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Database: UniProt
Entry: KCNA1_HUMAN
LinkDB: KCNA1_HUMAN
Original site: KCNA1_HUMAN 
ID   KCNA1_HUMAN             Reviewed;         495 AA.
AC   Q09470; A6NM83; Q3MIQ9;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   27-SEP-2017, entry version 182.
DE   RecName: Full=Potassium voltage-gated channel subfamily A member 1;
DE   AltName: Full=Voltage-gated K(+) channel HuKI {ECO:0000303|PubMed:19912772};
DE   AltName: Full=Voltage-gated potassium channel HBK1 {ECO:0000303|PubMed:2128063};
DE   AltName: Full=Voltage-gated potassium channel subunit Kv1.1;
GN   Name=KCNA1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND ENZYME
RP   REGULATION.
RC   TISSUE=Brain;
RX   PubMed=19912772; DOI=10.1016/1044-7431(90)90004-N;
RA   Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.;
RT   "Human potassium channel genes: molecular cloning and functional
RT   expression.";
RL   Mol. Cell. Neurosci. 1:214-223(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
RA   Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA   Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA   Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA   Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA   Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA   Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA   Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA   Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA   Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA   Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA   Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA   Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
RA   Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA   Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA   Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA   Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA   Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA   Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA   Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA   Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA   Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA   Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA   Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA   Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA   Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
RA   Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA   Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA   Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA   Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA   Kucherlapati R., Weinstock G., Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 263-315.
RX   PubMed=2128063;
RA   Freeman S.N., Conley E.C., Brennand J.C., Russell N.J.W.,
RA   Brammar W.J.;
RT   "Cloning and characterization of a cDNA encoding a human brain
RT   potassium channel.";
RL   Biochem. Soc. Trans. 18:891-892(1990).
RN   [6]
RP   INTERACTION WITH KCNA2 AND KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=11086297;
RX   DOI=10.1002/1096-9861(20000101)429:1<166::AID-CNE13>3.0.CO;2-Y;
RA   Rasband M.N., Trimmer J.S.;
RT   "Subunit composition and novel localization of K+ channels in spinal
RT   cord.";
RL   J. Comp. Neurol. 429:166-176(2001).
RN   [7]
RP   RNA EDITING OF POSITION 400.
RX   PubMed=12907802; DOI=10.1126/science.1086763;
RA   Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT   "Nervous system targets of RNA editing identified by comparative
RT   genomics.";
RL   Science 301:832-836(2003).
RN   [8]
RP   PALMITOYLATION AT CYS-243, MUTAGENESIS OF 35-CYS--CYS-36 AND CYS-243,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=15837928; DOI=10.1073/pnas.0501999102;
RA   Gubitosi-Klug R.A., Mancuso D.J., Gross R.W.;
RT   "The human Kv1.1 channel is palmitoylated, modulating voltage sensing:
RT   Identification of a palmitoylation consensus sequence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:5964-5968(2005).
RN   [9]
RP   REVIEW.
RX   PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
RA   Baranauskas G.;
RT   "Ionic channel function in action potential generation: current
RT   perspective.";
RL   Mol. Neurobiol. 35:129-150(2007).
RN   [10]
RP   INTERACTION WITH KCNRG, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19968958; DOI=10.1016/j.bbrc.2009.11.143;
RA   Usman H., Mathew M.K.;
RT   "Potassium channel regulator KCNRG regulates surface expression of
RT   Shaker-type potassium channels.";
RL   Biochem. Biophys. Res. Commun. 391:1301-1305(2010).
RN   [11]
RP   FUNCTION.
RX   PubMed=21106501; DOI=10.1093/brain/awq318;
RA   Tomlinson S.E., Tan S.V., Kullmann D.M., Griggs R.C., Burke D.,
RA   Hanna M.G., Bostock H.;
RT   "Nerve excitability studies characterize Kv1.1 fast potassium channel
RT   dysfunction in patients with episodic ataxia type 1.";
RL   Brain 133:3530-3540(2010).
RN   [12]
RP   TISSUE SPECIFICITY.
RX   PubMed=21483673; DOI=10.1371/journal.pone.0018213;
RA   Ma Z., Lavebratt C., Almgren M., Portwood N., Forsberg L.E.,
RA   Branstrom R., Berglund E., Falkmer S., Sundler F., Wierup N.,
RA   Bjorklund A.;
RT   "Evidence for presence and functional effects of Kv1.1 channels in
RT   beta-cells: general survey and results from mceph/mceph mice.";
RL   PLoS ONE 6:E18213-E18213(2011).
RN   [13]
RP   SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-446, AND MUTAGENESIS OF
RP   SER-446.
RX   PubMed=23774215; DOI=10.1158/0008-5472.CAN-12-3690;
RA   Lallet-Daher H., Wiel C., Gitenay D., Navaratnam N., Augert A.,
RA   Le Calve B., Verbeke S., Carling D., Aubert S., Vindrieux D.,
RA   Bernard D.;
RT   "Potassium channel KCNA1 modulates oncogene-induced senescence and
RT   transformation.";
RL   Cancer Res. 73:5253-5265(2013).
RN   [14]
RP   INTERACTION WITH ANK3, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=23903368; DOI=10.1038/ki.2013.280;
RA   San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G.,
RA   Bindels R.J.;
RT   "Ankyrin-3 is a novel binding partner of the voltage-gated potassium
RT   channel Kv1.1 implicated in renal magnesium handling.";
RL   Kidney Int. 85:94-102(2014).
RN   [15]
RP   VARIANTS EA1 PHE-174; SER-239; ILE-249 AND ALA-408.
RX   PubMed=7842011; DOI=10.1038/ng1094-136;
RA   Browne D.L., Gancher S.T., Nutt J.G., Brunt E.R.P., Smith E.A.,
RA   Kramer P., Litt M.;
RT   "Episodic ataxia/myokymia syndrome is associated with point mutations
RT   in the human potassium channel gene, KCNA1.";
RL   Nat. Genet. 8:136-140(1994).
RN   [16]
RP   VARIANTS EA1 PHE-174; CYS-184 AND ASP-325.
RX   PubMed=8541859; DOI=10.1093/hmg/4.9.1671;
RA   Browne D.L., Brunt E.R.P., Griggs R.C., Nutt J.G., Gancher S.T.,
RA   Smith E.A., Litt M.;
RT   "Identification of two new KCNA1 mutations in episodic ataxia/myokymia
RT   families.";
RL   Hum. Mol. Genet. 4:1671-1672(1995).
RN   [17]
RP   CHARACTERIZATION OF VARIANTS EA1 CYS-184; ASP-325 AND ALA-408.
RX   PubMed=8845167; DOI=10.1016/0896-6273(95)90022-5;
RA   Adelman J.P., Bond C.T., Pessia M., Maylie J.;
RT   "Episodic ataxia results from voltage-dependent potassium channels
RT   with altered functions.";
RL   Neuron 15:1449-1454(1995).
RN   [18]
RP   VARIANT EA1 MET-226.
RX   PubMed=8871592; DOI=10.1002/ana.410400422;
RA   Comu S., Giuliani M., Narayanan V.;
RT   "Episodic ataxia and myokymia syndrome: a new mutation of potassium
RT   channel gene Kv1.1.";
RL   Ann. Neurol. 40:684-687(1996).
RN   [19]
RP   VARIANTS EA1 ARG-177; ALA-226 AND ILE-404.
RX   PubMed=9600245; DOI=10.1007/s004390050722;
RA   Scheffer H., Brunt E.R.P., Mol G.J.J., van der Vlies P., Stulp R.P.,
RA   Verlind E., Mantel G., Averyanov Y.N., Hofstra R.M.W., Buys C.H.C.M.;
RT   "Three novel KCNA1 mutations in episodic ataxia type I families.";
RL   Hum. Genet. 102:464-466(1998).
RN   [20]
RP   VARIANT EA1 ARG-226, AND CHARACTERIZATION OF VARIANT EA1 ARG-226.
RX   PubMed=10355668; DOI=10.1093/brain/122.5.817;
RA   Zuberi S.M., Eunson L.H., Spauschus A., De Silva R., Tolmie J.,
RA   Wood N.W., McWilliam R.C., Stephenson J.P.B., Kullmann D.M.,
RA   Hanna M.G.;
RT   "A novel mutation in the human voltage-gated potassium channel gene
RT   (Kv1.1) associates with episodic ataxia type 1 and sometimes with
RT   partial epilepsy.";
RL   Brain 122:817-825(1999).
RN   [21]
RP   VARIANTS MK1 PRO-242 AND HIS-244, VARIANT EA1 ILE-404,
RP   CHARACTERIZATION OF VARIANTS MK1 PRO-242 AND HIS-244, CHARACTERIZATION
RP   OF VARIANT EA1 ILE-404, AND FUNCTION.
RX   PubMed=11026449;
RX   DOI=10.1002/1531-8249(200010)48:4<647::AID-ANA12>3.3.CO;2-H;
RA   Eunson L.H., Rea R., Zuberi S.M., Youroukos S., Panayiotopoulos C.P.,
RA   Liguori R., Avoni P., McWilliam R.C., Stephenson J.B.P., Hanna M.G.,
RA   Kullmann D.M., Spauschus A.;
RT   "Clinical, genetic, and expression studies of mutations in the
RT   potassium channel gene KCNA1 reveal new phenotypic variability.";
RL   Ann. Neurol. 48:647-656(2000).
RN   [22]
RP   VARIANT EA1 ILE-329.
RX   PubMed=11013453;
RX   DOI=10.1002/1098-1004(200010)16:4<374::AID-HUMU15>3.3.CO;2-W;
RA   Knight M.A., Storey E., McKinlay Gardner R.J., Hand P., Forrest S.M.;
RT   "Identification of a novel missense mutation L329I in the episodic
RT   ataxia type 1 gene KCNA1 -- a challenging problem.";
RL   Hum. Mutat. 16:374-374(2000).
RN   [23]
RP   CHARACTERIZATION OF VARIANTS EA1 ASP-325 AND ALA-408, FUNCTION,
RP   SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNAB1.
RX   PubMed=12077175;
RA   Maylie B., Bissonnette E., Virk M., Adelman J.P., Maylie J.G.;
RT   "Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel
RT   alter hKvbeta 1-induced N-type inactivation.";
RL   J. Neurosci. 22:4786-4793(2002).
RN   [24]
RP   VARIANT EA1 ILE-342.
RX   PubMed=15532032; DOI=10.1002/humu.9295;
RA   Lee H., Wang H., Jen J.C., Sabatti C., Baloh R.W., Nelson S.F.;
RT   "A novel mutation in KCNA1 causes episodic ataxia without myokymia.";
RL   Hum. Mutat. 24:536-536(2004).
RN   [25]
RP   CHARACTERIZATION OF VARIANTS EA1 ASP-325; ILE-404 AND ALA-408,
RP   MUTAGENESIS OF ILE-177, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
RA   Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
RT   "Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
RT   inactivation properties of the human potassium channels Kv1.4-
RT   1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2.";
RL   Eur. J. Neurosci. 24:3073-3083(2006).
RN   [26]
RP   VARIANT MK1 LYS-226, CHARACTERIZATION OF VARIANT MK1 LYS-226,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=17136396; DOI=10.1007/s10048-006-0071-z;
RA   Chen H., von Hehn C., Kaczmarek L.K., Ment L.R., Pober B.R.,
RA   Hisama F.M.;
RT   "Functional analysis of a novel potassium channel (KCNA1) mutation in
RT   hereditary myokymia.";
RL   Neurogenetics 8:131-135(2007).
RN   [27]
RP   VARIANT MK1 ASP-255, CHARACTERIZATION OF VARIANT MK1 ASP-255,
RP   FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
RX   PubMed=19307729; DOI=10.1172/JCI36948;
RA   Glaudemans B., van der Wijst J., Scola R.H., Lorenzoni P.J.,
RA   Heister A., van der Kemp A.W., Knoers N.V., Hoenderop J.G.,
RA   Bindels R.J.;
RT   "A missense mutation in the Kv1.1 voltage-gated potassium channel-
RT   encoding gene KCNA1 is linked to human autosomal dominant
RT   hypomagnesemia.";
RL   J. Clin. Invest. 119:936-942(2009).
RN   [28]
RP   CHARACTERIZATION OF VARIANT MK1 ASP-255, MUTAGENESIS OF ASN-255,
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=19903818; DOI=10.1074/jbc.M109.041517;
RA   van der Wijst J., Glaudemans B., Venselaar H., Nair A.V., Forst A.L.,
RA   Hoenderop J.G., Bindels R.J.;
RT   "Functional analysis of the Kv1.1 N255D mutation associated with
RT   autosomal dominant hypomagnesemia.";
RL   J. Biol. Chem. 285:171-178(2010).
RN   [29]
RP   VARIANT LEU-405.
RX   PubMed=27864847; DOI=10.1002/humu.23149;
RG   Clinical Study Group;
RA   Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
RA   Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
RA   Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
RA   Guerrini R.;
RT   "Diagnostic targeted resequencing in 349 patients with drug-resistant
RT   pediatric epilepsies identifies causative mutations in 30 different
RT   genes.";
RL   Hum. Mutat. 38:216-225(2017).
CC   -!- FUNCTION: Voltage-gated potassium channel that mediates
CC       transmembrane potassium transport in excitable membranes,
CC       primarily in the brain and the central nervous system, but also in
CC       the kidney (PubMed:19903818). Contributes to the regulation of the
CC       membrane potential and nerve signaling, and prevents neuronal
CC       hyperexcitability (PubMed:17156368). Forms tetrameric potassium-
CC       selective channels through which potassium ions pass in accordance
CC       with their electrochemical gradient. The channel alternates
CC       between opened and closed conformations in response to the voltage
CC       difference across the membrane (PubMed:19912772). Can form
CC       functional homotetrameric channels and heterotetrameric channels
CC       that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5,
CC       KCNA6, KCNA7, and possibly other family members as well; channel
CC       properties depend on the type of alpha subunits that are part of
CC       the channel (PubMed:12077175, PubMed:17156368). Channel properties
CC       are modulated by cytoplasmic beta subunits that regulate the
CC       subcellular location of the alpha subunits and promote rapid
CC       inactivation of delayed rectifier potassium channels
CC       (PubMed:12077175, PubMed:17156368). In vivo, membranes probably
CC       contain a mixture of heteromeric potassium channel complexes,
CC       making it difficult to assign currents observed in intact tissues
CC       to any particular potassium channel family member. Homotetrameric
CC       KCNA1 forms a delayed-rectifier potassium channel that opens in
CC       response to membrane depolarization, followed by slow spontaneous
CC       channel closure (PubMed:19912772, PubMed:19968958,
CC       PubMed:19307729, PubMed:19903818). In contrast, a heterotetrameric
CC       channel formed by KCNA1 and KCNA4 shows rapid inactivation
CC       (PubMed:17156368). Regulates neuronal excitability in hippocampus,
CC       especially in mossy fibers and medial perforant path axons,
CC       preventing neuronal hyperexcitability. Response to toxins that are
CC       selective for KCNA1, respectively for KCNA2, suggests that
CC       heteromeric potassium channels composed of both KCNA1 and KCNA2
CC       play a role in pacemaking and regulate the output of deep
CC       cerebellar nuclear neurons (By similarity). May function as down-
CC       stream effector for G protein-coupled receptors and inhibit
CC       GABAergic inputs to basolateral amygdala neurons (By similarity).
CC       May contribute to the regulation of neurotransmitter release, such
CC       as gamma-aminobutyric acid (GABA) release (By similarity). Plays a
CC       role in regulating the generation of action potentials and
CC       preventing hyperexcitability in myelinated axons of the vagus
CC       nerve, and thereby contributes to the regulation of heart
CC       contraction (By similarity). Required for normal neuromuscular
CC       responses (PubMed:11026449, PubMed:17136396). Regulates the
CC       frequency of neuronal action potential firing in response to
CC       mechanical stimuli, and plays a role in the perception of pain
CC       caused by mechanical stimuli, but does not play a role in the
CC       perception of pain due to heat stimuli (By similarity). Required
CC       for normal responses to auditory stimuli and precise location of
CC       sound sources, but not for sound perception (By similarity). The
CC       use of toxins that block specific channels suggest that it
CC       contributes to the regulation of the axonal release of the
CC       neurotransmitter dopamine (By similarity). Required for normal
CC       postnatal brain development and normal proliferation of neuronal
CC       precursor cells in the brain (By similarity). Plays a role in the
CC       reabsorption of Mg(2+) in the distal convoluted tubules in the
CC       kidney and in magnesium ion homeostasis, probably via its effect
CC       on the membrane potential (PubMed:23903368, PubMed:19307729).
CC       {ECO:0000250|UniProtKB:P10499, ECO:0000269|PubMed:11026449,
CC       ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:15837928,
CC       ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:17156368,
CC       ECO:0000269|PubMed:19307729, ECO:0000269|PubMed:19903818,
CC       ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958,
CC       ECO:0000269|PubMed:21106501, ECO:0000269|PubMed:23903368}.
CC   -!- ENZYME REGULATION: Inhibited by 1.1 mM 4-aminopyridine (4-AP) and
CC       by 20 mM tetraethylammonium (TEA), but not by charybdotoxin
CC       (CTX)(PubMed:19912772). Inhibited by dendrotoxin (DTX)
CC       (PubMed:19307729). {ECO:0000269|PubMed:19307729,
CC       ECO:0000269|PubMed:19912772}.
CC   -!- SUBUNIT: Homotetramer and heterotetramer with other channel-
CC       forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and
CC       KCNA7 (PubMed:12077175, PubMed:17156368). Channel activity is
CC       regulated by interaction with the beta subunits KCNAB1 and KCNAB2
CC       (PubMed:12077175, PubMed:17156368). Identified in a complex with
CC       KCNA2 and KCNAB2 (PubMed:11086297). Interacts (via C-terminus)
CC       with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity).
CC       Interacts with LGI1 within a complex containing LGI1, KCNA4 and
CC       KCNAB1 (By similarity). Interacts (via N-terminus) with STX1A;
CC       this promotes channel inactivation (By similarity). Interacts (via
CC       N-terminus) with the heterodimer formed by GNB1 and GNG2; this
CC       promotes channel inactivation (By similarity). Can interact
CC       simultaneously with STX1A and the heterodimer formed by GNB1 and
CC       GNG2 (By similarity). Interacts (via cytoplasmic N-terminal
CC       domain) with KCNRG; this inhibits channel activity
CC       (PubMed:19968958). Interacts with ANK3; this inhibits channel
CC       activity (PubMed:23903368). {ECO:0000250|UniProtKB:P10499,
CC       ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:17156368,
CC       ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:23903368,
CC       ECO:0000305}.
CC   -!- INTERACTION:
CC       Q62936:Dlg3 (xeno); NbExp=2; IntAct=EBI-8286599, EBI-349596;
CC       P78352:DLG4; NbExp=2; IntAct=EBI-8286599, EBI-80389;
CC       Q9Y5U9:IER3IP1; NbExp=4; IntAct=EBI-8286599, EBI-725665;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12077175,
CC       ECO:0000269|PubMed:15837928, ECO:0000269|PubMed:17136396,
CC       ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:19307729,
CC       ECO:0000269|PubMed:19903818, ECO:0000269|PubMed:19912772,
CC       ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:23903368}; Multi-
CC       pass membrane protein {ECO:0000305}. Membrane
CC       {ECO:0000269|PubMed:11086297}. Cell projection, axon
CC       {ECO:0000269|PubMed:11086297}. Cytoplasmic vesicle
CC       {ECO:0000269|PubMed:23774215}. Perikaryon
CC       {ECO:0000250|UniProtKB:P10499}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:P10499}. Cell projection, dendrite
CC       {ECO:0000250|UniProtKB:P16388}. Cell junction
CC       {ECO:0000250|UniProtKB:P16388}. Cell junction, synapse
CC       {ECO:0000250|UniProtKB:P16388}. Cell junction, synapse,
CC       presynaptic cell membrane {ECO:0000250|UniProtKB:P10499}.
CC       Note=Homotetrameric KCNA1 is primarily located in the endoplasmic
CC       reticulum. Interaction with KCNA2 and KCNAB2 or with KCNA4 and
CC       KCNAB2 promotes expression at the cell membrane (By similarity).
CC       Detected at axon terminals (By similarity).
CC       {ECO:0000250|UniProtKB:P10499, ECO:0000250|UniProtKB:P16388}.
CC   -!- TISSUE SPECIFICITY: Detected adjacent to nodes of Ranvier in
CC       juxtaparanodal zones in spinal cord nerve fibers, but also in
CC       paranodal regions in some myelinated spinal cord axons (at protein
CC       level) (PubMed:11086297). Detected in the islet of Langerhans
CC       (PubMed:21483673). {ECO:0000269|PubMed:11086297,
CC       ECO:0000269|PubMed:21483673}.
CC   -!- DOMAIN: The cytoplasmic N-terminus is important for
CC       tetramerization and for interaction with the beta subunits that
CC       promote rapid channel closure. {ECO:0000250|UniProtKB:P10499}.
CC   -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
CC       and is characterized by a series of positively charged amino acids
CC       at every third position. Channel opening and closing is effected
CC       by a conformation change that affects the position and orientation
CC       of the voltage-sensor paddle formed by S3 and S4 within the
CC       membrane. A transmembrane electric field that is positive inside
CC       would push the positively charged S4 segment outwards, thereby
CC       opening the pore, while a field that is negative inside would pull
CC       the S4 segment inwards and close the pore. Changes in the position
CC       and orientation of S4 are then transmitted to the activation gate
CC       formed by the inner helix bundle via the S4-S5 linker region.
CC       {ECO:0000250|UniProtKB:P63142}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P10499}.
CC   -!- PTM: Palmitoylated on Cys-243; which may be required for membrane
CC       targeting. {ECO:0000269|PubMed:15837928}.
CC   -!- PTM: Phosphorylated on tyrosine residues. Phosphorylation
CC       increases in response to NRG1; this inhibits channel activity (By
CC       similarity). Phosphorylation at Ser-446 regulates channel activity
CC       by down-regulating expression at the cell membrane
CC       (PubMed:23774215). {ECO:0000250|UniProtKB:P16388,
CC       ECO:0000269|PubMed:23774215}.
CC   -!- RNA EDITING: Modified_positions=400 {ECO:0000269|PubMed:12907802};
CC       Note=Partially edited. RNA editing varies from 17% in the caudate
CC       nucleus to 68% in the spinal cord and to 77% in the medulla.;
CC   -!- DISEASE: Episodic ataxia 1 (EA1) [MIM:160120]: An autosomal
CC       dominant disorder characterized by brief episodes of ataxia and
CC       dysarthria. Neurological examination during and between the
CC       attacks demonstrates spontaneous, repetitive discharges in the
CC       distal musculature (myokymia) that arise from peripheral nerve.
CC       Nystagmus is absent. {ECO:0000269|PubMed:10355668,
CC       ECO:0000269|PubMed:11013453, ECO:0000269|PubMed:11026449,
CC       ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:15532032,
CC       ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:7842011,
CC       ECO:0000269|PubMed:8541859, ECO:0000269|PubMed:8845167,
CC       ECO:0000269|PubMed:8871592, ECO:0000269|PubMed:9600245}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Myokymia isolated 1 (MK1) [MIM:160120]: A condition
CC       characterized by spontaneous involuntary contraction of muscle
CC       fiber groups that can be observed as vermiform movement of the
CC       overlying skin. Electromyography typically shows continuous motor
CC       unit activity with spontaneous oligo- and multiplet-discharges of
CC       high intraburst frequency (myokymic discharges). Isolated
CC       spontaneous muscle twitches occur in many persons and have no
CC       grave significance. {ECO:0000269|PubMed:11026449,
CC       ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:19307729,
CC       ECO:0000269|PubMed:19903818}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
CC       pyramidal neurons is probably mediated by potassium channels
CC       containing KCNA2 plus KCNA1 or other family members. It is
CC       activated at about -50 mV, i.e. below the action potential
CC       threshold, and is characterized by slow inactivation, extremely
CC       slow recovery from inactivation, sensitivity to dendrotoxin (DTX)
CC       and to 4-aminopyridine (4-AP). {ECO:0000305|PubMed:17917103}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker)
CC       (TC 1.A.1.2) subfamily. Kv1.1/KCNA1 sub-subfamily. {ECO:0000305}.
DR   EMBL; L02750; AAA36139.1; -; mRNA.
DR   EMBL; AC006063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471116; EAW88833.1; -; Genomic_DNA.
DR   EMBL; BC101733; AAI01734.1; -; mRNA.
DR   EMBL; BC112180; AAI12181.1; -; mRNA.
DR   CCDS; CCDS8535.1; -.
DR   PIR; I57680; I57680.
DR   RefSeq; NP_000208.2; NM_000217.2.
DR   UniGene; Hs.416139; -.
DR   PDB; 2AFL; Model; -; A/B/C/D=326-407.
DR   PDBsum; 2AFL; -.
DR   ProteinModelPortal; Q09470; -.
DR   SMR; Q09470; -.
DR   BioGrid; 109939; 7.
DR   CORUM; Q09470; -.
DR   IntAct; Q09470; 13.
DR   MINT; MINT-1900397; -.
DR   STRING; 9606.ENSP00000371985; -.
DR   BindingDB; Q09470; -.
DR   ChEMBL; CHEMBL2309; -.
DR   DrugBank; DB00321; Amitriptyline.
DR   DrugBank; DB06637; Dalfampridine.
DR   DrugBank; DB01189; Desflurane.
DR   DrugBank; DB00228; Enflurane.
DR   DrugBank; DB00753; Isoflurane.
DR   DrugBank; DB01028; Methoxyflurane.
DR   DrugBank; DB01115; Nifedipine.
DR   DrugBank; DB01236; Sevoflurane.
DR   GuidetoPHARMACOLOGY; 538; -.
DR   TCDB; 1.A.1.2.12; the voltage-gated ion channel (vic) superfamily.
DR   iPTMnet; Q09470; -.
DR   PhosphoSitePlus; Q09470; -.
DR   SwissPalm; Q09470; -.
DR   BioMuta; KCNA1; -.
DR   DMDM; 223590092; -.
DR   MaxQB; Q09470; -.
DR   PaxDb; Q09470; -.
DR   PeptideAtlas; Q09470; -.
DR   PRIDE; Q09470; -.
DR   Ensembl; ENST00000382545; ENSP00000371985; ENSG00000111262.
DR   GeneID; 3736; -.
DR   KEGG; hsa:3736; -.
DR   UCSC; uc001qnh.4; human.
DR   CTD; 3736; -.
DR   DisGeNET; 3736; -.
DR   EuPathDB; HostDB:ENSG00000111262.4; -.
DR   GeneCards; KCNA1; -.
DR   GeneReviews; KCNA1; -.
DR   HGNC; HGNC:6218; KCNA1.
DR   HPA; CAB022365; -.
DR   MalaCards; KCNA1; -.
DR   MIM; 160120; phenotype.
DR   MIM; 176260; gene.
DR   neXtProt; NX_Q09470; -.
DR   OpenTargets; ENSG00000111262; -.
DR   Orphanet; 37612; Episodic ataxia type 1.
DR   Orphanet; 972; Hereditary continuous muscle fiber activity.
DR   Orphanet; 199326; Isolated autosomal dominant hypomagnesemia, Glaudemans type.
DR   PharmGKB; PA30019; -.
DR   eggNOG; KOG1545; Eukaryota.
DR   eggNOG; COG1226; LUCA.
DR   GeneTree; ENSGT00760000118846; -.
DR   HOGENOM; HOG000231015; -.
DR   HOVERGEN; HBG052230; -.
DR   InParanoid; Q09470; -.
DR   KO; K04874; -.
DR   OMA; AHYRQAN; -.
DR   OrthoDB; EOG091G10NU; -.
DR   PhylomeDB; Q09470; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR   ChiTaRS; KCNA1; human.
DR   GeneWiki; Kv1.1; -.
DR   GenomeRNAi; 3736; -.
DR   PRO; PR:Q09470; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   Bgee; ENSG00000111262; -.
DR   CleanEx; HS_KCNA1; -.
DR   Genevisible; Q09470; HS.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
DR   GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
DR   GO; GO:0030054; C:cell junction; ISS:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR   GO; GO:0043025; C:neuronal cell body; ISS:UniProtKB.
DR   GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
DR   GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
DR   GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
DR   GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
DR   GO; GO:0015079; F:potassium ion transmembrane transporter activity; TAS:ProtInc.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
DR   GO; GO:0010644; P:cell communication by electrical coupling; ISS:UniProtKB.
DR   GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
DR   GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
DR   GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
DR   GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; ISS:UniProtKB.
DR   GO; GO:0050976; P:detection of mechanical stimulus involved in sensory perception of touch; ISS:UniProtKB.
DR   GO; GO:0021766; P:hippocampus development; IEA:Ensembl.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IMP:UniProtKB.
DR   GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
DR   GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
DR   GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
DR   GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
DR   GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
DR   GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
DR   GO; GO:0001964; P:startle response; IEA:Ensembl.
DR   InterPro; IPR000210; BTB/POZ_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR   InterPro; IPR004048; K_chnl_volt-dep_Kv1.1.
DR   InterPro; IPR011333; SKP1/BTB/POZ.
DR   InterPro; IPR003131; T1-type_BTB.
DR   InterPro; IPR028325; VG_K_chnl.
DR   PANTHER; PTHR11537; PTHR11537; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01508; KV11CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   PRINTS; PR01496; SHAKERCHANEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; SSF54695; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cell junction; Cell membrane; Cell projection;
KW   Complete proteome; Cytoplasmic vesicle; Disease mutation;
KW   Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport;
KW   Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   RNA editing; Synapse; Transmembrane; Transmembrane helix; Transport;
KW   Voltage-gated channel.
FT   CHAIN         1    495       Potassium voltage-gated channel subfamily
FT                                A member 1.
FT                                /FTId=PRO_0000053968.
FT   TOPO_DOM      1    164       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    165    186       Helical; Name=Segment S1.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    187    220       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    221    242       Helical; Name=Segment S2.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    243    253       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    254    274       Helical; Name=Segment S3.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    275    287       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    288    308       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    309    323       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    324    345       Helical; Name=Segment S5.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    346    359       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    360    371       Helical; Name=Pore helix.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   INTRAMEM    372    379       {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    380    386       Extracellular.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TRANSMEM    387    415       Helical; Name=Segment S6.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   TOPO_DOM    416    495       Cytoplasmic.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   REGION        1    128       Tetramerization domain.
FT                                {ECO:0000250|UniProtKB:P10499}.
FT   REGION      310    323       S4-S5 linker.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       372    377       Selectivity filter.
FT                                {ECO:0000250|UniProtKB:P63142}.
FT   MOTIF       493    495       PDZ-binding. {ECO:0000250}.
FT   MOD_RES      23     23       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P10499}.
FT   MOD_RES     322    322       Phosphoserine; by PKA. {ECO:0000255}.
FT   MOD_RES     437    437       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P10499}.
FT   MOD_RES     439    439       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P10499}.
FT   MOD_RES     446    446       Phosphoserine; by PKA.
FT                                {ECO:0000305|PubMed:23774215}.
FT   LIPID       243    243       S-palmitoyl cysteine.
FT                                {ECO:0000269|PubMed:15837928}.
FT   CARBOHYD    207    207       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   VARIANT     174    174       V -> F (in EA1; dbSNP:rs104894349).
FT                                {ECO:0000269|PubMed:7842011,
FT                                ECO:0000269|PubMed:8541859}.
FT                                /FTId=VAR_001508.
FT   VARIANT     177    177       I -> R (in EA1).
FT                                {ECO:0000269|PubMed:9600245}.
FT                                /FTId=VAR_001509.
FT   VARIANT     184    184       F -> C (in EA1; alters voltage dependence
FT                                and kinetics of activation though not of
FT                                C-type inactivation; dbSNP:rs104894357).
FT                                {ECO:0000269|PubMed:8541859,
FT                                ECO:0000269|PubMed:8845167}.
FT                                /FTId=VAR_020830.
FT   VARIANT     204    204       R -> H (in dbSNP:rs2229000).
FT                                /FTId=VAR_020051.
FT   VARIANT     226    226       T -> A (in EA1; dbSNP:rs104894354).
FT                                {ECO:0000269|PubMed:9600245}.
FT                                /FTId=VAR_001510.
FT   VARIANT     226    226       T -> K (in MK1; induces a reduced efflux
FT                                of potassium ions during depolarization
FT                                which results in increased muscle cell
FT                                activity; coexpression studies of the
FT                                mutant protein with the wild-type protein
FT                                produces significantly reduced currents
FT                                suggesting a severe effect of the
FT                                mutation; dbSNP:rs28933383).
FT                                {ECO:0000269|PubMed:17136396}.
FT                                /FTId=VAR_037100.
FT   VARIANT     226    226       T -> M (in EA1; dbSNP:rs28933383).
FT                                {ECO:0000269|PubMed:8871592}.
FT                                /FTId=VAR_020831.
FT   VARIANT     226    226       T -> R (in EA1; yields currents with a
FT                                largely reduced amplitude;
FT                                dbSNP:rs28933383).
FT                                {ECO:0000269|PubMed:10355668}.
FT                                /FTId=VAR_037101.
FT   VARIANT     239    239       R -> S (in EA1; dbSNP:rs104894348).
FT                                {ECO:0000269|PubMed:7842011}.
FT                                /FTId=VAR_001511.
FT   VARIANT     242    242       A -> P (in MK1; 10% reduction of mean
FT                                peak current amplitudes compared to wil-
FT                                dtype; mutant and wild-type expression
FT                                together is consistent with a loss-of-
FT                                function effect of the mutation;
FT                                dbSNP:rs28933381).
FT                                {ECO:0000269|PubMed:11026449}.
FT                                /FTId=VAR_037102.
FT   VARIANT     244    244       P -> H (in MK1; does not affect channel
FT                                activity; dbSNP:rs28933382).
FT                                {ECO:0000269|PubMed:11026449}.
FT                                /FTId=VAR_037103.
FT   VARIANT     249    249       F -> I (in EA1; dbSNP:rs104894356).
FT                                {ECO:0000269|PubMed:7842011}.
FT                                /FTId=VAR_001512.
FT   VARIANT     255    255       N -> D (in MK1; strongly reduces the
FT                                activity of homomeric channels with
FT                                dominant negative effects on wild-type
FT                                channels; dbSNP:rs121918067).
FT                                {ECO:0000269|PubMed:19307729}.
FT                                /FTId=VAR_072397.
FT   VARIANT     325    325       E -> D (in EA1; results in non-functional
FT                                homomeric channels; accelerates recovery
FT                                from N-type inactivation due to
FT                                interaction with KCNAB1; slows down N-
FT                                type inactivation of heteromeric channels
FT                                formed by KCNA1 and KCNA4;
FT                                dbSNP:rs104894353).
FT                                {ECO:0000269|PubMed:12077175,
FT                                ECO:0000269|PubMed:17156368,
FT                                ECO:0000269|PubMed:8541859,
FT                                ECO:0000269|PubMed:8845167}.
FT                                /FTId=VAR_020832.
FT   VARIANT     329    329       L -> I (in EA1).
FT                                {ECO:0000269|PubMed:11013453}.
FT                                /FTId=VAR_020833.
FT   VARIANT     342    342       S -> I (in EA1; phenotype without
FT                                myokymia). {ECO:0000269|PubMed:15532032}.
FT                                /FTId=VAR_020834.
FT   VARIANT     400    400       I -> V (in RNA edited version).
FT                                /FTId=VAR_016805.
FT   VARIANT     404    404       V -> I (in EA1; results in slower channel
FT                                activation compared to wild-type; slows
FT                                down N-type inactivation of heteromeric
FT                                channels formed by KCNA1 and KCNA4;
FT                                dbSNP:rs104894355).
FT                                {ECO:0000269|PubMed:11026449,
FT                                ECO:0000269|PubMed:17156368,
FT                                ECO:0000269|PubMed:9600245}.
FT                                /FTId=VAR_001513.
FT   VARIANT     405    405       P -> L (probable disease-associated
FT                                mutation found in a patient with neonatal
FT                                onset epileptic encephalopathy).
FT                                {ECO:0000269|PubMed:27864847}.
FT                                /FTId=VAR_078205.
FT   VARIANT     408    408       V -> A (in EA1; channels have voltage
FT                                dependence similar to that of wild-type
FT                                channels but with faster kinetics and
FT                                increased C-type inactivation;
FT                                accelerates recovery from N-type
FT                                inactivation due to interaction with
FT                                KCNAB1; slows down N-type inactivation of
FT                                heteromeric channels formed by KCNA1 and
FT                                KCNA4; dbSNP:rs104894352).
FT                                {ECO:0000269|PubMed:12077175,
FT                                ECO:0000269|PubMed:17156368,
FT                                ECO:0000269|PubMed:7842011,
FT                                ECO:0000269|PubMed:8845167}.
FT                                /FTId=VAR_001514.
FT   MUTAGEN      35     36       CC->AA: No effect on palmitoylation, no
FT                                effect on current kinetics.
FT                                {ECO:0000269|PubMed:15837928}.
FT   MUTAGEN     177    177       I->N: Slows down N-type inactivation of
FT                                heteromeric channels formed by KCNA1 and
FT                                KCNA4. {ECO:0000269|PubMed:17156368}.
FT   MUTAGEN     243    243       C->A: Strongly decreases palmitoylation
FT                                and alters current kinetics.
FT                                {ECO:0000269|PubMed:15837928}.
FT   MUTAGEN     255    255       N->A,H,T: Slightly increases channel
FT                                activity, but does not affect expression
FT                                at the cell membrane.
FT                                {ECO:0000269|PubMed:19307729}.
FT   MUTAGEN     255    255       N->E: Abolishes channel activity, but
FT                                does not affect expression at the cell
FT                                membrane. {ECO:0000269|PubMed:19307729}.
FT   MUTAGEN     255    255       N->Q: Strongly reduces channel activity,
FT                                but does not affect expression at the
FT                                cell membrane.
FT                                {ECO:0000269|PubMed:19307729}.
FT   MUTAGEN     255    255       N->V: No effect on channel activity.
FT                                {ECO:0000269|PubMed:19307729}.
FT   MUTAGEN     446    446       S->A: Impairs phosphorylation by PKA.
FT                                {ECO:0000269|PubMed:23774215}.
FT   MUTAGEN     446    446       S->E: Impairs expression at the cell
FT                                membrane. {ECO:0000269|PubMed:23774215}.
FT   CONFLICT    265    265       Missing (in Ref. 5; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    315    315       L -> R (in Ref. 5; no nucleotide entry).
FT                                {ECO:0000305}.
FT   CONFLICT    452    452       S -> Y (in Ref. 1; AAA36139).
FT                                {ECO:0000305}.
SQ   SEQUENCE   495 AA;  56466 MW;  0A1B1AB87BCDDEBA CRC64;
     MTVMSGENVD EASAAPGHPQ DGSYPRQADH DDHECCERVV INISGLRFET QLKTLAQFPN
     TLLGNPKKRM RYFDPLRNEY FFDRNRPSFD AILYYYQSGG RLRRPVNVPL DMFSEEIKFY
     ELGEEAMEKF REDEGFIKEE ERPLPEKEYQ RQVWLLFEYP ESSGPARVIA IVSVMVILIS
     IVIFCLETLP ELKDDKDFTG TVHRIDNTTV IYNSNIFTDP FFIVETLCII WFSFELVVRF
     FACPSKTDFF KNIMNFIDIV AIIPYFITLG TEIAEQEGNQ KGEQATSLAI LRVIRLVRVF
     RIFKLSRHSK GLQILGQTLK ASMRELGLLI FFLFIGVILF SSAVYFAEAE EAESHFSSIP
     DAFWWAVVSM TTVGYGDMYP VTIGGKIVGS LCAIAGVLTI ALPVPVIVSN FNYFYHRETE
     GEEQAQLLHV SSPNLASDSD LSRRSSSTMS KSEYMEIEED MNNSIAHYRQ VNIRTANCTT
     ANQNCVNKSK LLTDV
//
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