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Potassium voltage-gated channel subfamily A member 1 (RBKI) (RCK1) (Voltage-gated potassium channel subunit Kv1.1)

 KCNA1_RAT               Reviewed;         495 AA.
P10499;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
01-APR-1990, sequence version 1.
28-FEB-2018, entry version 163.
RecName: Full=Potassium voltage-gated channel subfamily A member 1;
AltName: Full=RBKI {ECO:0000303|PubMed:2539643};
AltName: Full=RCK1 {ECO:0000303|PubMed:2348860, ECO:0000303|PubMed:8038169};
AltName: Full=Voltage-gated potassium channel subunit Kv1.1;
Name=Kcna1;
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].
TISSUE=Brain;
PubMed=3191911;
Baumann A., Grupe A., Ackermann A., Pongs O.;
"Structure of the voltage-dependent potassium channel is highly
conserved from Drosophila to vertebrate central nervous systems.";
EMBO J. 7:2457-2463(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
TISSUE=Brain;
PubMed=2539643; DOI=10.1126/science.2539643;
Christie M.J., Adelman J.P., Douglass J., North R.A.;
"Expression of a cloned rat brain potassium channel in Xenopus
oocytes.";
Science 244:221-224(1989).
[3]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=2348860; DOI=10.1038/345535a0;
Ruppersberg J.P., Schroeter K.H., Sakmann B., Stocker M., Sewing S.,
Pongs O.;
"Heteromultimeric channels formed by rat brain potassium-channel
proteins.";
Nature 345:535-537(1990).
[4]
FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, PHOSPHORYLATION AT
SER-446, AND MUTAGENESIS OF ARG-443 AND SER-446.
PubMed=8038169; DOI=10.1021/bi00195a021;
Ivanina T., Perets T., Thornhill W.B., Levin G., Dascal N., Lotan I.;
"Phosphorylation by protein kinase A of RCK1 K+ channels expressed in
Xenopus oocytes.";
Biochemistry 33:8786-8792(1994).
[5]
RNA EDITING OF POSITION 400.
PubMed=12907802; DOI=10.1126/science.1086763;
Hoopengardner B., Bhalla T., Staber C., Reenan R.;
"Nervous system targets of RNA editing identified by comparative
genomics.";
Science 301:832-836(2003).
[6]
INTERACTION WITH KCNAB1 AND KCNAB2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=9334400;
Rhodes K.J., Strassle B.W., Monaghan M.M., Bekele-Arcuri Z.,
Matos M.F., Trimmer J.S.;
"Association and colocalization of the Kvbeta1 and Kvbeta2 beta-
subunits with Kv1 alpha-subunits in mammalian brain K+ channel
complexes.";
J. Neurosci. 17:8246-8258(1997).
[7]
SUBUNIT, INTERACTION WITH KCNA2 AND KCNA4, SUBCELLULAR LOCATION, 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).
[8]
INTERACTION WITH KCNA2 AND KCNA4, SUBUNIT, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
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).
[9]
INTERACTION WITH STX1A; GNB1 AND GNG2, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=12114518; DOI=10.1074/jbc.M203943200;
Michaelevski I., Chikvashvili D., Tsuk S., Fili O., Lohse M.J.,
Singer-Lahat D., Lotan I.;
"Modulation of a brain voltage-gated K+ channel by syntaxin 1A
requires the physical interaction of Gbetagamma with the channel.";
J. Biol. Chem. 277:34909-34917(2002).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[11]
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).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=12681381; DOI=10.1016/S0028-3908(03)00070-4;
Winklhofer M., Matthias K., Seifert G., Stocker M., Sewing S.,
Herget T., Steinhaeuser C., Saaler-Reinhardt S.;
"Analysis of phosphorylation-dependent modulation of Kv1.1 potassium
channels.";
Neuropharmacology 44:829-842(2003).
[13]
INTERACTION WITH DLG1; DLG2 AND DLG4.
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).
[14]
FUNCTION, AND TISSUE SPECIFICITY.
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).
[15]
INTERACTION WITH LGI1; KCNA4 AND KCNAB1.
PubMed=16504945; DOI=10.1016/j.neuron.2006.01.033;
Schulte U., Thumfart J.-O., Kloecker N., Sailer C.A., Bildl W.,
Biniossek M., Dehn D., Deller T., Eble S., Abbass K., Wangler T.,
Knaus H.-G., Fakler B.;
"The epilepsy-linked Lgi1 protein assembles into presynaptic Kv1
channels and inhibits inactivation by Kvbeta1.";
Neuron 49:697-706(2006).
[16]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17855588; DOI=10.1152/jn.00437.2007;
Chi X.X., Nicol G.D.;
"Manipulation of the potassium channel Kv1.1 and its effect on
neuronal excitability in rat sensory neurons.";
J. Neurophysiol. 98:2683-2692(2007).
[17]
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).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
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).
[19]
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).
[20]
TISSUE SPECIFICITY.
PubMed=21483673; DOI=10.1371/journal.pone.0018213;
Ma Z., Lavebratt C., Almgren M., Portwood N., Forsberg L.E.,
Branstrom R., Berglund E., Falkmer S., Sundler F., Wierup N.,
Bjorklund A.;
"Evidence for presence and functional effects of Kv1.1 channels in
beta-cells: general survey and results from mceph/mceph mice.";
PLoS ONE 6:E18213-E18213(2011).
[21]
FUNCTION, MUTAGENESIS OF SER-309, SUBCELLULAR LOCATION, AND
MISCELLANEOUS.
PubMed=22206926; DOI=10.1016/j.brainres.2011.11.023;
Ishida S., Sakamoto Y., Nishio T., Baulac S., Kuwamura M., Ohno Y.,
Takizawa A., Kaneko S., Serikawa T., Mashimo T.;
"Kcna1-mutant rats dominantly display myokymia, neuromyotonia and
spontaneous epileptic seizures.";
Brain Res. 1435:154-166(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-437 AND SER-439,
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).
[23]
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
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).
[24]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND IDENTIFICATION IN A
COMPLEX WITH KCNA2 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).
[25]
MUTAGENESIS OF ALA-352; HIS-355; SER-357; TYR-379 AND 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).
[26]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 29-128, INTERACTION WITH
KCNAB2, TETRAMERIZATION, SUBUNIT, AND DOMAIN.
PubMed=10884227; DOI=10.1126/science.289.5476.123;
Gulbis J.M., Zhou M., Mann S., MacKinnon R.;
"Structure of the cytoplasmic beta subunit-T1 assembly of voltage-
dependent K+ channels.";
Science 289:123-127(2000).
-!- 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 kidney. Contributes to the regulation of the membrane
potential and nerve signaling, and prevents neuronal
hyperexcitability (PubMed:12177193, PubMed:17855588,
PubMed:22206926). Forms tetrameric potassium-selective channels
through which potassium ions pass in accordance with their
electrochemical gradient (PubMed:23725331). The channel alternates
between opened and closed conformations in response to the voltage
difference across the membrane (PubMed:2539643). 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:2348860, PubMed:12177193, PubMed:10896669,
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:10896669, PubMed:12114518). In vivo,
membranes probably contain a mixture of heteromeric potassium
channel complexes, making it difficult to assign currents observed
in intact tissues to any particular potassium channel family
member. Homotetrameric KCNA1 forms a delayed-rectifier potassium
channel that opens in response to membrane depolarization,
followed by slow spontaneous channel closure (PubMed:2348860,
PubMed:8038169, PubMed:12681381, PubMed:22206926,
PubMed:23725331). In contrast, a heterotetrameric channel formed
by KCNA1 and KCNA4 shows rapid inactivation (PubMed:2348860).
Regulates neuronal excitability in hippocampus, especially in
mossy fibers and medial perforant path axons, preventing neuronal
hyperexcitability. 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:12177193, PubMed:23318870). 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)
release (PubMed:17869444). Plays a role in regulating the
generation of action potentials and preventing hyperexcitability
in myelinated axons of the vagus nerve, and thereby contributes to
the regulation of heart contraction (By similarity). Required for
normal neuromuscular responses (PubMed:22206926). Regulates the
frequency of neuronal action potential firing in response to
mechanical stimuli, and plays a role in the perception of pain
caused by mechanical stimuli, but does not play a role in the
perception of pain due to heat stimuli (By similarity). Required
for normal responses to auditory stimuli and precise location of
sound sources, but not for sound perception (By similarity). The
use of toxins that block specific channels suggest that it
contributes to the regulation of the axonal release of the
neurotransmitter dopamine (By similarity). Required for normal
postnatal brain development and normal proliferation of neuronal
precursor cells in the brain (By similarity). Plays a role in the
reabsorption of Mg(2+) in the distal convoluted tubules in the
kidney and in magnesium ion homeostasis, probably via its effect
on the membrane potential (By similarity).
{ECO:0000250|UniProtKB:P16388, ECO:0000250|UniProtKB:Q09470,
ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:12114518,
ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:12681381,
ECO:0000269|PubMed:17855588, ECO:0000269|PubMed:17869444,
ECO:0000269|PubMed:22206926, ECO:0000269|PubMed:23318870,
ECO:0000269|PubMed:2348860, ECO:0000269|PubMed:23725331,
ECO:0000269|PubMed:2539643, ECO:0000269|PubMed:8038169,
ECO:0000305|PubMed:16306173}.
-!- ENZYME REGULATION: Inhibited by 4-aminopyridine (4-AP) and by
tetraethylammonium (TEA) (PubMed:2539643). Inhibited by kaliotoxin
(KTX) (PubMed:23725331). {ECO:0000269|PubMed:2348860,
ECO:0000269|PubMed:23725331, ECO:0000269|PubMed:2539643}.
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and
KCNA7 (PubMed:10896669, PubMed:10884227). Channel activity is
regulated by interaction with the beta subunits KCNAB1 and KCNAB2
(PubMed:9334400, PubMed:12114518). Identified in a complex with
KCNA2 and KCNAB2 (PubMed:10896669, PubMed:11086297,
PubMed:23318870, PubMed:10884227). Interacts (via C-terminus) with
the PDZ domains of DLG1, DLG2 and DLG4. Interacts with LGI1 within
a complex containing LGI1, KCNA4 and KCNAB1. Interacts (via
cytoplasmic N-terminal domain) with KCNRG; this inhibits channel
activity (By similarity). Interacts with ANK3; this inhibits
channel activity (By similarity). Interacts (via N-terminus) with
STX1A; this promotes channel inactivation (PubMed:12114518).
Interacts (via N-terminus) with the heterodimer formed by GNB1 and
GNG2; this promotes channel inactivation (PubMed:12114518). Can
interact simultaneously with STX1A and the heterodimer formed by
GNB1 and GNG2 (PubMed:12114518). {ECO:0000250,
ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:10884227,
ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:12114518, ECO:0000269|PubMed:16504945,
ECO:0000269|PubMed:23318870, ECO:0000269|PubMed:7477295,
ECO:0000269|PubMed:9334400}.
-!- INTERACTION:
P78352:DLG4 (xeno); NbExp=2; IntAct=EBI-631463, EBI-80389;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12114518,
ECO:0000269|PubMed:12681381, ECO:0000269|PubMed:17855588,
ECO:0000269|PubMed:22206926, ECO:0000269|PubMed:2348860,
ECO:0000269|PubMed:23725331, ECO:0000269|PubMed:2539643,
ECO:0000269|PubMed:8038169}; Multi-pass membrane protein
{ECO:0000305}. Membrane {ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:9334400}. Cell projection, axon
{ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:12177193,
ECO:0000269|PubMed:9334400}. Cytoplasmic vesicle
{ECO:0000269|PubMed:12177193, ECO:0000269|PubMed:8038169}.
Perikaryon {ECO:0000269|PubMed:12177193}. Endoplasmic reticulum
{ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:12681381}. Cell
projection, dendrite {ECO:0000250|UniProtKB:P16388}. Cell junction
{ECO:0000250|UniProtKB:P16388}. Cell junction, synapse
{ECO:0000250|UniProtKB:P16388}. Cell junction, synapse,
presynaptic cell membrane {ECO:0000269|PubMed:17869444}.
Note=Homotetrameric KCNA1 is primarily located in the endoplasmic
reticulum. Interaction with KCNA2 and KCNAB2 or with KCNA4 and
KCNAB2 promotes expression at the cell membrane (PubMed:10896669).
Detected at axon terminals (By similarity).
{ECO:0000250|UniProtKB:P16388, ECO:0000269|PubMed:10896669}.
-!- TISSUE SPECIFICITY: Detected in hippocampus, in the middle third
of the molecular layer of the dentate gyrus and in stratum
radiatum and stratum oriens (PubMed:9334400). Detected in the
mossy fiber zone in the hippocampus CA3 region, at or near axon
terminals (PubMed:9334400). Detected in brain cortex, at basket
cell terminals (PubMed:9334400). Detected adjacent to nodes of
Ranvier in juxtaparanodal zones in spinal cord nerve fibers, but
also in paranodal regions in some myelinated spinal cord axons
(PubMed:11086297). Detected in juxtaparanodal regions adjacent to
the nodes of Ranvier in myelinated axons in cerebellar white
matter (PubMed:9334400). Detected in sensory neurons
(PubMed:17855588). Detected in neurons from the medial nucleus of
the trapezoid body (PubMed:12177193). Detected in basolateral
amygdala (PubMed:16306173). Detected in the paraventricular
nucleus of the hypothalamus (PubMed:17869444). Detected in the
islet of Langerhans (at protein level) (PubMed:21483673). Detected
in the islet of Langerhans (PubMed:21483673).
{ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:12177193,
ECO:0000269|PubMed:16306173, ECO:0000269|PubMed:17855588,
ECO:0000269|PubMed:21483673, ECO:0000269|PubMed:9334400}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization and for interaction with the beta subunits that
promote rapid channel closure. {ECO:0000269|PubMed:10884227}.
-!- 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}.
-!- PTM: Palmitoylated on Cys-243; which may be required for membrane
targeting. {ECO:0000250|UniProtKB:Q09470}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:10896669,
ECO:0000269|PubMed:8038169}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation
increases in response to NRG1; this inhibits channel activity (By
similarity). Phosphorylated by PKA (PubMed:8038169,
PubMed:12681381). Phosphorylation at Ser-446 regulates channel
activity by down-regulating expression at the cell membrane (By
similarity). {ECO:0000250|UniProtKB:P16388,
ECO:0000250|UniProtKB:Q09470, ECO:0000269|PubMed:12681381,
ECO:0000269|PubMed:8038169}.
-!- RNA EDITING: Modified_positions=400 {ECO:0000269|PubMed:12907802};
Note=Partially edited. RNA editing is at an average of 50% in the
whole brain.;
-!- MISCELLANEOUS: A missense mutation at Ser-309 is the cause of the
autosomal dominant myokymia and seizures (ADMS) phenotype.
Homozygous and heterozygous rats are born at the expected
Mendelian rate. After 6 weeks, heterozygous rats begin to display
muscle twitching, startle responses and spontaneous convulsive
seizures; over 80% of the animals are dead after 30 weeks. After
16 weeks, they display lower body weight compared to wild-type.
The rats exhibit severe periodic seizures with characteristic
alterations in their cortical and hippocampal
electroencephalogram, similar to rodent models of temporal lobe
epilepsy. Homozygous rats display impaired development starting 14
days after birth, with reduced body weight, tremors, motor
incoordination, spontaneous convulsive seizures; none survive past
18 days after birth. {ECO:0000269|PubMed:22206926}.
-!- 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. Kv1.1/KCNA1 sub-subfamily. {ECO:0000305}.
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EMBL; X12589; CAA31102.1; -; mRNA.
EMBL; M26161; AAA41982.1; -; mRNA.
PIR; B39113; B39113.
RefSeq; NP_775118.1; NM_173095.3.
UniGene; Rn.9769; -.
PDB; 1EXB; X-ray; 2.10 A; E=27-129.
PDBsum; 1EXB; -.
ProteinModelPortal; P10499; -.
SMR; P10499; -.
BioGrid; 246675; 3.
IntAct; P10499; 2.
MINT; P10499; -.
STRING; 10116.ENSRNOP00000026731; -.
ChEMBL; CHEMBL5190; -.
GuidetoPHARMACOLOGY; 538; -.
iPTMnet; P10499; -.
PhosphoSitePlus; P10499; -.
PaxDb; P10499; -.
PRIDE; P10499; -.
Ensembl; ENSRNOT00000026731; ENSRNOP00000026731; ENSRNOG00000019750.
GeneID; 24520; -.
KEGG; rno:24520; -.
UCSC; RGD:2949; rat.
CTD; 3736; -.
RGD; 2949; Kcna1.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; P10499; -.
KO; K04874; -.
OMA; AHYRQAN; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; P10499; -.
TreeFam; TF313103; -.
Reactome; R-RNO-1296072; Voltage gated Potassium channels.
EvolutionaryTrace; P10499; -.
PRO; PR:P10499; -.
Proteomes; UP000002494; Chromosome 4.
Bgee; ENSRNOG00000019750; -.
Genevisible; P10499; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0030424; C:axon; ISO:RGD.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IDA:RGD.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0030425; C:dendrite; IDA:BHF-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:UniProtKB.
GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; IDA:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IMP:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
GO; GO:0007420; P:brain development; ISO:RGD.
GO; GO:0010644; P:cell communication by electrical coupling; IMP:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IDA:UniProtKB.
GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
GO; GO:0021766; P:hippocampus development; ISO:RGD.
GO; GO:0010960; P:magnesium ion homeostasis; ISS:UniProtKB.
GO; GO:0007405; P:neuroblast proliferation; ISO:RGD.
GO; GO:0050905; P:neuromuscular process; ISS:UniProtKB.
GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
GO; GO:0023041; P:neuronal signal transduction; IMP:UniProtKB.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0042391; P:regulation of membrane potential; ISS:UniProtKB.
GO; GO:0006937; P:regulation of muscle contraction; IMP:UniProtKB.
GO; GO:0001964; P:startle response; 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; IPR004048; K_chnl_volt-dep_Kv1.1.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01508; KV11CHANNEL.
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; Cytoplasmic vesicle; Endoplasmic reticulum;
Glycoprotein; Ion channel; Ion transport; Lipoprotein; Membrane;
Palmitate; Phosphoprotein; Potassium; Potassium channel;
Potassium transport; Reference proteome; RNA editing; Synapse;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 495 Potassium voltage-gated channel subfamily
A member 1.
/FTId=PRO_0000053970.
TOPO_DOM 1 164 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 165 186 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 187 220 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 221 242 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 243 253 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 254 274 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 275 287 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 288 308 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 309 323 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 324 345 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 346 359 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 360 371 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 372 379 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 380 386 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 387 415 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 416 495 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 1 128 Tetramerization domain. {ECO:0000305}.
REGION 310 323 S4-S5 linker.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 372 377 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
MOTIF 493 495 PDZ-binding. {ECO:0000305}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 322 322 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 446 446 Phosphoserine; by PKA.
{ECO:0000269|PubMed:8038169}.
LIPID 243 243 S-palmitoyl cysteine.
{ECO:0000250|UniProtKB:Q09470}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 400 400 I -> V (in RNA edited version).
MUTAGEN 309 309 S->T: In ADMS: Dominant negative mutation
that abolishes channel activity; leads to
myokymia, neuromyotonia, spontaneous
epileptic seizures and premature death.
{ECO:0000269|PubMed:22206926}.
MUTAGEN 352 352 A->R: Is not blocked by the scorpion
mesomartoxin.
{ECO:0000269|PubMed:25514171}.
MUTAGEN 355 355 H->Q: Is not blocked by the scorpion
mesomartoxin.
{ECO:0000269|PubMed:25514171}.
MUTAGEN 357 357 S->P: Is not blocked by the scorpion
mesomartoxin.
{ECO:0000269|PubMed:25514171}.
MUTAGEN 379 379 Y->V: Is blocked by the scorpion
mesomartoxin, with an IC(50)=16.60 nM.
{ECO:0000269|PubMed:25514171}.
MUTAGEN 381 381 V->T: Is not blocked by the scorpion
mesomartoxin.
{ECO:0000269|PubMed:25514171}.
MUTAGEN 443 443 R->C: Abolishes phosphorylation by PKA;
when associated with A-446.
MUTAGEN 446 446 S->A: Abolishes phosphorylation by PKA;
when associated with C-443.
STRAND 38 43 {ECO:0000244|PDB:1EXB}.
STRAND 46 51 {ECO:0000244|PDB:1EXB}.
HELIX 52 56 {ECO:0000244|PDB:1EXB}.
TURN 62 64 {ECO:0000244|PDB:1EXB}.
HELIX 66 69 {ECO:0000244|PDB:1EXB}.
HELIX 70 72 {ECO:0000244|PDB:1EXB}.
TURN 75 78 {ECO:0000244|PDB:1EXB}.
STRAND 79 82 {ECO:0000244|PDB:1EXB}.
HELIX 86 97 {ECO:0000244|PDB:1EXB}.
HELIX 110 119 {ECO:0000244|PDB:1EXB}.
SEQUENCE 495 AA; 56379 MW; 29804463133F5D31 CRC64;
MTVMSGENAD EASAAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET QLKTLAQFPN
TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG RLRRPVNVPL DMFSEEIKFY
ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ RQVWLLFEYP ESSGPARVIA IVSVMVILIS
IVIFCLETLP ELKDDKDFTG TIHRIDNTTV IYTSNIFTDP FFIVETLCII WFSFELVVRF
FACPSKTDFF KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE EAESHFSSIP
DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE
GEEQAQLLHV SSPNLASDSD LSRRSSSTIS KSEYMEIEED MNNSIAHYRQ ANIRTGNCTA
TDQNCVNKSK LLTDV


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