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Potassium voltage-gated channel subfamily A member 1 (Voltage-gated K( ) channel HuKI) (Voltage-gated potassium channel HBK1) (Voltage-gated potassium channel subunit Kv1.1)

 KCNA1_HUMAN             Reviewed;         495 AA.
Q09470; A6NM83; Q3MIQ9;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
10-FEB-2009, sequence version 2.
18-JUL-2018, entry version 188.
RecName: Full=Potassium voltage-gated channel subfamily A member 1;
AltName: Full=Voltage-gated K(+) channel HuKI {ECO:0000303|PubMed:19912772};
AltName: Full=Voltage-gated potassium channel HBK1 {ECO:0000303|PubMed:2128063};
AltName: Full=Voltage-gated potassium channel subunit Kv1.1;
Name=KCNA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND ENZYME
REGULATION.
TISSUE=Brain;
PubMed=19912772; DOI=10.1016/1044-7431(90)90004-N;
Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.;
"Human potassium channel genes: molecular cloning and functional
expression.";
Mol. Cell. Neurosci. 1:214-223(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain cortex;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 263-315.
PubMed=2128063;
Freeman S.N., Conley E.C., Brennand J.C., Russell N.J.W.,
Brammar W.J.;
"Cloning and characterization of a cDNA encoding a human brain
potassium channel.";
Biochem. Soc. Trans. 18:891-892(1990).
[6]
INTERACTION WITH KCNA2 AND KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, 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).
[7]
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).
[8]
PALMITOYLATION AT CYS-243, MUTAGENESIS OF 35-CYS--CYS-36 AND CYS-243,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15837928; DOI=10.1073/pnas.0501999102;
Gubitosi-Klug R.A., Mancuso D.J., Gross R.W.;
"The human Kv1.1 channel is palmitoylated, modulating voltage sensing:
Identification of a palmitoylation consensus sequence.";
Proc. Natl. Acad. Sci. U.S.A. 102:5964-5968(2005).
[9]
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).
[10]
INTERACTION WITH KCNRG, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19968958; DOI=10.1016/j.bbrc.2009.11.143;
Usman H., Mathew M.K.;
"Potassium channel regulator KCNRG regulates surface expression of
Shaker-type potassium channels.";
Biochem. Biophys. Res. Commun. 391:1301-1305(2010).
[11]
FUNCTION.
PubMed=21106501; DOI=10.1093/brain/awq318;
Tomlinson S.E., Tan S.V., Kullmann D.M., Griggs R.C., Burke D.,
Hanna M.G., Bostock H.;
"Nerve excitability studies characterize Kv1.1 fast potassium channel
dysfunction in patients with episodic ataxia type 1.";
Brain 133:3530-3540(2010).
[12]
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).
[13]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-446, AND MUTAGENESIS OF
SER-446.
PubMed=23774215; DOI=10.1158/0008-5472.CAN-12-3690;
Lallet-Daher H., Wiel C., Gitenay D., Navaratnam N., Augert A.,
Le Calve B., Verbeke S., Carling D., Aubert S., Vindrieux D.,
Bernard D.;
"Potassium channel KCNA1 modulates oncogene-induced senescence and
transformation.";
Cancer Res. 73:5253-5265(2013).
[14]
INTERACTION WITH ANK3, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23903368; DOI=10.1038/ki.2013.280;
San-Cristobal P., Lainez S., Dimke H., de Graaf M.J., Hoenderop J.G.,
Bindels R.J.;
"Ankyrin-3 is a novel binding partner of the voltage-gated potassium
channel Kv1.1 implicated in renal magnesium handling.";
Kidney Int. 85:94-102(2014).
[15]
VARIANTS EA1 PHE-174; SER-239; ILE-249 AND ALA-408.
PubMed=7842011; DOI=10.1038/ng1094-136;
Browne D.L., Gancher S.T., Nutt J.G., Brunt E.R.P., Smith E.A.,
Kramer P., Litt M.;
"Episodic ataxia/myokymia syndrome is associated with point mutations
in the human potassium channel gene, KCNA1.";
Nat. Genet. 8:136-140(1994).
[16]
VARIANTS EA1 PHE-174; CYS-184 AND ASP-325.
PubMed=8541859; DOI=10.1093/hmg/4.9.1671;
Browne D.L., Brunt E.R.P., Griggs R.C., Nutt J.G., Gancher S.T.,
Smith E.A., Litt M.;
"Identification of two new KCNA1 mutations in episodic ataxia/myokymia
families.";
Hum. Mol. Genet. 4:1671-1672(1995).
[17]
CHARACTERIZATION OF VARIANTS EA1 CYS-184; ASP-325 AND ALA-408.
PubMed=8845167; DOI=10.1016/0896-6273(95)90022-5;
Adelman J.P., Bond C.T., Pessia M., Maylie J.;
"Episodic ataxia results from voltage-dependent potassium channels
with altered functions.";
Neuron 15:1449-1454(1995).
[18]
VARIANT EA1 MET-226.
PubMed=8871592; DOI=10.1002/ana.410400422;
Comu S., Giuliani M., Narayanan V.;
"Episodic ataxia and myokymia syndrome: a new mutation of potassium
channel gene Kv1.1.";
Ann. Neurol. 40:684-687(1996).
[19]
VARIANTS EA1 ARG-177; ALA-226 AND ILE-404.
PubMed=9600245; DOI=10.1007/s004390050722;
Scheffer H., Brunt E.R.P., Mol G.J.J., van der Vlies P., Stulp R.P.,
Verlind E., Mantel G., Averyanov Y.N., Hofstra R.M.W., Buys C.H.C.M.;
"Three novel KCNA1 mutations in episodic ataxia type I families.";
Hum. Genet. 102:464-466(1998).
[20]
VARIANT EA1 ARG-226, AND CHARACTERIZATION OF VARIANT EA1 ARG-226.
PubMed=10355668; DOI=10.1093/brain/122.5.817;
Zuberi S.M., Eunson L.H., Spauschus A., De Silva R., Tolmie J.,
Wood N.W., McWilliam R.C., Stephenson J.P.B., Kullmann D.M.,
Hanna M.G.;
"A novel mutation in the human voltage-gated potassium channel gene
(Kv1.1) associates with episodic ataxia type 1 and sometimes with
partial epilepsy.";
Brain 122:817-825(1999).
[21]
VARIANTS MK1 PRO-242 AND HIS-244, VARIANT EA1 ILE-404,
CHARACTERIZATION OF VARIANTS MK1 PRO-242 AND HIS-244, CHARACTERIZATION
OF VARIANT EA1 ILE-404, AND FUNCTION.
PubMed=11026449;
DOI=10.1002/1531-8249(200010)48:4<647::AID-ANA12>3.3.CO;2-H;
Eunson L.H., Rea R., Zuberi S.M., Youroukos S., Panayiotopoulos C.P.,
Liguori R., Avoni P., McWilliam R.C., Stephenson J.B.P., Hanna M.G.,
Kullmann D.M., Spauschus A.;
"Clinical, genetic, and expression studies of mutations in the
potassium channel gene KCNA1 reveal new phenotypic variability.";
Ann. Neurol. 48:647-656(2000).
[22]
VARIANT EA1 ILE-329.
PubMed=11013453;
DOI=10.1002/1098-1004(200010)16:4<374::AID-HUMU15>3.3.CO;2-W;
Knight M.A., Storey E., McKinlay Gardner R.J., Hand P., Forrest S.M.;
"Identification of a novel missense mutation L329I in the episodic
ataxia type 1 gene KCNA1 -- a challenging problem.";
Hum. Mutat. 16:374-374(2000).
[23]
CHARACTERIZATION OF VARIANTS EA1 ASP-325 AND ALA-408, FUNCTION,
SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNAB1.
PubMed=12077175;
Maylie B., Bissonnette E., Virk M., Adelman J.P., Maylie J.G.;
"Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel
alter hKvbeta 1-induced N-type inactivation.";
J. Neurosci. 22:4786-4793(2002).
[24]
VARIANT EA1 ILE-342.
PubMed=15532032; DOI=10.1002/humu.9295;
Lee H., Wang H., Jen J.C., Sabatti C., Baloh R.W., Nelson S.F.;
"A novel mutation in KCNA1 causes episodic ataxia without myokymia.";
Hum. Mutat. 24:536-536(2004).
[25]
CHARACTERIZATION OF VARIANTS EA1 ASP-325; ILE-404 AND ALA-408,
MUTAGENESIS OF ILE-177, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
"Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
inactivation properties of the human potassium channels Kv1.4-
1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2.";
Eur. J. Neurosci. 24:3073-3083(2006).
[26]
VARIANT MK1 LYS-226, CHARACTERIZATION OF VARIANT MK1 LYS-226,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17136396; DOI=10.1007/s10048-006-0071-z;
Chen H., von Hehn C., Kaczmarek L.K., Ment L.R., Pober B.R.,
Hisama F.M.;
"Functional analysis of a novel potassium channel (KCNA1) mutation in
hereditary myokymia.";
Neurogenetics 8:131-135(2007).
[27]
VARIANT MK1 ASP-255, CHARACTERIZATION OF VARIANT MK1 ASP-255,
FUNCTION, SUBCELLULAR LOCATION, AND ENZYME REGULATION.
PubMed=19307729; DOI=10.1172/JCI36948;
Glaudemans B., van der Wijst J., Scola R.H., Lorenzoni P.J.,
Heister A., van der Kemp A.W., Knoers N.V., Hoenderop J.G.,
Bindels R.J.;
"A missense mutation in the Kv1.1 voltage-gated potassium channel-
encoding gene KCNA1 is linked to human autosomal dominant
hypomagnesemia.";
J. Clin. Invest. 119:936-942(2009).
[28]
CHARACTERIZATION OF VARIANT MK1 ASP-255, MUTAGENESIS OF ASN-255,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19903818; DOI=10.1074/jbc.M109.041517;
van der Wijst J., Glaudemans B., Venselaar H., Nair A.V., Forst A.L.,
Hoenderop J.G., Bindels R.J.;
"Functional analysis of the Kv1.1 N255D mutation associated with
autosomal dominant hypomagnesemia.";
J. Biol. Chem. 285:171-178(2010).
[29]
VARIANT LEU-405.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D.,
Bigoni S., Barba C., Mari F., Montomoli M., Pisano T., Rosati A.,
Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
-!- 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 (PubMed:19903818). Contributes to the regulation of the
membrane potential and nerve signaling, and prevents neuronal
hyperexcitability (PubMed:17156368). 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:19912772). 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:12077175, PubMed:17156368). 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:12077175, PubMed:17156368). 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:19912772, PubMed:19968958,
PubMed:19307729, PubMed:19903818). In contrast, a heterotetrameric
channel formed by KCNA1 and KCNA4 shows rapid inactivation
(PubMed:17156368). 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 (By similarity). May function as down-
stream effector for G protein-coupled receptors and inhibit
GABAergic inputs to basolateral amygdala neurons (By similarity).
May contribute to the regulation of neurotransmitter release, such
as gamma-aminobutyric acid (GABA) release (By similarity). 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:11026449, PubMed:17136396). 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 (PubMed:23903368, PubMed:19307729).
{ECO:0000250|UniProtKB:P10499, ECO:0000269|PubMed:11026449,
ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:15837928,
ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:19307729, ECO:0000269|PubMed:19903818,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:19968958,
ECO:0000269|PubMed:21106501, ECO:0000269|PubMed:23903368}.
-!- ENZYME REGULATION: Inhibited by 1.1 mM 4-aminopyridine (4-AP) and
by 20 mM tetraethylammonium (TEA), but not by charybdotoxin
(CTX)(PubMed:19912772). Inhibited by dendrotoxin (DTX)
(PubMed:19307729). {ECO:0000269|PubMed:19307729,
ECO:0000269|PubMed:19912772}.
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNA2, KCNA4, KCNA5, KCNA6 and
KCNA7 (PubMed:12077175, PubMed:17156368). Channel activity is
regulated by interaction with the beta subunits KCNAB1 and KCNAB2
(PubMed:12077175, PubMed:17156368). Identified in a complex with
KCNA2 and KCNAB2 (PubMed:11086297). Interacts (via C-terminus)
with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity).
Interacts with LGI1 within a complex containing LGI1, KCNA4 and
KCNAB1 (By similarity). Interacts (via N-terminus) with STX1A;
this promotes channel inactivation (By similarity). Interacts (via
N-terminus) with the heterodimer formed by GNB1 and GNG2; this
promotes channel inactivation (By similarity). Can interact
simultaneously with STX1A and the heterodimer formed by GNB1 and
GNG2 (By similarity). Interacts (via cytoplasmic N-terminal
domain) with KCNRG; this inhibits channel activity
(PubMed:19968958). Interacts with ANK3; this inhibits channel
activity (PubMed:23903368). {ECO:0000250|UniProtKB:P10499,
ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:23903368,
ECO:0000305}.
-!- INTERACTION:
Q62936:Dlg3 (xeno); NbExp=2; IntAct=EBI-8286599, EBI-349596;
P78352:DLG4; NbExp=2; IntAct=EBI-8286599, EBI-80389;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12077175,
ECO:0000269|PubMed:15837928, ECO:0000269|PubMed:17136396,
ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:19307729,
ECO:0000269|PubMed:19903818, ECO:0000269|PubMed:19912772,
ECO:0000269|PubMed:19968958, ECO:0000269|PubMed:23903368}; Multi-
pass membrane protein {ECO:0000305}. Membrane
{ECO:0000269|PubMed:11086297}. Cell projection, axon
{ECO:0000269|PubMed:11086297}. Cytoplasmic vesicle
{ECO:0000269|PubMed:23774215}. Perikaryon
{ECO:0000250|UniProtKB:P10499}. Endoplasmic reticulum
{ECO:0000250|UniProtKB:P10499}. 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:0000250|UniProtKB:P10499}.
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 (By similarity).
Detected at axon terminals (By similarity).
{ECO:0000250|UniProtKB:P10499, ECO:0000250|UniProtKB:P16388}.
-!- TISSUE SPECIFICITY: 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 (at protein
level) (PubMed:11086297). Detected in the islet of Langerhans
(PubMed:21483673). {ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:21483673}.
-!- DOMAIN: The cytoplasmic N-terminus is important for
tetramerization and for interaction with the beta subunits that
promote rapid channel closure. {ECO:0000250|UniProtKB:P10499}.
-!- 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: N-glycosylated. {ECO:0000250|UniProtKB:P10499}.
-!- PTM: Palmitoylated on Cys-243; which may be required for membrane
targeting. {ECO:0000269|PubMed:15837928}.
-!- PTM: Phosphorylated on tyrosine residues. Phosphorylation
increases in response to NRG1; this inhibits channel activity (By
similarity). Phosphorylation at Ser-446 regulates channel activity
by down-regulating expression at the cell membrane
(PubMed:23774215). {ECO:0000250|UniProtKB:P16388,
ECO:0000269|PubMed:23774215}.
-!- RNA EDITING: Modified_positions=400 {ECO:0000269|PubMed:12907802};
Note=Partially edited. RNA editing varies from 17% in the caudate
nucleus to 68% in the spinal cord and to 77% in the medulla.;
-!- DISEASE: Episodic ataxia 1 (EA1) [MIM:160120]: An autosomal
dominant disorder characterized by brief episodes of ataxia and
dysarthria. Neurological examination during and between the
attacks demonstrates spontaneous, repetitive discharges in the
distal musculature (myokymia) that arise from peripheral nerve.
Nystagmus is absent. {ECO:0000269|PubMed:10355668,
ECO:0000269|PubMed:11013453, ECO:0000269|PubMed:11026449,
ECO:0000269|PubMed:12077175, ECO:0000269|PubMed:15532032,
ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:7842011,
ECO:0000269|PubMed:8541859, ECO:0000269|PubMed:8845167,
ECO:0000269|PubMed:8871592, ECO:0000269|PubMed:9600245}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Myokymia isolated 1 (MK1) [MIM:160120]: A condition
characterized by spontaneous involuntary contraction of muscle
fiber groups that can be observed as vermiform movement of the
overlying skin. Electromyography typically shows continuous motor
unit activity with spontaneous oligo- and multiplet-discharges of
high intraburst frequency (myokymic discharges). Isolated
spontaneous muscle twitches occur in many persons and have no
grave significance. {ECO:0000269|PubMed:11026449,
ECO:0000269|PubMed:17136396, ECO:0000269|PubMed:19307729,
ECO:0000269|PubMed:19903818}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; L02750; AAA36139.1; -; mRNA.
EMBL; AC006063; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471116; EAW88833.1; -; Genomic_DNA.
EMBL; BC101733; AAI01734.1; -; mRNA.
EMBL; BC112180; AAI12181.1; -; mRNA.
CCDS; CCDS8535.1; -.
PIR; I57680; I57680.
RefSeq; NP_000208.2; NM_000217.2.
UniGene; Hs.416139; -.
PDB; 2AFL; Model; -; A/B/C/D=326-407.
PDBsum; 2AFL; -.
ProteinModelPortal; Q09470; -.
SMR; Q09470; -.
BioGrid; 109939; 7.
CORUM; Q09470; -.
IntAct; Q09470; 15.
MINT; Q09470; -.
STRING; 9606.ENSP00000371985; -.
BindingDB; Q09470; -.
ChEMBL; CHEMBL2309; -.
DrugBank; DB00321; Amitriptyline.
DrugBank; DB06637; Dalfampridine.
DrugBank; DB01189; Desflurane.
DrugBank; DB00228; Enflurane.
DrugBank; DB00753; Isoflurane.
DrugBank; DB01028; Methoxyflurane.
DrugBank; DB01115; Nifedipine.
DrugBank; DB01236; Sevoflurane.
GuidetoPHARMACOLOGY; 538; -.
TCDB; 1.A.1.2.12; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q09470; -.
PhosphoSitePlus; Q09470; -.
SwissPalm; Q09470; -.
BioMuta; KCNA1; -.
DMDM; 223590092; -.
MaxQB; Q09470; -.
PaxDb; Q09470; -.
PeptideAtlas; Q09470; -.
PRIDE; Q09470; -.
ProteomicsDB; 58722; -.
Ensembl; ENST00000382545; ENSP00000371985; ENSG00000111262.
GeneID; 3736; -.
KEGG; hsa:3736; -.
UCSC; uc001qnh.4; human.
CTD; 3736; -.
DisGeNET; 3736; -.
EuPathDB; HostDB:ENSG00000111262.4; -.
GeneCards; KCNA1; -.
GeneReviews; KCNA1; -.
HGNC; HGNC:6218; KCNA1.
HPA; CAB022365; -.
MalaCards; KCNA1; -.
MIM; 160120; phenotype.
MIM; 176260; gene.
neXtProt; NX_Q09470; -.
OpenTargets; ENSG00000111262; -.
Orphanet; 37612; Episodic ataxia type 1.
Orphanet; 972; Hereditary continuous muscle fiber activity.
Orphanet; 199326; Isolated autosomal dominant hypomagnesemia, Glaudemans type.
PharmGKB; PA30019; -.
eggNOG; KOG1545; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231015; -.
HOVERGEN; HBG052230; -.
InParanoid; Q09470; -.
KO; K04874; -.
OMA; AHYRQAN; -.
OrthoDB; EOG091G10NU; -.
PhylomeDB; Q09470; -.
TreeFam; TF313103; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
ChiTaRS; KCNA1; human.
GeneWiki; Kv1.1; -.
GenomeRNAi; 3736; -.
PRO; PR:Q09470; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111262; -.
CleanEx; HS_KCNA1; -.
ExpressionAtlas; Q09470; baseline and differential.
Genevisible; Q09470; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; ISS:UniProtKB.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS: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; ISS:UniProtKB.
GO; GO:0033270; C:paranode region of axon; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0097718; F:disordered domain specific binding; IPI:CAFA.
GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
GO; GO:0015079; F:potassium ion transmembrane transporter activity; TAS:ProtInc.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0010644; P:cell communication by electrical coupling; ISS:UniProtKB.
GO; GO:0034613; P:cellular protein localization; IEA:Ensembl.
GO; GO:0071286; P:cellular response to magnesium ion; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:ProtInc.
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; IEA:Ensembl.
GO; GO:0010960; P:magnesium ion homeostasis; IMP:UniProtKB.
GO; GO:0007405; P:neuroblast proliferation; IEA:Ensembl.
GO; GO:0050905; P:neuromuscular process; IMP:UniProtKB.
GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
GO; GO:0023041; P:neuronal signal transduction; ISS:UniProtKB.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0042391; P:regulation of membrane potential; IMP:UniProtKB.
GO; GO:0006937; P:regulation of muscle contraction; ISS:UniProtKB.
GO; GO:0001964; P:startle response; IEA:Ensembl.
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; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Ion channel; Ion transport;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
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_0000053968.
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:0000250|UniProtKB:P10499}.
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:0000250}.
MOD_RES 23 23 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 322 322 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 437 437 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 439 439 Phosphoserine.
{ECO:0000250|UniProtKB:P10499}.
MOD_RES 446 446 Phosphoserine; by PKA.
{ECO:0000305|PubMed:23774215}.
LIPID 243 243 S-palmitoyl cysteine.
{ECO:0000269|PubMed:15837928}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 174 174 V -> F (in EA1; dbSNP:rs104894349).
{ECO:0000269|PubMed:7842011,
ECO:0000269|PubMed:8541859}.
/FTId=VAR_001508.
VARIANT 177 177 I -> R (in EA1).
{ECO:0000269|PubMed:9600245}.
/FTId=VAR_001509.
VARIANT 184 184 F -> C (in EA1; alters voltage dependence
and kinetics of activation though not of
C-type inactivation; dbSNP:rs104894357).
{ECO:0000269|PubMed:8541859,
ECO:0000269|PubMed:8845167}.
/FTId=VAR_020830.
VARIANT 204 204 R -> H (in dbSNP:rs2229000).
/FTId=VAR_020051.
VARIANT 226 226 T -> A (in EA1; dbSNP:rs104894354).
{ECO:0000269|PubMed:9600245}.
/FTId=VAR_001510.
VARIANT 226 226 T -> K (in MK1; induces a reduced efflux
of potassium ions during depolarization
which results in increased muscle cell
activity; coexpression studies of the
mutant protein with the wild-type protein
produces significantly reduced currents
suggesting a severe effect of the
mutation; dbSNP:rs28933383).
{ECO:0000269|PubMed:17136396}.
/FTId=VAR_037100.
VARIANT 226 226 T -> M (in EA1; dbSNP:rs28933383).
{ECO:0000269|PubMed:8871592}.
/FTId=VAR_020831.
VARIANT 226 226 T -> R (in EA1; yields currents with a
largely reduced amplitude;
dbSNP:rs28933383).
{ECO:0000269|PubMed:10355668}.
/FTId=VAR_037101.
VARIANT 239 239 R -> S (in EA1; dbSNP:rs104894348).
{ECO:0000269|PubMed:7842011}.
/FTId=VAR_001511.
VARIANT 242 242 A -> P (in MK1; 10% reduction of mean
peak current amplitudes compared to wil-
dtype; mutant and wild-type expression
together is consistent with a loss-of-
function effect of the mutation;
dbSNP:rs28933381).
{ECO:0000269|PubMed:11026449}.
/FTId=VAR_037102.
VARIANT 244 244 P -> H (in MK1; does not affect channel
activity; dbSNP:rs28933382).
{ECO:0000269|PubMed:11026449}.
/FTId=VAR_037103.
VARIANT 249 249 F -> I (in EA1; dbSNP:rs104894356).
{ECO:0000269|PubMed:7842011}.
/FTId=VAR_001512.
VARIANT 255 255 N -> D (in MK1; strongly reduces the
activity of homomeric channels with
dominant negative effects on wild-type
channels; dbSNP:rs121918067).
{ECO:0000269|PubMed:19307729}.
/FTId=VAR_072397.
VARIANT 325 325 E -> D (in EA1; results in non-functional
homomeric channels; accelerates recovery
from N-type inactivation due to
interaction with KCNAB1; slows down N-
type inactivation of heteromeric channels
formed by KCNA1 and KCNA4;
dbSNP:rs104894353).
{ECO:0000269|PubMed:12077175,
ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:8541859,
ECO:0000269|PubMed:8845167}.
/FTId=VAR_020832.
VARIANT 329 329 L -> I (in EA1).
{ECO:0000269|PubMed:11013453}.
/FTId=VAR_020833.
VARIANT 342 342 S -> I (in EA1; phenotype without
myokymia). {ECO:0000269|PubMed:15532032}.
/FTId=VAR_020834.
VARIANT 400 400 I -> V (in RNA edited version).
/FTId=VAR_016805.
VARIANT 404 404 V -> I (in EA1; results in slower channel
activation compared to wild-type; slows
down N-type inactivation of heteromeric
channels formed by KCNA1 and KCNA4;
dbSNP:rs104894355).
{ECO:0000269|PubMed:11026449,
ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:9600245}.
/FTId=VAR_001513.
VARIANT 405 405 P -> L (probable disease-associated
mutation found in a patient with neonatal
onset epileptic encephalopathy).
{ECO:0000269|PubMed:27864847}.
/FTId=VAR_078205.
VARIANT 408 408 V -> A (in EA1; channels have voltage
dependence similar to that of wild-type
channels but with faster kinetics and
increased C-type inactivation;
accelerates recovery from N-type
inactivation due to interaction with
KCNAB1; slows down N-type inactivation of
heteromeric channels formed by KCNA1 and
KCNA4; dbSNP:rs104894352).
{ECO:0000269|PubMed:12077175,
ECO:0000269|PubMed:17156368,
ECO:0000269|PubMed:7842011,
ECO:0000269|PubMed:8845167}.
/FTId=VAR_001514.
MUTAGEN 35 36 CC->AA: No effect on palmitoylation, no
effect on current kinetics.
{ECO:0000269|PubMed:15837928}.
MUTAGEN 177 177 I->N: Slows down N-type inactivation of
heteromeric channels formed by KCNA1 and
KCNA4. {ECO:0000269|PubMed:17156368}.
MUTAGEN 243 243 C->A: Strongly decreases palmitoylation
and alters current kinetics.
{ECO:0000269|PubMed:15837928}.
MUTAGEN 255 255 N->A,H,T: Slightly increases channel
activity, but does not affect expression
at the cell membrane.
{ECO:0000269|PubMed:19307729}.
MUTAGEN 255 255 N->E: Abolishes channel activity, but
does not affect expression at the cell
membrane. {ECO:0000269|PubMed:19307729}.
MUTAGEN 255 255 N->Q: Strongly reduces channel activity,
but does not affect expression at the
cell membrane.
{ECO:0000269|PubMed:19307729}.
MUTAGEN 255 255 N->V: No effect on channel activity.
{ECO:0000269|PubMed:19307729}.
MUTAGEN 446 446 S->A: Impairs phosphorylation by PKA.
{ECO:0000269|PubMed:23774215}.
MUTAGEN 446 446 S->E: Impairs expression at the cell
membrane. {ECO:0000269|PubMed:23774215}.
CONFLICT 265 265 Missing (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 315 315 L -> R (in Ref. 5; no nucleotide entry).
{ECO:0000305}.
CONFLICT 452 452 S -> Y (in Ref. 1; AAA36139).
{ECO:0000305}.
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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