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Potassium voltage-gated channel subfamily A member 2 (RAK) (RBK2) (RCK5) (Voltage-gated potassium channel subunit Kv1.2)

 KCNA2_RAT               Reviewed;         499 AA.
P63142; P15386; Q02010;
13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
13-SEP-2004, sequence version 1.
20-JUN-2018, entry version 139.
RecName: Full=Potassium voltage-gated channel subfamily A member 2;
AltName: Full=RAK;
AltName: Full=RBK2 {ECO:0000303|PubMed:2722779};
AltName: Full=RCK5 {ECO:0000303|PubMed:2555158};
AltName: Full=Voltage-gated potassium channel subunit Kv1.2;
Name=Kcna2;
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], AND TISSUE SPECIFICITY.
PubMed=2722779;
McKinnon D.;
"Isolation of a cDNA clone coding for a putative second potassium
channel indicates the existence of a gene family.";
J. Biol. Chem. 264:8230-8236(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYME
REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=2555158;
Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B.,
Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O.;
"Molecular basis of functional diversity of voltage-gated potassium
channels in mammalian brain.";
EMBO J. 8:3235-3244(1989).
[3]
SEQUENCE REVISION.
Ludwig J.;
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
TISSUE=Heart atrium;
PubMed=1715584; DOI=10.1073/pnas.88.17.7892;
Paulmichl M., Nasmith P., Herllmiss R., Reed K., Boyle W.A.,
Nerbonne J.M., Peralta E.G., Clapham D.E.;
"Cloning and expression of a rat cardiac delayed rectifier potassium
channel.";
Proc. Natl. Acad. Sci. U.S.A. 88:7892-7895(1991).
[5]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNA4, AND
ENZYME REGULATION.
PubMed=8495559; DOI=10.1161/01.RES.72.6.1326;
Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.;
"Heteromultimeric assembly of human potassium channels. Molecular
basis of a transient outward current?";
Circ. Res. 72:1326-1336(1993).
[6]
ENZYME REGULATION.
PubMed=8355670;
Werkman T.R., Gustafson T.A., Rogowski R.S., Blaustein M.P.,
Rogawski M.A.;
"Tityustoxin-K alpha, a structurally novel and highly potent K+
channel peptide toxin, interacts with the alpha-dendrotoxin binding
site on the cloned Kv1.2 K+ channel.";
Mol. Pharmacol. 44:430-436(1993).
[7]
SUBUNIT, INTERACTION WITH KCNA4, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=8361540; DOI=10.1038/365072a0;
Sheng M., Liao Y.J., Jan Y.N., Jan L.Y.;
"Presynaptic A-current based on heteromultimeric K+ channels detected
in vivo.";
Nature 365:72-75(1993).
[8]
INTERACTION WITH DLG1; DLG2 AND DLG4, AND TISSUE SPECIFICITY.
PubMed=7477295; DOI=10.1038/378085a0;
Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.;
"Clustering of Shaker-type K+ channels by interaction with a family of
membrane-associated guanylate kinases.";
Nature 378:85-88(1995).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
TISSUE=Brain;
PubMed=7544443; DOI=10.1038/376737a0;
Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M.,
Plowman G.D., Rudy B., Schlessinger J.;
"Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of
ion channel and MAP kinase functions.";
Nature 376:737-745(1995).
[10]
FUNCTION, AND INTERACTION WITH RHOA.
PubMed=9635436; DOI=10.1016/S0092-8674(00)81212-X;
Cachero T.G., Morielli A.D., Peralta E.G.;
"The small GTP-binding protein RhoA regulates a delayed rectifier
potassium channel.";
Cell 93:1077-1085(1998).
[11]
INTERACTION WITH CNTNAP2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=10624965; DOI=10.1016/S0896-6273(00)81049-1;
Poliak S., Gollan L., Martinez R., Custer A., Einheber S.,
Salzer J.L., Trimmer J.S., Shrager P., Peles E.;
"Caspr2, a new member of the neurexin superfamily, is localized at the
juxtaparanodes of myelinated axons and associates with K+ channels.";
Neuron 24:1037-1047(1999).
[12]
SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNAB2; KCNA1 AND
KCNA4, AND GLYCOSYLATION.
PubMed=10896669; DOI=10.1074/jbc.M005010200;
Manganas L.N., Trimmer J.S.;
"Subunit composition determines Kv1 potassium channel surface
expression.";
J. Biol. Chem. 275:29685-29693(2000).
[13]
SUBCELLULAR LOCATION, INTERACTION WITH KCNA1 AND KCNAB2, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=11086297;
DOI=10.1002/1096-9861(20000101)429:1<166::AID-CNE13>3.0.CO;2-Y;
Rasband M.N., Trimmer J.S.;
"Subunit composition and novel localization of K+ channels in spinal
cord.";
J. Comp. Neurol. 429:166-176(2001).
[14]
INTERACTION WITH PTK2B, AND PHOSPHORYLATION.
PubMed=11739373; DOI=10.1074/jbc.M104726200;
Byron K.L., Lucchesi P.A.;
"Signal transduction of physiological concentrations of vasopressin in
A7r5 vascular smooth muscle cells. A role for PYK2 and tyrosine
phosphorylation of K+ channels in the stimulation of Ca2+ spiking.";
J. Biol. Chem. 277:7298-7307(2002).
[15]
FUNCTION, PHOSPHORYLATION, INTERACTION WITH CTTN, SUBCELLULAR
LOCATION, TOPOLOGY, AND MUTAGENESIS OF TYR-415 AND TYR-417.
PubMed=12151401; DOI=10.1074/jbc.M205005200;
Hattan D., Nesti E., Cachero T.G., Morielli A.D.;
"Tyrosine phosphorylation of Kv1.2 modulates its interaction with the
actin-binding protein cortactin.";
J. Biol. Chem. 277:38596-38606(2002).
[16]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=12177193;
Dodson P.D., Barker M.C., Forsythe I.D.;
"Two heteromeric Kv1 potassium channels differentially regulate action
potential firing.";
J. Neurosci. 22:6953-6961(2002).
[17]
INDUCTION BY HYPOXIA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
PHOSPHORYLATION.
PubMed=14713306;
Qiu M.H., Zhang R., Sun F.Y.;
"Enhancement of ischemia-induced tyrosine phosphorylation of Kv1.2 by
vascular endothelial growth factor via activation of
phosphatidylinositol 3-kinase.";
J. Neurochem. 87:1509-1517(2003).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12777451; DOI=10.1113/jphysiol.2003.046250;
Dodson P.D., Billups B., Rusznak Z., Szucs G., Barker M.C.,
Forsythe I.D.;
"Presynaptic rat Kv1.2 channels suppress synaptic terminal
hyperexcitability following action potential invasion.";
J. Physiol. (Lond.) 550:27-33(2003).
[19]
SUBUNIT, INTERACTION WITH KCNA4, AND TISSUE SPECIFICITY.
PubMed=12632190; DOI=10.1007/s00424-002-0994-7;
Fergus D.J., Martens J.R., England S.K.;
"Kv channel subunits that contribute to voltage-gated K+ current in
renal vascular smooth muscle.";
Pflugers Arch. 445:697-704(2003).
[20]
INDUCTION BY HYPOXIA.
PubMed=15151918; DOI=10.1165/rcmb.2003-0386OC;
Hong Z., Weir E.K., Nelson D.P., Olschewski A.;
"Subacute hypoxia decreases voltage-activated potassium channel
expression and function in pulmonary artery myocytes.";
Am. J. Respir. Cell Mol. Biol. 31:337-343(2004).
[21]
FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=15618540; DOI=10.1161/01.RES.0000154070.06421.25;
Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K.,
Chen T., Cole W.;
"Heteromultimeric Kv1 channels contribute to myogenic control of
arterial diameter.";
Circ. Res. 96:216-224(2005).
[22]
FUNCTION.
PubMed=16210348; DOI=10.1113/jphysiol.2005.098053;
Khavandgar S., Walter J.T., Sageser K., Khodakhah K.;
"Kv1 channels selectively prevent dendritic hyperexcitability in rat
Purkinje cells.";
J. Physiol. (Lond.) 569:545-557(2005).
[23]
FUNCTION.
PubMed=16306173; DOI=10.1152/jn.01004.2005;
Finnegan T.F., Chen S.R., Pan H.L.;
"Mu opioid receptor activation inhibits GABAergic inputs to
basolateral amygdala neurons through Kv1.1/1.2 channels.";
J. Neurophysiol. 95:2032-2041(2006).
[24]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-207, AND
MUTAGENESIS OF ASN-207; SER-356; SER-360 AND THR-383.
PubMed=16770729; DOI=10.1007/s11064-006-9056-4;
Fujita T., Utsunomiya I., Ren J., Matsushita Y., Kawai M., Sasaki S.,
Hoshi K., Miyatake T., Taguchi K.;
"Glycosylation and cell surface expression of Kv1.2 potassium channel
are regulated by determinants in the pore region.";
Neurochem. Res. 31:589-596(2006).
[25]
SUBCELLULAR LOCATION, GLYCOSYLATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=17324383; DOI=10.1016/j.brainres.2007.01.092;
Watanabe I., Zhu J., Sutachan J.J., Gottschalk A., Recio-Pinto E.,
Thornhill W.B.;
"The glycosylation state of Kv1.2 potassium channels affects
trafficking, gating, and simulated action potentials.";
Brain Res. 1144:1-18(2007).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-252.
PubMed=17766348; DOI=10.1529/biophysj.107.116160;
Rezazadeh S., Kurata H.T., Claydon T.W., Kehl S.J., Fedida D.;
"An activation gating switch in Kv1.2 is localized to a threonine
residue in the S2-S3 linker.";
Biophys. J. 93:4173-4186(2007).
[27]
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).
[28]
FUNCTION.
PubMed=17869444; DOI=10.1016/j.neuroscience.2007.08.007;
Yang Q., Chen S.R., Li D.P., Pan H.L.;
"Kv1.1/1.2 channels are downstream effectors of nitric oxide on
synaptic GABA release to preautonomic neurons in the paraventricular
nucleus.";
Neuroscience 149:315-327(2007).
[29]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-440 AND SER-449,
IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH KCNAB2, AND
MUTAGENESIS OF THR-46; SER-440 AND SER-449.
PubMed=18003609; DOI=10.1074/jbc.M708875200;
Connors E.C., Ballif B.A., Morielli A.D.;
"Homeostatic regulation of Kv1.2 potassium channel trafficking by
cyclic AMP.";
J. Biol. Chem. 283:3445-3453(2008).
[30]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF 267-PHE--PHE-302.
PubMed=18638484; DOI=10.1016/j.jmb.2008.06.085;
Tao X., MacKinnon R.;
"Functional analysis of Kv1.2 and paddle chimera Kv channels in planar
lipid bilayers.";
J. Mol. Biol. 382:24-33(2008).
[31]
FUNCTION, SUBUNIT, AND INTERACTION WITH KCNAB1.
PubMed=19713757; DOI=10.4161/chan.3.5.9558;
Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.;
"The molecular basis for the actions of Kvbeta1.2 on the opening and
closing of the Kv1.2 delayed rectifier channel.";
Channels 3:314-322(2009).
[32]
SUBCELLULAR LOCATION.
PubMed=19403695; DOI=10.1091/mbc.E08-10-1074;
Stirling L., Williams M.R., Morielli A.D.;
"Dual roles for RHOA/RHO-kinase in the regulated trafficking of a
voltage-sensitive potassium channel.";
Mol. Biol. Cell 20:2991-3002(2009).
[33]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=20805574; DOI=10.1085/jgp.200910398;
Al-Sabi A., Shamotienko O., Dhochartaigh S.N., Muniyappa N.,
Le Berre M., Shaban H., Wang J., Sack J.T., Dolly J.O.;
"Arrangement of Kv1 alpha subunits dictates sensitivity to
tetraethylammonium.";
J. Gen. Physiol. 136:273-282(2010).
[34]
FUNCTION, INTERACTION WITH ADAM22 AND DLG4, SUBCELLULAR LOCATION,
IDENTIFICATION BY MASS SPECTROMETRY, AND TISSUE SPECIFICITY.
PubMed=20089912; DOI=10.1523/JNEUROSCI.4661-09.2010;
Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E.,
Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.;
"ADAM22, a Kv1 channel-interacting protein, recruits membrane-
associated guanylate kinases to juxtaparanodes of myelinated axons.";
J. Neurosci. 30:1038-1048(2010).
[35]
FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT
TYR-458, AND MUTAGENESIS OF TYR-458.
PubMed=21602278; DOI=10.1074/jbc.M111.219113;
Gu C., Gu Y.;
"Clustering and activity tuning of Kv1 channels in myelinated
hippocampal axons.";
J. Biol. Chem. 286:25835-25847(2011).
[36]
FUNCTION.
PubMed=21647367; DOI=10.1371/journal.pone.0020402;
Martel P., Leo D., Fulton S., Berard M., Trudeau L.E.;
"Role of Kv1 potassium channels in regulating dopamine release and
presynaptic D2 receptor function.";
PLoS ONE 6:E20402-E20402(2011).
[37]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440; SER-441 AND
SER-468, 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).
[38]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF VAL-381.
PubMed=23725331; DOI=10.1042/BJ20130297;
Al-Sabi A., Kaza S.K., Dolly J.O., Wang J.;
"Pharmacological characteristics of Kv1.1- and Kv1.2-containing
channels are influenced by the stoichiometry and positioning of their
alpha subunits.";
Biochem. J. 454:101-108(2013).
[39]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION IN A
COMPLEX WITH KCNA1 AND KCNAB2.
PubMed=23318870; DOI=10.1113/jphysiol.2012.249706;
Ovsepian S.V., Steuber V., Le Berre M., O'Hara L., O'Leary V.B.,
Dolly J.O.;
"A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking
and regulates the output of deep cerebellar nuclear neurons to
thalamic targets.";
J. Physiol. (Lond.) 591:1771-1791(2013).
[40]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=24472174; DOI=10.1186/1744-8069-10-8;
Fan L., Guan X., Wang W., Zhao J.Y., Zhang H., Tiwari V.,
Hoffman P.N., Li M., Tao Y.X.;
"Impaired neuropathic pain and preserved acute pain in rats
overexpressing voltage-gated potassium channel subunit Kv1.2 in
primary afferent neurons.";
Mol. Pain 10:8-8(2014).
[41]
SITE VAL-381.
PubMed=25514171; DOI=10.1016/j.bcp.2014.12.002;
Wang X., Umetsu Y., Gao B., Ohki S., Zhu S.;
"Mesomartoxin, a new K(v)1.2-selective scorpion toxin interacting with
the channel selectivity filter.";
Biochem. Pharmacol. 93:232-239(2015).
[42]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-119 OF WILD-TYPE AND
MUTANT VAL-46, FUNCTION, SUBUNIT, REGION, DOMAIN, AND MUTAGENESIS OF
ARG-34; ASN-38; SER-40; GLY-41; LEU-42; ARG-43; PHE-44; GLU-45;
THR-46; GLN-47; THR-50; ASP-70; ARG-73; GLU-75; PHE-77; ASP-79;
ASN-81; ARG-82; ASP-86; LEU-89; TYR-90; GLN-93; ARG-97; ARG-99;
VAL-102; ASN-103; PRO-105; ASP-107; ILE-108 AND GLU-111.
PubMed=11007484; DOI=10.1016/S0092-8674(00)00088-X;
Minor D.L. Jr., Lin Y.-F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y.,
Berger J.M.;
"The polar T1 interface is linked to conformational changes that open
the voltage-gated potassium channel.";
Cell 102:657-670(2000).
[43]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2,
SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, AND INTERACTION WITH KCNAB2.
PubMed=16002581; DOI=10.1126/science.1116269;
Long S.B., Campbell E.B., Mackinnon R.;
"Crystal structure of a mammalian voltage-dependent Shaker family K+
channel.";
Science 309:897-903(2005).
[44]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, AND
DOMAIN.
PubMed=16002579; DOI=10.1126/science.1116270;
Long S.B., Campbell E.B., Mackinnon R.;
"Voltage sensor of Kv1.2: structural basis of electromechanical
coupling.";
Science 309:903-908(2005).
[45]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN
COMPLEX WITH KCNAB2, FUNCTION, SUBUNIT, INTERACTION WITH KCNAB2,
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=18004376; DOI=10.1038/nature06265;
Long S.B., Tao X., Campbell E.B., MacKinnon R.;
"Atomic structure of a voltage-dependent K+ channel in a lipid
membrane-like environment.";
Nature 450:376-382(2007).
[46]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH KCNAB2,
INTERACTION WITH KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=20534430; DOI=10.1073/pnas.1000142107;
Chen X., Wang Q., Ni F., Ma J.;
"Structure of the full-length Shaker potassium channel Kv1.2 by
normal-mode-based X-ray crystallographic refinement.";
Proc. Natl. Acad. Sci. U.S.A. 107:11352-11357(2010).
[47]
X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-266 AND 303-499 IN COMPLEX
WITH KCNAB2, SUBUNIT, INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION,
AND TOPOLOGY.
PubMed=20360102; DOI=10.1126/science.1185954;
Tao X., Lee A., Limapichat W., Dougherty D.A., MacKinnon R.;
"A gating charge transfer center in voltage sensors.";
Science 328:67-73(2010).
[48]
X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN
COMPLEX WITH KCNAB2 AND CHARYBDOTOXIN, INTERACTION WITH KCNAB2,
SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=23705070; DOI=10.7554/eLife.00594;
Banerjee A., Lee A., Campbell E., Mackinnon R.;
"Structure of a pore-blocking toxin in complex with a eukaryotic
voltage-dependent K(+) channel.";
Elife 2:E00594-E00594(2013).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain and the central nervous system, but also in
the cardiovascular system. Prevents aberrant action potential
firing and regulates neuronal output. 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:12151401, PubMed:21602278,
PubMed:24472174). Can form functional homotetrameric channels and
heterotetrameric channels that contain variable proportions of
KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other
family members as well; channel properties depend on the type of
alpha subunits that are part of the channel (PubMed:8495559,
PubMed:15618540, PubMed:20805574, PubMed:23725331). Channel
properties are modulated by cytoplasmic beta subunits that
regulate the subcellular location of the alpha subunits and
promote rapid inactivation of delayed rectifier potassium channels
(PubMed:18003609, PubMed:19713757). In vivo, membranes probably
contain a mixture of heteromeric potassium channel complexes,
making it difficult to assign currents observed in intact tissues
to a particular potassium channel family member. Homotetrameric
KCNA2 forms a delayed-rectifier potassium channel that opens in
response to membrane depolarization, followed by slow spontaneous
channel closure (PubMed:1715584, PubMed:16770729, PubMed:17766348,
PubMed:18003609, PubMed:18638484, PubMed:19713757,
PubMed:20089912). In contrast, a heteromultimer formed by KCNA2
and KCNA4 shows rapid inactivation (PubMed:8495559). Response to
toxins that are selective for KCNA1, respectively for KCNA2,
suggests that heteromeric potassium channels composed of both
KCNA1 and KCNA2 play a role in pacemaking and regulate the output
of deep cerebellar nuclear neurons (PubMed:23318870). KCNA2-
containing channels play a presynaptic role and prevent
hyperexcitability and aberrant action potential firing
(PubMed:12777451). Response to toxins that are selective for
KCNA2-containing potassium channels suggests that in Purkinje
cells, dendritic subthreshold KCNA2-containing potassium channels
prevent random spontaneous calcium spikes, suppressing dendritic
hyperexcitability without hindering the generation of somatic
action potentials, and thereby play an important role in motor
coordination (PubMed:16210348). Plays a role in the induction of
long-term potentiation of neuron excitability in the CA3 layer of
the hippocampus (By similarity). May function as down-stream
effector for G protein-coupled receptors and inhibit GABAergic
inputs to basolateral amygdala neurons (PubMed:16306173). May
contribute to the regulation of neurotransmitter release, such as
gamma-aminobutyric acid (GABA) (PubMed:17869444). Contributes to
the regulation of the axonal release of the neurotransmitter
dopamine (PubMed:21647367). Reduced KCNA2 expression plays a role
in the perception of neuropathic pain after peripheral nerve
injury, but not acute pain (PubMed:24472174). Plays a role in the
regulation of the time spent in non-rapid eye movement (NREM)
sleep (By similarity). {ECO:0000250|UniProtKB:P63141,
ECO:0000269|PubMed:11007484, ECO:0000269|PubMed:12151401,
ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12777451,
ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:16210348,
ECO:0000269|PubMed:16770729, ECO:0000269|PubMed:1715584,
ECO:0000269|PubMed:17766348, ECO:0000269|PubMed:18003609,
ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:18638484,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:20805574,
ECO:0000269|PubMed:21602278, ECO:0000269|PubMed:23318870,
ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2555158,
ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:8495559,
ECO:0000305, ECO:0000305|PubMed:12177193,
ECO:0000305|PubMed:16306173, ECO:0000305|PubMed:17869444,
ECO:0000305|PubMed:21647367}.
-!- ENZYME REGULATION: Inhibited by 4-aminopyridine (4-AP),
dendrotoxin (DTX) and charybdotoxin (CTX), but not by
tetraethylammonium (TEA) (PubMed:2555158, PubMed:8495559,
PubMed:18638484). Inhibited by tityustoxin-K alpha (TsTX-Kalpha),
a toxin that is highly specific for KCNA2 (PubMed:8355670).
Inhibited by maurotoxin (PubMed:24472174). Inhibited by kappaM
conotoxins kappaM-RIIIJ and kappaM-RIIIK (By similarity).
{ECO:0000250|UniProtKB:P16389, ECO:0000269|PubMed:18638484,
ECO:0000269|PubMed:20805574, ECO:0000269|PubMed:24472174,
ECO:0000269|PubMed:2555158, ECO:0000269|PubMed:8355670,
ECO:0000269|PubMed:8495559}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few
msec, but inactivation is very slow, with only a marginal
decrease in conductance over several seconds. The voltage-
dependence of activation and inactivation and other channel
characteristics vary depending on the experimental conditions,
the expression system, post-translational modifications and the
presence or absence of ancillary subunits. For the activation of
homotetrameric channels expressed in xenopus oocytes, the
voltage at half-maximal amplitude is about -34 mV
(PubMed:2555158). Unit channel conductance is about 10 pS
(PubMed:2555158). For the activation of homotetrameric channels
expressed in Chinese hamster ovary (CHO) cells, the voltage at
half-maximal amplitude is about -10 mV (PubMed:17324383).
{ECO:0000269|PubMed:17324383, ECO:0000269|PubMed:2555158};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and
KCNA7 (PubMed:8495559, PubMed:8361540, PubMed:10896669,
PubMed:12777451, PubMed:12632190, PubMed:15618540,
PubMed:11007484, PubMed:16002581, PubMed:18004376,
PubMed:20534430). Channel activity is regulated by interaction
with beta subunits, including KCNAB1 and KCNAB2 (PubMed:18003609,
PubMed:19713757, PubMed:16002581, PubMed:18004376,
PubMed:20534430, PubMed:20360102, PubMed:23705070). Identified in
a complex with KCNA1 and KCNAB2 (PubMed:11086297,
PubMed:23318870). Identified in a complex with KCNA5 and KCNAB1
(By similarity). Identified in a complex with KCNA4 and FYN (By
similarity). Interacts (via C-terminus) with the PDZ domains of
DLG1 and DLG2 (PubMed:7477295). Interacts with DLG4 (via PDZ
domain) (PubMed:7477295, PubMed:20089912). Interacts with PTK2B
(PubMed:11739373). Interacts (via C-terminus) with CTTN
(PubMed:12151401). Interacts (via N-terminal cytoplasmic domain)
with RHOA (GTP-bound form); this regulates channel activity by
reducing location at the cell surface in response to CHRM1
activation (PubMed:9635436). Interacts with DRD2 (By similarity).
Interacts with SIGMAR1; cocaine consumption leads to increased
interaction (By similarity). Interacts with CNTNAP2
(PubMed:10624965). Interacts with ADAM22 (PubMed:20089912).
{ECO:0000250|UniProtKB:P63141, ECO:0000250|UniProtKB:Q09081,
ECO:0000269|PubMed:10624965, ECO:0000269|PubMed:10896669,
ECO:0000269|PubMed:11007484, ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:11739373, ECO:0000269|PubMed:12151401,
ECO:0000269|PubMed:12632190, ECO:0000269|PubMed:15618540,
ECO:0000269|PubMed:16002581, ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:19713757, ECO:0000269|PubMed:20089912,
ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430,
ECO:0000269|PubMed:23318870, ECO:0000269|PubMed:23705070,
ECO:0000269|PubMed:7477295, ECO:0000269|PubMed:8361540,
ECO:0000269|PubMed:8495559, ECO:0000269|PubMed:9635436,
ECO:0000305}.
-!- INTERACTION:
P78352:DLG4 (xeno); NbExp=2; IntAct=EBI-631446, EBI-80389;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10896669,
ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:14713306,
ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:16770729,
ECO:0000269|PubMed:1715584, ECO:0000269|PubMed:17766348,
ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:20089912,
ECO:0000269|PubMed:20805574, ECO:0000269|PubMed:21602278,
ECO:0000269|PubMed:23318870, ECO:0000269|PubMed:23725331,
ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2555158,
ECO:0000269|PubMed:7544443, ECO:0000269|PubMed:9635436,
ECO:0000305|PubMed:11086297}; Multi-pass membrane protein
{ECO:0000269|PubMed:12151401, ECO:0000269|PubMed:16002581,
ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430, ECO:0000269|PubMed:23705070,
ECO:0000305}. Membrane {ECO:0000269|PubMed:10624965,
ECO:0000269|PubMed:16002581, ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:18638484, ECO:0000269|PubMed:20089912,
ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430,
ECO:0000269|PubMed:23705070, ECO:0000269|PubMed:8361540}. Cell
projection, axon {ECO:0000269|PubMed:10624965,
ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12777451,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:21602278,
ECO:0000269|PubMed:8361540}. Cell junction, synapse
{ECO:0000269|PubMed:8361540}. Cell junction, synapse, synaptosome
{ECO:0000250|UniProtKB:P63141}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000250|UniProtKB:P63141}. Cell
projection, dendrite {ECO:0000250|UniProtKB:P63141}. Endoplasmic
reticulum membrane {ECO:0000269|PubMed:10896669}. Cell projection,
lamellipodium membrane {ECO:0000269|PubMed:12151401}. Endosome
{ECO:0000269|PubMed:19403695}. Perikaryon
{ECO:0000269|PubMed:23318870}. Cell junction, paranodal septate
junction {ECO:0000250|UniProtKB:P63141}. Note=KCNA2 by itself is
detected both at the endoplasmic reticulum and at the cell
membrane. Coexpression with KCNA4 or with beta subunits promotes
expression at the cell membrane (PubMed:10896669, PubMed:16770729,
PubMed:18003609). Coexpression with KCNA1 inhibits cell surface
expression (PubMed:10896669). Surface levels are regulated both by
steady-state and stimulus-induced clathrin-dependent endocytosis
(PubMed:19403695). Expression at the cell surface is down-
regulated in response to CHRM1 activation (PubMed:9635436).
Expression at the cell surface is increased in response to the
activation of beta-adrenergic receptors and increased cAMP levels
(PubMed:18003609). Detected on presynaptic and postsynaptic axon
segments (PubMed:12777451). In myelinated peripheral axons,
clustered in the juxtaparadonal region and at an internodal line
located along the mesaxon and below the Schmidt-Lanterman
incisures (By similarity). {ECO:0000250|UniProtKB:P63141,
ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:12777451,
ECO:0000269|PubMed:16770729, ECO:0000269|PubMed:18003609,
ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:9635436}.
-!- TISSUE SPECIFICITY: Detected in neurons in dorsal root ganglion
(PubMed:24472174). Detected in hippocampus neurons
(PubMed:21602278). Detected on neurons of the anteroventral
cochlear nucleus (PubMed:12777451). Detected in renal arteries
(PubMed:12632190). Detected in neurons of the medial nucleus of
the trapezoid body (PubMed:12177193). Detected in neurons in the
brain cortex (PubMed:14713306). Detected in axon tracts of the
corpus callosum, specific terminal fields of the brain cortex
neuropil, neurons in the medial entorhinal cortex, and in puncta
representing mossy fiber terminals in the hippocampus mossy fiber
tract; these puncta correspond to synapses made by dentate granule
cells (PubMed:8361540). Detected in paranodal and juxtanodal zones
in the central nervous system, including myelinated spinal cord
(PubMed:11086297, PubMed:20089912). Detected in the juxtaparanodal
region in optic nerve (PubMed:10624965). Detected at nerve
terminal plexuses of basket cells in the cerebellum (at protein
level) (PubMed:7477295, PubMed:20089912). Detected in brain
(PubMed:2722779). Detected in heart atrium and ventricle
(PubMed:1715584). Detected in renal arteries (PubMed:12632190).
{ECO:0000269|PubMed:10624965, ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12632190,
ECO:0000269|PubMed:14713306, ECO:0000269|PubMed:1715584,
ECO:0000269|PubMed:20089912, ECO:0000269|PubMed:21602278,
ECO:0000269|PubMed:24472174, ECO:0000269|PubMed:2722779,
ECO:0000269|PubMed:7477295, ECO:0000269|PubMed:8361540}.
-!- INDUCTION: Up-regulated in brain cortex in response to ischemia
(at protein level) (PubMed:14713306). Down-regulated in dorsal
root ganglion neurons after peripheral nerve injury (at protein
level) (PubMed:24472174). Down-regulated in pulmonary artery
myocytes in response to chronic moderate hypoxia.
{ECO:0000269|PubMed:14713306, ECO:0000269|PubMed:15151918,
ECO:0000269|PubMed:24472174}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization. Interactions between the different subunits
modulate the gating characteristics (PubMed:11007484). Besides,
the cytoplasmic N-terminal domain mediates interaction with RHOA
and thus is required for RHOA-mediated endocytosis
(PubMed:9635436). {ECO:0000269|PubMed:11007484,
ECO:0000269|PubMed:19403695, ECO:0000269|PubMed:9635436}.
-!- 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:0000305|PubMed:16002579, ECO:0000305|PubMed:20360102}.
-!- PTM: Phosphorylated on tyrosine residues; phosphorylation
increases in response to ischemia (PubMed:14713306).
Phosphorylated on tyrosine residues by activated PTK2B/PYK2
(PubMed:7544443). Phosphorylation on tyrosine residues suppresses
ion channel activity (PubMed:7544443). Phosphorylated on tyrosine
residues in response to CHRM1 activation; this abolishes
interaction with CTTN (PubMed:12151401). This is probably due to
endocytosis of the phosphorylated channel subunits. Phosphorylated
on serine residues in response to increased cAMP levels;
phosphorylation is apparently not catalyzed by PKA
(PubMed:18003609). {ECO:0000269|PubMed:12151401,
ECO:0000269|PubMed:14713306, ECO:0000269|PubMed:18003609,
ECO:0000269|PubMed:7544443}.
-!- PTM: N-glycosylated, with complex, sialylated N-glycans.
{ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:16770729}.
-!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
pyramidal neurons is probably mediated by potassium channels
containing KCNA2 plus KCNA1 or other family members. It is
activated at about -50 mV, i.e. below the action potential
threshold, and is characterized by slow inactivation, extremely
slow recovery from inactivation, sensitivity to dendrotoxin (DTX)
and to 4-aminopyridine (4-AP). {ECO:0000305|PubMed:17917103}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
(TC 1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04731; AAA40819.1; -; mRNA.
EMBL; X16003; CAA34134.1; -; mRNA.
EMBL; M74449; AAA19867.1; -; mRNA.
PIR; A33814; A33814.
RefSeq; NP_037102.1; NM_012970.3.
RefSeq; XP_006233194.1; XM_006233132.3.
RefSeq; XP_006233195.1; XM_006233133.3.
RefSeq; XP_006233196.1; XM_006233134.3.
RefSeq; XP_006233197.1; XM_006233135.3.
RefSeq; XP_008759593.1; XM_008761371.2.
UniGene; Rn.10298; -.
UniGene; Rn.40779; -.
PDB; 1DSX; X-ray; 1.60 A; A/B/C/D/E/F/G/H=33-119.
PDB; 1QDV; X-ray; 1.60 A; A/B/C/D=33-131.
PDB; 1QDW; X-ray; 2.10 A; A/B/C/D/E/F/G/H=33-119.
PDB; 2A79; X-ray; 2.90 A; B=1-499.
PDB; 2R9R; X-ray; 2.40 A; B/H=1-499.
PDB; 3LNM; X-ray; 2.90 A; B/D=1-266, B/D=303-499.
PDB; 3LUT; X-ray; 2.90 A; B=1-499.
PDB; 4JTA; X-ray; 2.50 A; B/Q=1-266, B/Q=304-499.
PDB; 4JTC; X-ray; 2.56 A; B/H=1-266, B/H=304-499.
PDB; 4JTD; X-ray; 2.54 A; B/H=1-266, B/H=304-499.
PDB; 5WIE; X-ray; 3.30 A; B/H=1-42.
PDBsum; 1DSX; -.
PDBsum; 1QDV; -.
PDBsum; 1QDW; -.
PDBsum; 2A79; -.
PDBsum; 2R9R; -.
PDBsum; 3LNM; -.
PDBsum; 3LUT; -.
PDBsum; 4JTA; -.
PDBsum; 4JTC; -.
PDBsum; 4JTD; -.
PDBsum; 5WIE; -.
ProteinModelPortal; P63142; -.
SMR; P63142; -.
BioGrid; 247501; 5.
CORUM; P63142; -.
IntAct; P63142; 3.
STRING; 10116.ENSRNOP00000042653; -.
GuidetoPHARMACOLOGY; 539; -.
iPTMnet; P63142; -.
PhosphoSitePlus; P63142; -.
PaxDb; P63142; -.
PRIDE; P63142; -.
Ensembl; ENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
Ensembl; ENSRNOT00000092365; ENSRNOP00000075841; ENSRNOG00000018285.
Ensembl; ENSRNOT00000092450; ENSRNOP00000075852; ENSRNOG00000018285.
GeneID; 25468; -.
KEGG; rno:25468; -.
CTD; 3737; -.
RGD; 2950; Kcna2.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; P63142; -.
KO; K04875; -.
OMA; PEPDHEC; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; P63142; -.
TreeFam; TF313103; -.
Reactome; R-RNO-1296072; Voltage gated Potassium channels.
EvolutionaryTrace; P63142; -.
PRO; PR:P63142; -.
Proteomes; UP000002494; Chromosome 2.
Bgee; ENSRNOG00000018285; -.
ExpressionAtlas; P63142; baseline and differential.
Genevisible; P63142; RN.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IMP:UniProtKB.
GO; GO:0019894; F:kinesin binding; IPI:RGD.
GO; GO:0015271; F:outward rectifier potassium channel activity; IMP:RGD.
GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
GO; GO:0021633; P:optic nerve structural organization; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0051259; P:protein complex oligomerization; IMP:RGD.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; IMP:UniProtKB.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR004049; K_chnl_volt-dep_Kv1.2.
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.
PANTHER; PTHR11537:SF23; PTHR11537:SF23; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01509; KV12CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
3D-structure; Cell junction; Cell membrane; Cell projection;
Complete proteome; Endoplasmic reticulum; Endosome; Glycoprotein;
Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Potassium; Potassium channel; Potassium transport;
Reference proteome; Synapse; Synaptosome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 499 Potassium voltage-gated channel subfamily
A member 2.
/FTId=PRO_0000053975.
TOPO_DOM 1 160 Cytoplasmic.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TRANSMEM 161 182 Helical; Name=Segment S1.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 183 221 Extracellular.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430,
ECO:0000305|PubMed:12151401}.
TRANSMEM 222 243 Helical; Name=Segment S2.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 244 254 Cytoplasmic.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TRANSMEM 255 275 Helical; Name=Segment S3.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 276 289 Extracellular.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TRANSMEM 290 310 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 311 325 Cytoplasmic.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TRANSMEM 326 347 Helical; Name=Segment S5.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 348 361 Extracellular.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
INTRAMEM 362 373 Helical; Name=Pore helix.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
INTRAMEM 374 381 {ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 382 388 Extracellular.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TRANSMEM 389 417 Helical; Name=Segment S6.
{ECO:0000269|PubMed:18004376,
ECO:0000269|PubMed:20360102,
ECO:0000269|PubMed:20534430}.
TOPO_DOM 418 499 Cytoplasmic.
{ECO:0000269|PubMed:12151401,
ECO:0000305}.
REGION 1 125 Tetramerization domain.
{ECO:0000305|PubMed:11007484}.
REGION 312 325 S4-S5 linker.
{ECO:0000305|PubMed:16002579}.
MOTIF 374 379 Selectivity filter. {ECO:0000305}.
MOTIF 497 499 PDZ-binding.
{ECO:0000269|PubMed:7477295}.
SITE 252 252 Important for normal, slow channel
gating. {ECO:0000269|PubMed:17766348}.
SITE 381 381 Important for binding with the scorpion
mesomartoxin; when the scorpion
mesomartoxin-rKv1.2/KCNA2 interaction is
modeled, this residue is close to the 'Y-
57' residue of the toxin.
{ECO:0000305|PubMed:25514171}.
MOD_RES 429 429 Phosphotyrosine.
{ECO:0000250|UniProtKB:P63141}.
MOD_RES 434 434 Phosphoserine.
{ECO:0000250|UniProtKB:P63141}.
MOD_RES 440 440 Phosphoserine.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:18003609}.
MOD_RES 441 441 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000269|PubMed:18003609,
ECO:0000269|PubMed:21602278}.
MOD_RES 458 458 Phosphotyrosine.
{ECO:0000305|PubMed:21602278}.
MOD_RES 468 468 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
LIPID 244 244 S-palmitoyl cysteine. {ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255,
ECO:0000269|PubMed:16770729}.
MUTAGEN 34 34 R->L: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 38 38 N->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 40 40 S->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 41 41 G->A: Loss of channel activity.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 42 42 L->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 43 43 R->L: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 44 44 F->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 45 45 E->A: Loss of channel activity.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 46 46 T->D: Impairs protein folding. Loss of
tetramerization.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 46 46 T->V,A: No effect on tetramerization.
Alters voltage-sensitive channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 46 46 T->V: Abolishes interaction with KCNAB2
and strongly reduces cell surface
expression. No effect phosphorylation in
response to increased cAMP levels.
{ECO:0000269|PubMed:18003609}.
MUTAGEN 47 47 Q->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 50 50 T->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 70 70 D->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 73 73 R->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 75 75 E->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 77 77 F->W: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 79 79 D->N: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 81 81 N->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 82 82 R->A: Loss of channel activity.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 86 86 D->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 89 89 L->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 90 90 Y->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 93 93 Q->A: Loss of channel activity.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 97 97 R->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 99 99 R->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 102 102 V->T: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 103 103 N->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 105 105 P->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 107 107 D->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 108 108 I->A: No effect on channel opening.
{ECO:0000269|PubMed:11007484}.
MUTAGEN 111 111 E->A: Alters voltage-sensitive channel
opening. {ECO:0000269|PubMed:11007484}.
MUTAGEN 207 207 N->Q: Loss of glycosylation site.
{ECO:0000269|PubMed:16770729}.
MUTAGEN 252 252 T->R: Changes channel gating from a
predominantly slow mode to a much more
rapid mode.
{ECO:0000269|PubMed:17766348}.
MUTAGEN 267 302 FITLGTELAEKPEDAQQGQQAMSLAILRVIRLVRVF->YVT
IFLTESNKSVLQFQNVRRVVQIFRIM: In paddle
chimera; changes channel activation to
less negative voltage values and renders
the channel susceptible to inhibition by
the spider toxin VsTx1.
{ECO:0000269|PubMed:18638484}.
MUTAGEN 356 356 S->A: Impairs N-glycosylation and
abolishes expression at the cell surface.
{ECO:0000269|PubMed:16770729}.
MUTAGEN 360 360 S->A: No effect on N-glycosylation.
Abolishes channel activity of the
homotetramer, but retains channel
activity in the presence of a beta
subunit. {ECO:0000269|PubMed:16770729}.
MUTAGEN 381 381 V->Y: Confers sensitivity to inhibition
by tetraethylammonium (TEA).
{ECO:0000269|PubMed:23725331}.
MUTAGEN 383 383 T->A: Impairs N-glycosylation and
abolishes expression at the cell surface.
{ECO:0000269|PubMed:16770729}.
MUTAGEN 415 415 Y->F: Nearly abolishes interaction with
CTTN; when associated with F-417.
{ECO:0000269|PubMed:12151401}.
MUTAGEN 417 417 Y->F: Nearly abolishes interaction with
CTTN; when associated with F-415.
Strongly reduces channel activity.
{ECO:0000269|PubMed:12151401}.
MUTAGEN 440 440 S->A: Strongly reduces cell surface
expression. Abolishes phosphorylation in
response to increased cAMP levels.
{ECO:0000269|PubMed:18003609}.
MUTAGEN 449 449 S->A: Strongly reduces cell surface
expression. Abolishes phosphorylation in
response to increased cAMP levels.
{ECO:0000269|PubMed:18003609}.
MUTAGEN 458 458 Y->A: Impairs clustering on axon
membranes. {ECO:0000269|PubMed:21602278}.
CONFLICT 411 411 S -> F (in Ref. 4; AAA19867).
{ECO:0000305}.
STRAND 34 39 {ECO:0000244|PDB:1DSX}.
STRAND 42 47 {ECO:0000244|PDB:1DSX}.
HELIX 48 52 {ECO:0000244|PDB:1DSX}.
TURN 58 60 {ECO:0000244|PDB:1DSX}.
HELIX 62 66 {ECO:0000244|PDB:1DSX}.
TURN 71 74 {ECO:0000244|PDB:1DSX}.
STRAND 75 78 {ECO:0000244|PDB:1DSX}.
TURN 82 84 {ECO:0000244|PDB:1QDW}.
HELIX 85 93 {ECO:0000244|PDB:1DSX}.
HELIX 106 116 {ECO:0000244|PDB:1DSX}.
HELIX 120 130 {ECO:0000244|PDB:1QDV}.
TURN 143 145 {ECO:0000244|PDB:4JTA}.
HELIX 146 149 {ECO:0000244|PDB:4JTA}.
TURN 150 154 {ECO:0000244|PDB:4JTA}.
STRAND 156 158 {ECO:0000244|PDB:4JTC}.
HELIX 160 182 {ECO:0000244|PDB:4JTA}.
HELIX 186 189 {ECO:0000244|PDB:4JTA}.
STRAND 190 192 {ECO:0000244|PDB:4JTA}.
TURN 193 196 {ECO:0000244|PDB:4JTA}.
HELIX 202 210 {ECO:0000244|PDB:4JTA}.
HELIX 221 241 {ECO:0000244|PDB:4JTA}.
TURN 249 252 {ECO:0000244|PDB:4JTA}.
HELIX 254 261 {ECO:0000244|PDB:4JTA}.
HELIX 279 282 {ECO:0000244|PDB:3LUT}.
HELIX 283 287 {ECO:0000244|PDB:5WIE}.
HELIX 291 299 {ECO:0000244|PDB:2A79}.
HELIX 305 309 {ECO:0000244|PDB:4JTA}.
HELIX 312 323 {ECO:0000244|PDB:4JTA}.
HELIX 325 351 {ECO:0000244|PDB:4JTA}.
HELIX 361 372 {ECO:0000244|PDB:4JTA}.
STRAND 378 380 {ECO:0000244|PDB:4JTA}.
HELIX 385 403 {ECO:0000244|PDB:4JTA}.
HELIX 406 418 {ECO:0000244|PDB:4JTA}.
SEQUENCE 499 AA; 56701 MW; A8FEA6F3F59AF42A CRC64;
MTVATGDPVD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG
DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE
EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF
CLETLPIFRD ENEDMHGGGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR
FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERDSQFPS
IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE
TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA
NCTLANTNYV NITKMLTDV


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