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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.
22-NOV-2017, entry version 152.
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, ENZYME 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, ENZYME 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, ENZYME 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, ENZYME 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;
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;
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}.
-!- ENZYME 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; Positions=477; 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.
UniGene; Rn.87841; -.
PDB; 1NN7; X-ray; 2.10 A; A=42-146.
PDB; 1S6C; X-ray; 2.00 A; B=1-30.
PDBsum; 1NN7; -.
PDBsum; 1S6C; -.
ProteinModelPortal; Q63881; -.
SMR; Q63881; -.
BioGrid; 249292; 2.
CORUM; Q63881; -.
IntAct; Q63881; 3.
MINT; MINT-104113; -.
STRING; 10116.ENSRNOP00000039227; -.
BindingDB; Q63881; -.
ChEMBL; CHEMBL1075227; -.
GuidetoPHARMACOLOGY; 553; -.
iPTMnet; Q63881; -.
PhosphoSitePlus; Q63881; -.
PaxDb; Q63881; -.
PRIDE; Q63881; -.
GeneID; 65180; -.
KEGG; rno:65180; -.
UCSC; RGD:68393; rat.
CTD; 3751; -.
RGD; 68393; Kcnd2.
eggNOG; KOG4390; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000231013; -.
HOVERGEN; HBG106687; -.
InParanoid; Q63881; -.
KO; K04892; -.
PhylomeDB; Q63881; -.
EvolutionaryTrace; Q63881; -.
PRO; PR:Q63881; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005901; C:caveola; IDA:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0043197; C:dendritic spine; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA: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:0046982; F:protein heterodimerization activity; 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:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0019233; P:sensory perception of pain; ISO:RGD.
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.
PANTHER; PTHR11537; PTHR11537; 2.
Pfam; PF02214; BTB_2; 1.
Pfam; PF11879; DUF3399; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11601; Shal-type; 1.
PRINTS; PR00169; KCHANNEL.
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;
Complete proteome; 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 Potassium voltage-gated channel subfamily
D member 2.
/FTId=PRO_0000054067.
TOPO_DOM 1 182 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 183 204 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 205 228 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 229 250 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 251 261 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 262 279 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 280 286 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 287 306 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 307 321 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 322 343 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 344 357 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 358 369 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 370 377 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 378 384 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 385 413 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 414 630 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 2 20 Interaction with KCNIP1, KCNIP2, and
other family members.
{ECO:0000305|PubMed:14980206,
ECO:0000305|PubMed:14980207}.
REGION 71 90 Interaction with KCNIP1.
{ECO:0000305|PubMed:14980207}.
REGION 308 321 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
REGION 474 630 Important for normal channel activation
and inactivation, for interaction with
KCNIP2, and probably other family members
as well. {ECO:0000305|PubMed:16820361}.
REGION 474 489 Required for dendritic targeting.
{ECO:0000269|PubMed:12592409}.
MOTIF 370 375 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 627 630 PDZ-binding.
{ECO:0000269|PubMed:11923279,
ECO:0000269|PubMed:14559911}.
METAL 105 105 Zinc; via pros nitrogen.
{ECO:0000244|PDB:1NN7}.
METAL 132 132 Zinc. {ECO:0000244|PDB:1NN7}.
METAL 133 133 Zinc. {ECO:0000244|PDB:1NN7}.
MOD_RES 38 38 Phosphothreonine.
{ECO:0000269|PubMed:10681507}.
MOD_RES 438 438 Phosphoserine.
{ECO:0000269|PubMed:24404150}.
MOD_RES 548 548 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:19441798}.
MOD_RES 552 552 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:10681507,
ECO:0000269|PubMed:12451113,
ECO:0000269|PubMed:12829703,
ECO:0000269|PubMed:18650329,
ECO:0000269|PubMed:19441798}.
MOD_RES 572 572 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:19441798}.
MOD_RES 575 575 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:19441798}.
MOD_RES 602 602 Phosphothreonine.
{ECO:0000269|PubMed:11080179}.
MOD_RES 607 607 Phosphothreonine.
{ECO:0000269|PubMed:11080179}.
MOD_RES 616 616 Phosphoserine.
{ECO:0000269|PubMed:11080179}.
MUTAGEN 7 11 Missing: Greatly reduces interaction with
KCNIP1. {ECO:0000269|PubMed:14980207}.
MUTAGEN 8 8 W->A: Abolishes interaction with KCNP1;
when associated with A-11.
{ECO:0000269|PubMed:14980206}.
MUTAGEN 11 11 F->A: Abolishes interaction with KCNP1;
when associated with A-8.
{ECO:0000269|PubMed:14980206}.
MUTAGEN 66 66 L->R: Abolishes expression.
{ECO:0000269|PubMed:12835418}.
MUTAGEN 71 71 E->K: Abolishes interaction with KCNIP1.
{ECO:0000269|PubMed:14980207}.
MUTAGEN 73 73 D->M: Abolishes interaction with KCNIP1.
{ECO:0000269|PubMed:14980207}.
MUTAGEN 74 74 F->R: Abolishes interaction with KCNIP1.
{ECO:0000269|PubMed:14980207}.
MUTAGEN 79 79 E->L,R: Abolishes interaction with
KCNIP1. {ECO:0000269|PubMed:14980207}.
MUTAGEN 93 93 R->A: Greatly reduces expression and
changes multimerization.
{ECO:0000269|PubMed:12835418}.
MUTAGEN 105 105 H->A: Abolishes tetramerization and
assembly of a functional channel.
{ECO:0000269|PubMed:12754210}.
MUTAGEN 111 111 C->A: Abolishes tetramerization and
assembly of a functional channel; when
associated with A-105; A-132 and A-133.
{ECO:0000269|PubMed:12754210}.
MUTAGEN 132 132 C->A: Abolishes tetramerization and
assembly of a functional channel; when
associated with A-105; A-111 and A-133.
{ECO:0000269|PubMed:12754210}.
MUTAGEN 133 133 C->A: Abolishes tetramerization and
assembly of a functional channel; when
associated with A-105; A-111 and A-132.
{ECO:0000269|PubMed:12754210}.
MUTAGEN 481 482 Missing: Loss of dendritic targeted
expression.
{ECO:0000269|PubMed:12592409}.
MUTAGEN 552 552 S->A: Abolishes PKA-mediated modulation
of cell surface expression and channel
activity. {ECO:0000269|PubMed:12451113,
ECO:0000269|PubMed:18650329}.
MUTAGEN 627 630 Missing: Abolishes interaction with DLG4.
{ECO:0000269|PubMed:11923279,
ECO:0000269|PubMed:14559911}.
HELIX 1 6 {ECO:0000244|PDB:1S6C}.
HELIX 9 17 {ECO:0000244|PDB:1S6C}.
STRAND 43 47 {ECO:0000244|PDB:1NN7}.
STRAND 50 54 {ECO:0000244|PDB:1NN7}.
HELIX 56 60 {ECO:0000244|PDB:1NN7}.
STRAND 64 66 {ECO:0000244|PDB:1NN7}.
HELIX 70 75 {ECO:0000244|PDB:1NN7}.
HELIX 78 80 {ECO:0000244|PDB:1NN7}.
STRAND 81 85 {ECO:0000244|PDB:1NN7}.
TURN 89 91 {ECO:0000244|PDB:1NN7}.
HELIX 92 101 {ECO:0000244|PDB:1NN7}.
HELIX 112 122 {ECO:0000244|PDB:1NN7}.
HELIX 131 145 {ECO:0000244|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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