; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel; Zinc.
CHAIN 1..630
/note="Potassium voltage-gated channel subfamily D member
2"
/id="PRO_0000054067"
TOPO_DOM 1..182
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 183..204
/note="Helical; Name=Segment S1"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 205..228
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 229..250
/note="Helical; Name=Segment S2"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 251..261
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 262..279
/note="Helical; Name=Segment S3"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 280..286
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 287..306
/note="Helical; Voltage-sensor; Name=Segment S4"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 307..321
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 322..343
/note="Helical; Name=Segment S5"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 344..357
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 358..369
/note="Helical; Name=Pore helix"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 370..377
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 378..384
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 385..413
/note="Helical; Name=Segment S6"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 414..630
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 2..20
/note="Interaction with KCNIP1, KCNIP2, and other family
members"
/evidence="ECO:0000305|PubMed:14980206,
ECO:0000305|PubMed:14980207"
REGION 71..90
/note="Interaction with KCNIP1"
/evidence="ECO:0000305|PubMed:14980207"
REGION 308..321
/note="S4-S5 linker"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 474..630
/note="Important for normal channel activation and
inactivation, for interaction with KCNIP2, and probably
other family members as well"
/evidence="ECO:0000305|PubMed:16820361"
REGION 474..489
/note="Required for dendritic targeting"
/evidence="ECO:0000269|PubMed:12592409"
REGION 600..623
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 370..375
/note="Selectivity filter"
/evidence="ECO:0000250|UniProtKB:P63142"
MOTIF 627..630
/note="PDZ-binding"
/evidence="ECO:0000269|PubMed:11923279,
ECO:0000269|PubMed:14559911"
METAL 105
/note="Zinc; via pros nitrogen"
/evidence="ECO:0007744|PDB:1NN7"
METAL 132
/note="Zinc"
/evidence="ECO:0007744|PDB:1NN7"
METAL 133
/note="Zinc"
/evidence="ECO:0007744|PDB:1NN7"
MOD_RES 38
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:10681507"
MOD_RES 438
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:24404150"
MOD_RES 548
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19441798,
ECO:0007744|PubMed:22673903"
MOD_RES 552
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:10681507,
ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:12829703,
ECO:0000269|PubMed:18650329, ECO:0000269|PubMed:19441798,
ECO:0007744|PubMed:22673903"
MOD_RES 572
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19441798,
ECO:0007744|PubMed:22673903"
MOD_RES 575
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:19441798,
ECO:0007744|PubMed:22673903"
MOD_RES 602
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:11080179"
MOD_RES 607
/note="Phosphothreonine"
/evidence="ECO:0000269|PubMed:11080179"
MOD_RES 616
/note="Phosphoserine"
/evidence="ECO:0000269|PubMed:11080179"
MUTAGEN 7..11
/note="Missing: Greatly reduces interaction with KCNIP1."
/evidence="ECO:0000269|PubMed:14980207"
MUTAGEN 8
/note="W->A: Abolishes interaction with KCNP1; when
associated with A-11."
/evidence="ECO:0000269|PubMed:14980206"
MUTAGEN 11
/note="F->A: Abolishes interaction with KCNP1; when
associated with A-8."
/evidence="ECO:0000269|PubMed:14980206"
MUTAGEN 66
/note="L->R: Abolishes expression."
/evidence="ECO:0000269|PubMed:12835418"
MUTAGEN 71
/note="E->K: Abolishes interaction with KCNIP1."
/evidence="ECO:0000269|PubMed:14980207"
MUTAGEN 73
/note="D->M: Abolishes interaction with KCNIP1."
/evidence="ECO:0000269|PubMed:14980207"
MUTAGEN 74
/note="F->R: Abolishes interaction with KCNIP1."
/evidence="ECO:0000269|PubMed:14980207"
MUTAGEN 79
/note="E->L,R: Abolishes interaction with KCNIP1."
/evidence="ECO:0000269|PubMed:14980207"
MUTAGEN 93
/note="R->A: Greatly reduces expression and changes
multimerization."
/evidence="ECO:0000269|PubMed:12835418"
MUTAGEN 105
/note="H->A: Abolishes tetramerization and assembly of a
functional channel."
/evidence="ECO:0000269|PubMed:12754210"
MUTAGEN 111
/note="C->A: Abolishes tetramerization and assembly of a
functional channel; when associated with A-105; A-132 and
A-133."
/evidence="ECO:0000269|PubMed:12754210"
MUTAGEN 132
/note="C->A: Abolishes tetramerization and assembly of a
functional channel; when associated with A-105; A-111 and
A-133."
/evidence="ECO:0000269|PubMed:12754210"
MUTAGEN 133
/note="C->A: Abolishes tetramerization and assembly of a
functional channel; when associated with A-105; A-111 and
A-132."
/evidence="ECO:0000269|PubMed:12754210"
MUTAGEN 481..482
/note="Missing: Loss of dendritic targeted expression."
/evidence="ECO:0000269|PubMed:12592409"
MUTAGEN 552
/note="S->A: Abolishes PKA-mediated modulation of cell
surface expression and channel activity."
/evidence="ECO:0000269|PubMed:12451113,
ECO:0000269|PubMed:18650329"
MUTAGEN 627..630
/note="Missing: Abolishes interaction with DLG4."
/evidence="ECO:0000269|PubMed:11923279,
ECO:0000269|PubMed:14559911"
HELIX 1..6
/evidence="ECO:0007829|PDB:1S6C"
HELIX 9..17
/evidence="ECO:0007829|PDB:1S6C"
STRAND 43..47
/evidence="ECO:0007829|PDB:1NN7"
STRAND 50..54
/evidence="ECO:0007829|PDB:1NN7"
HELIX 56..60
/evidence="ECO:0007829|PDB:1NN7"
STRAND 64..66
/evidence="ECO:0007829|PDB:1NN7"
HELIX 70..75
/evidence="ECO:0007829|PDB:1NN7"
HELIX 78..80
/evidence="ECO:0007829|PDB:1NN7"
STRAND 81..85
/evidence="ECO:0007829|PDB:1NN7"
TURN 89..91
/evidence="ECO:0007829|PDB:1NN7"
HELIX 92..101
/evidence="ECO:0007829|PDB:1NN7"
HELIX 112..122
/evidence="ECO:0007829|PDB:1NN7"
HELIX 131..145
/evidence="ECO:0007829|PDB:1NN7"
SEQUENCE 630 AA; 70549 MW; FDE57E8A5113BABF CRC64;
MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE
RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA
FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDNTGES ALPTMTARQR VWRAFENPHT
STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF
TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA
FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
KRRAQKKARL ARIRAAKSGS ANAYMQSKRN GLLSNQLQSS EDEPAFVSKS GSSFETQHHH
LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKSFRI
PNANVSGSHR GSVQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
PTPPVTTPEG DDRPESPEYS GGNIVRVSAL


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Pathways :
WP2197: Endothelin
WP2272: Pathogenic Escherichia coli infection
WP1566: Citrate cycle (TCA cycle)
WP1634: Butanoate metabolism
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1711: Trinitrotoluene degradation
WP1626: Benzoate degradation via CoA ligation
WP1655: Geraniol degradation
WP1672: Mismatch repair
WP1694: Pyrimidine metabolism
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP2292: Chemokine signaling pathway
WP1614: 1- and 2-Methylnaphthalene degradation
WP1644: DNA replication
WP1671: Methane metabolism
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism

Related Genes :
[Kcnd2] Potassium voltage-gated channel subfamily D member 2 (RK5) (Shal1) (Voltage-gated potassium channel subunit Kv4.2)
[KCND2 KIAA1044] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcnd2 Kiaa1044 MNCb-7013] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[KCNC1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCND3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcnd3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcnd3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[KCND1] Potassium voltage-gated channel subfamily D member 1 (Voltage-gated potassium channel subunit Kv4.1)
[KCND2] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (RAW2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCND2] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[Kcnd1] Potassium voltage-gated channel subfamily D member 1 (Voltage-gated potassium channel subunit Kv4.1) (mShal)
[Kcnc2] Potassium voltage-gated channel subfamily C member 2 (Potassium channel voltage-gated Shaw-related subfamily C member 2) (Shaw-like potassium channel) (Voltage-gated potassium channel subunit Kv3.2)
[KCND3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcna5] Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5) (KV1-5)
[KCNA2] Potassium voltage-gated channel subfamily A member 2 (NGK1) (Voltage-gated K(+) channel HuKIV) (Voltage-gated potassium channel HBK5) (Voltage-gated potassium channel subunit Kv1.2)
[KCNA4 KCNA4L] Potassium voltage-gated channel subfamily A member 4 (HPCN2) (Voltage-gated K(+) channel HuKII) (Voltage-gated potassium channel HBK4) (Voltage-gated potassium channel HK1) (Voltage-gated potassium channel subunit Kv1.4)
[KCNA5] Potassium voltage-gated channel subfamily A member 5 (HPCN1) (Voltage-gated potassium channel HK2) (Voltage-gated potassium channel subunit Kv1.5)
[KCNQ2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Neuroblastoma-specific potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[Kcnq2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[KCNH3 KIAA1282] Potassium voltage-gated channel subfamily H member 3 (Brain-specific eag-like channel 1) (BEC1) (Ether-a-go-go-like potassium channel 2) (ELK channel 2) (ELK2) (Voltage-gated potassium channel subunit Kv12.2)
[KCNB1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (h-DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[KCNH6 ERG2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (hERG-2) (hERG2) (Voltage-gated potassium channel subunit Kv11.2)
[Kcnh6 Erg2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (Voltage-gated potassium channel subunit Kv11.2)
[KCNH2 ERG ERG1 HERG] Potassium voltage-gated channel subfamily H member 2 (Eag homolog) (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (H-ERG) (hERG-1) (hERG1) (Voltage-gated potassium channel subunit Kv11.1)
[KCNA1] Potassium voltage-gated channel subfamily A member 1 (Voltage-gated K(+) channel HuKI) (Voltage-gated potassium channel HBK1) (Voltage-gated potassium channel subunit Kv1.1)
[KCNB1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[KCNH5 EAG2] Potassium voltage-gated channel subfamily H member 5 (Ether-a-go-go potassium channel 2) (hEAG2) (Voltage-gated potassium channel subunit Kv10.2)

Bibliography :
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