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Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (h-DRK1) (Voltage-gated potassium channel subunit Kv2.1)

 KCNB1_HUMAN             Reviewed;         858 AA.
Q14721; Q14193;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
25-OCT-2002, sequence version 2.
20-JUN-2018, entry version 159.
RecName: Full=Potassium voltage-gated channel subfamily B member 1 {ECO:0000312|HGNC:HGNC:6231};
AltName: Full=Delayed rectifier potassium channel 1 {ECO:0000303|PubMed:8081723};
Short=DRK1 {ECO:0000303|PubMed:8081723};
Short=h-DRK1 {ECO:0000303|PubMed:8081723};
AltName: Full=Voltage-gated potassium channel subunit Kv2.1 {ECO:0000303|PubMed:8081723};
Name=KCNB1 {ECO:0000312|HGNC:HGNC:6231};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND SUBCELLULAR
LOCATION.
PubMed=8081723;
Albrecht B., Lorra C., Stocker K., Pongs O.;
"Cloning and characterization of a human delayed rectifier potassium
channel gene.";
Recept. Channels 1:99-110(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
TISSUE=Brain cortex;
PubMed=1283219; DOI=10.1007/BF00370422;
Ikeda S.R., Soler F., Zuhlke R.D., Joho R.H., Lewis D.L.;
"Heterologous expression of the human potassium channel Kv2.1 in
clonal mammalian cells by direct cytoplasmic microinjection of cRNA.";
Pflugers Arch. 422:201-203(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens epithelium;
Rae J.L., Shepard A.R.;
"Identification of potassium channels in human lens epithelium.";
(In) Civan M.M. (eds.);
The eye's aqueous humor-from secretion to glaucoma, pp.69-104,
Academic Press, San Diego (1998).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[5]
FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR
LOCATION.
PubMed=10484328;
Shepard A.R., Rae J.L.;
"Electrically silent potassium channel subunits from human lens
epithelium.";
Am. J. Physiol. 277:C412-C424(1999).
[6]
REVIEW.
PubMed=10414301; DOI=10.1111/j.1749-6632.1999.tb11293.x;
Coetzee W.A., Amarillo Y., Chiu J., Chow A., Lau D., McCormack T.,
Moreno H., Nadal M.S., Ozaita A., Pountney D., Saganich M.,
Vega-Saenz de Miera E., Rudy B.;
"Molecular diversity of K+ channels.";
Ann. N. Y. Acad. Sci. 868:233-285(1999).
[7]
FUNCTION, SUBUNIT, INTERACTION WITH KCNG3, SELF-ASSOCIATION, DOMAIN,
BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
PubMed=11852086; DOI=10.1016/S0014-5793(02)02267-6;
Sano Y., Mochizuki S., Miyake A., Kitada C., Inamura K., Yokoi H.,
Nozawa K., Matsushime H., Furuichi K.;
"Molecular cloning and characterization of Kv6.3, a novel modulatory
subunit for voltage-gated K(+) channel Kv2.1.";
FEBS Lett. 512:230-234(2002).
[8]
TISSUE SPECIFICITY.
PubMed=12403834; DOI=10.1210/me.2002-0058;
MacDonald P.E., Wang G., Tsuk S., Dodo C., Kang Y., Tang L.,
Wheeler M.B., Cattral M.S., Lakey J.R., Salapatek A.M., Lotan I.,
Gaisano H.Y.;
"Synaptosome-associated protein of 25 kilodaltons modulates Kv2.1
voltage-dependent K(+) channels in neuroendocrine islet beta-cells
through an interaction with the channel N terminus.";
Mol. Endocrinol. 16:2452-2461(2002).
[9]
FUNCTION, SUBUNIT, INTERACTION WITH KCNG3; KCNH1 AND KCNH2,
SELF-ASSOCIATION, DOMAIN, AND SUBCELLULAR LOCATION.
PubMed=12060745; DOI=10.1073/pnas.122617999;
Ottschytsch N., Raes A., Van Hoorick D., Snyders D.J.;
"Obligatory heterotetramerization of three previously uncharacterized
Kv channel alpha-subunits identified in the human genome.";
Proc. Natl. Acad. Sci. U.S.A. 99:7986-7991(2002).
[10]
ENZYME REGULATION.
PubMed=14565763; DOI=10.1021/tx0341097;
Shiau Y.S., Huang P.T., Liou H.H., Liaw Y.C., Shiau Y.Y., Lou K.L.;
"Structural basis of binding and inhibition of novel tarantula toxins
in mammalian voltage-dependent potassium channels.";
Chem. Res. Toxicol. 16:1217-1225(2003).
[11]
FUNCTION, SELF-ASSOCIATION, DOMAIN, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF GLU-71 AND ASP-79.
PubMed=12560340; DOI=10.1074/jbc.M212973200;
Ju M., Stevens L., Leadbitter E., Wray D.;
"The Roles of N- and C-terminal determinants in the activation of the
Kv2.1 potassium channel.";
J. Biol. Chem. 278:12769-12778(2003).
[12]
TISSUE SPECIFICITY.
PubMed=14988243; DOI=10.2337/diabetes.53.3.597;
Yan L., Figueroa D.J., Austin C.P., Liu Y., Bugianesi R.M.,
Slaughter R.S., Kaczorowski G.J., Kohler M.G.;
"Expression of voltage-gated potassium channels in human and rhesus
pancreatic islets.";
Diabetes 53:597-607(2004).
[13]
REVIEW.
PubMed=15858231; DOI=10.1385/CBB:42:2:167;
Cox R.H.;
"Molecular determinants of voltage-gated potassium currents in
vascular smooth muscle.";
Cell Biochem. Biophys. 42:167-195(2005).
[14]
SUBUNIT.
PubMed=19357235; DOI=10.1152/ajpcell.00088.2009;
Bocksteins E., Raes A.L., Van de Vijver G., Bruyns T.,
Van Bogaert P.P., Snyders D.J.;
"Kv2.1 and silent Kv subunits underlie the delayed rectifier K+
current in cultured small mouse DRG neurons.";
Am. J. Physiol. 296:C1271-C1278(2009).
[15]
FUNCTION, SUBUNIT, INTERACTION WITH KCNG4, SELF-ASSOCIATION, DOMAIN,
SUBCELLULAR LOCATION, MUTAGENESIS OF HIS-105, AND TISSUE SPECIFICITY.
PubMed=19074135; DOI=10.1074/jbc.M808786200;
Mederos y Schnitzler M., Rinne S., Skrobek L., Renigunta V.,
Schlichthorl G., Derst C., Gudermann T., Daut J., Preisig-Muller R.;
"Mutation of histidine 105 in the T1 domain of the potassium channel
Kv2.1 disrupts heteromerization with Kv6.3 and Kv6.4.";
J. Biol. Chem. 284:4695-4704(2009).
[16]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-74 AND
ASP-75.
PubMed=19717558; DOI=10.1074/jbc.M109.039479;
Bocksteins E., Labro A.J., Mayeur E., Bruyns T., Timmermans J.P.,
Adriaensen D., Snyders D.J.;
"Conserved negative charges in the N-terminal tetramerization domain
mediate efficient assembly of Kv2.1 and Kv2.1/Kv6.4 channels.";
J. Biol. Chem. 284:31625-31634(2009).
[17]
FUNCTION, SUMOYLATION, DESUMOYLATION, INTERACTION WITH SUMO1, AND
SUBCELLULAR LOCATION.
PubMed=19223394; DOI=10.1242/jcs.036632;
Dai X.Q., Kolic J., Marchi P., Sipione S., Macdonald P.E.;
"SUMOylation regulates Kv2.1 and modulates pancreatic beta-cell
excitability.";
J. Cell Sci. 122:775-779(2009).
[18]
FUNCTION.
PubMed=23161216; DOI=10.1124/jpet.112.199083;
Li X.N., Herrington J., Petrov A., Ge L., Eiermann G., Xiong Y.,
Jensen M.V., Hohmeier H.E., Newgard C.B., Garcia M.L., Wagner M.,
Zhang B.B., Thornberry N.A., Howard A.D., Kaczorowski G.J., Zhou Y.P.;
"The role of voltage-gated potassium channels Kv2.1 and Kv2.2 in the
regulation of insulin and somatostatin release from pancreatic
islets.";
J. Pharmacol. Exp. Ther. 344:407-416(2013).
[19]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=24477962; DOI=10.1002/cne.23551;
King A.N., Manning C.F., Trimmer J.S.;
"A unique ion channel clustering domain on the axon initial segment of
mammalian neurons.";
J. Comp. Neurol. 522:2594-2608(2014).
[20]
FUNCTION, SUBUNIT, INTERACTION WITH KCNG4, SELF-ASSOCIATION, DOMAIN,
SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-74 AND ASP-75.
PubMed=24901643; DOI=10.1371/journal.pone.0098960;
Bocksteins E., Mayeur E., Van Tilborg A., Regnier G., Timmermans J.P.,
Snyders D.J.;
"The subfamily-specific interaction between Kv2.1 and Kv6.4 subunits
is determined by interactions between the N- and C-termini.";
PLoS ONE 9:E98960-E98960(2014).
[21]
VARIANTS EIEE26 ARG-347; ILE-374 AND ARG-379, CHARACTERIZATION OF
VARIANTS EIEE26 ARG-347; ILE-374 AND ARG-379, AND INVOLVEMENT IN
EIEE26.
PubMed=25164438; DOI=10.1002/ana.24263;
Torkamani A., Bersell K., Jorge B.S., Bjork R.L. Jr., Friedman J.R.,
Bloss C.S., Cohen J., Gupta S., Naidu S., Vanoye C.G.,
George A.L. Jr., Kearney J.A.;
"De novo KCNB1 mutations in epileptic encephalopathy.";
Ann. Neurol. 76:529-540(2014).
[22]
VARIANT EIEE26 ALA-378, CHARACTERIZATION OF VARIANT EIEE26 ALA-378,
AND SUBCELLULAR LOCATION.
PubMed=26503721; DOI=10.1085/jgp.201511444;
Thiffault I., Speca D.J., Austin D.C., Cobb M.M., Eum K.S.,
Safina N.P., Grote L., Farrow E.G., Miller N., Soden S.,
Kingsmore S.F., Trimmer J.S., Saunders C.J., Sack J.T.;
"A novel epileptic encephalopathy mutation in KCNB1 disrupts Kv2.1 ion
selectivity, expression, and localization.";
J. Gen. Physiol. 146:399-410(2015).
[23]
VARIANTS EIEE26 CYS-306 AND ARG-401, AND CHARACTERIZATION OF VARIANTS
EIEE26 CYS-306 AND ARG-401.
PubMed=26477325; DOI=10.1038/srep15199;
Saitsu H., Akita T., Tohyama J., Goldberg-Stern H., Kobayashi Y.,
Cohen R., Kato M., Ohba C., Miyatake S., Tsurusaki Y., Nakashima M.,
Miyake N., Fukuda A., Matsumoto N.;
"De novo KCNB1 mutations in infantile epilepsy inhibit repetitive
neuronal firing.";
Sci. Rep. 5:15199-15199(2015).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain, but also in the pancreas and
cardiovascular system. Contributes to the regulation of the action
potential (AP) repolarization, duration and frequency of
repetitive AP firing in neurons, muscle cells and endocrine cells
and plays a role in homeostatic attenuation of electrical
excitability throughout the brain (PubMed:23161216). Plays also a
role in the regulation of exocytosis independently of its
electrical function (By similarity). 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. Homotetrameric channels mediate a
delayed-rectifier voltage-dependent outward potassium current that
display rapid activation and slow inactivation in response to
membrane depolarization (PubMed:8081723, PubMed:1283219,
PubMed:10484328, PubMed:12560340, PubMed:19074135,
PubMed:19717558, PubMed:24901643). Can form functional
homotetrameric and heterotetrameric channels that contain variable
proportions of KCNB2; channel properties depend on the type of
alpha subunits that are part of the channel (By similarity). Can
also form functional heterotetrameric channels with other alpha
subunits that are non-conducting when expressed alone, such as
KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and
KCNV1, creating a functionally diverse range of channel complexes
(PubMed:10484328, PubMed:11852086, PubMed:12060745,
PubMed:19074135, PubMed:19717558, PubMed:24901643).
Heterotetrameric channel activity formed with KCNS3 show increased
current amplitude with the threshold for action potential
activation shifted towards more negative values in hypoxic-treated
pulmonary artery smooth muscle cells (By similarity). Channel
properties are also modulated by cytoplasmic ancillary beta
subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3, slowing
activation and inactivation rate of the delayed rectifier
potassium channels (By similarity). 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. Major
contributor to the slowly inactivating delayed-rectifier voltage-
gated potassium current in neurons of the central nervous system,
sympathetic ganglion neurons, neuroendocrine cells, pancreatic
beta cells, cardiomyocytes and smooth muscle cells. Mediates the
major part of the somatodendritic delayed-rectifier potassium
current in hippocampal and cortical pyramidal neurons and
sympathetic superior cervical ganglion (CGC) neurons that acts to
slow down periods of firing, especially during high frequency
stimulation. Plays a role in the induction of long-term
potentiation (LTP) of neuron excitability in the CA3 layer of the
hippocampus (By similarity). Contributes to the regulation of
glucose-induced action potential amplitude and duration in
pancreatic beta cells, hence limiting calcium influx and insulin
secretion (PubMed:23161216). Plays a role in the regulation of
resting membrane potential and contraction in hypoxia-treated
pulmonary artery smooth muscle cells. May contribute to the
regulation of the duration of both the action potential of
cardiomyocytes and the heart ventricular repolarization QT
interval. Contributes to the pronounced pro-apoptotic potassium
current surge during neuronal apoptotic cell death in response to
oxidative injury. May confer neuroprotection in response to
hypoxia/ischemic insults by suppressing pyramidal neurons
hyperexcitability in hippocampal and cortical regions (By
similarity). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to the
cell surface membrane, presumably by forming heterotetrameric
channels with these subunits (PubMed:12060745). Plays a role in
the calcium-dependent recruitment and release of fusion-competent
vesicles from the soma of neurons, neuroendocrine and glucose-
induced pancreatic beta cells by binding key components of the
fusion machinery in a pore-independent manner (By similarity).
{ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717,
ECO:0000269|PubMed:10484328, ECO:0000269|PubMed:11852086,
ECO:0000269|PubMed:12060745, ECO:0000269|PubMed:12560340,
ECO:0000269|PubMed:1283219, ECO:0000269|PubMed:19074135,
ECO:0000269|PubMed:19717558, ECO:0000269|PubMed:23161216,
ECO:0000269|PubMed:24901643, ECO:0000269|PubMed:8081723}.
-!- ENZYME REGULATION: Inhibited by 12.7 nM stromatoxin 1 (ScTx1), a
spider venom toxin of the tarantula S.calceata (PubMed:14565763).
Inhibited by 42 nM hanatoxin 1 (HaTx1), a spider venom toxin of
the tarantula G.spatulata (PubMed:14565763). Modestly sensitive to
millimolar levels of tetraethylammonium (TEA) (PubMed:8081723,
PubMed:1283219). Modestly sensitive to millimolar levels of 4-
aminopyridine (4-AP). Completely insensitive to toxins such as
dendrotoxin (DTX) and charybdotoxin (CTX) (By similarity).
{ECO:0000250|UniProtKB:P15387, ECO:0000269|PubMed:1283219,
ECO:0000269|PubMed:14565763, ECO:0000269|PubMed:8081723,
ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels expressed in xenopus oocytes or in
mammalian non-neuronal cells display delayed-rectifier voltage-
dependent potassium currents which are activated during membrane
depolarization, i.e within a risetime of about 20 msec
(PubMed:8081723, PubMed:1283219). After that, inactivate very
slowly, i.e within more than 5 sec (PubMed:8081723,
PubMed:1283219). Their activation requires low threshold
potentials of about -20 to -30 mV, with a midpoint activation at
about 10 mV. For inactivation, the voltage at half-maximal
amplitude is about -20 mV (PubMed:11852086). The time constant
for recovery after inactivation is about 1.6 sec. Channels have
an unitary conductance of about 8 pS (PubMed:10484328). The
voltage-dependence of activation and inactivation and other
channel characteristics vary depending on the experimental
conditions, the expression system, the presence or absence of
ancillary subunits and post-translational modifications.
{ECO:0000250|UniProtKB:P15387, ECO:0000269|PubMed:10484328,
ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:1283219,
ECO:0000269|PubMed:8081723, ECO:0000305|PubMed:10414301,
ECO:0000305|PubMed:15858231};
-!- SUBUNIT: Homotetramer or heterotetramer with KCNB2
(PubMed:8081723, PubMed:1283219). Heterotetramer with non-
conducting channel-forming alpha subunits such as KCNF1, KCNG1,
KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1
(PubMed:10484328, PubMed:11852086, PubMed:12060745,
PubMed:19357235, PubMed:19074135, PubMed:19717558,
PubMed:24901643). Channel activity is regulated by association
with ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and
KCNE3 (By similarity). Self-associates (via N-terminus and C-
terminus) (PubMed:12560340, PubMed:24901643); self-association is
required to regulate trafficking, gating and C-terminal
phosphorylation-dependent modulation of the channel (By
similarity). Interacts (via C-terminus) with STX1A (via C-
terminus); this decreases the rate of channel activation and
increases the rate of channel inactivation in pancreatic beta
cells, induces also neuronal apoptosis in response to oxidative
injury as well as pore-independent enhancement of exocytosis in
neuroendocrine cells, chromaffin cells, pancreatic beta cells and
from the soma of dorsal root ganglia (DRG) neurons. Interacts (via
N-terminus) with SNAP25; this decreases the rate of channel
inactivation in pancreatic beta cells and also increases
interaction during neuronal apoptosis in a N-methyl-D-aspartate
receptor (NMDAR)-dependent manner. Interacts (via N-terminus and
C-terminus) with VAMP2 (via N-terminus); stimulates channel
inactivation rate. Interacts with CREB1; this promotes channel
acetylation in response to stimulation of incretin hormones.
Interacts (via N-terminus and C-terminus) with MYL12B. Interacts
(via N-terminus) with PIAS3; this increases the number of
functional channels at the cell surface (By similarity). Interacts
with SUMO1 (PubMed:19223394). Interacts (via phosphorylated form)
with PTPRE; this reduces phosphorylation and channel activity in
heterologous cells (By similarity). {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q03717, ECO:0000269|PubMed:10484328,
ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:12060745,
ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:1283219,
ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:19223394,
ECO:0000269|PubMed:19357235, ECO:0000269|PubMed:19717558,
ECO:0000269|PubMed:24901643, ECO:0000269|PubMed:8081723}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10484328,
ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:12060745,
ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:1283219,
ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:19223394,
ECO:0000269|PubMed:19717558, ECO:0000269|PubMed:24477962,
ECO:0000269|PubMed:24901643, ECO:0000269|PubMed:26503721,
ECO:0000269|PubMed:8081723}. Perikaryon
{ECO:0000269|PubMed:24477962}. Cell projection, axon
{ECO:0000269|PubMed:24477962}. Cell projection, dendrite
{ECO:0000269|PubMed:24477962}. Membrane; Multi-pass membrane
protein. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:P15387}. Cell junction, synapse
{ECO:0000250|UniProtKB:P15387}. Cell junction, synapse,
synaptosome {ECO:0000250|UniProtKB:P15387}. Lateral cell membrane
{ECO:0000250|UniProtKB:P15387}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P15387}. Note=Localizes to high-density
somatodendritic clusters and non-clustered sites on the surface of
neocortical and hippocampal pyramidal neurons in a cortical actin
cytoskeleton-dependent manner (PubMed:24477962). Localizes also to
high-density clusters in the axon initial segment (AIS), at
ankyrin-G-deficient sites, on the surface of neocortical and
hippocampal pyramidal neurons (PubMed:24477962). KCNB1-containing
AIS clusters localize either in close apposition to smooth
endoplasmic reticulum cisternal organelles or with GABA-A
receptor-containing synapses of hippocampal and cortical pyramidal
neurons, respectively (PubMed:24477962). Localizes to high-density
clusters on the cell surface of atrial and ventricular myocytes
and at the lateral plasma membrane in epithelial cells. Localizes
both to the axial and transverse tubules (T tubule) and sarcolemma
in ventricular myocytes. Associated with lipid raft domains. In
cortical neurons, apoptotic injuries induce de novo plasma
membrane insertion in a SNARE-dependent manner causing an
apoptotic potassium current surge. {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q03717, ECO:0000269|PubMed:12060745,
ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:24477962,
ECO:0000269|PubMed:24901643}.
-!- TISSUE SPECIFICITY: Expressed in neocortical pyramidal cells
(PubMed:24477962). Expressed in pancreatic beta cells (at protein
level) (PubMed:12403834, PubMed:14988243). Expressed in brain,
heart, lung, liver, colon, kidney and adrenal gland
(PubMed:19074135). Expressed in the cortex, amygdala, cerebellum,
pons, thalamus, hypothalamus, hippocampus and substantia nigra
(PubMed:19074135). {ECO:0000269|PubMed:12403834,
ECO:0000269|PubMed:14988243, ECO:0000269|PubMed:19074135,
ECO:0000269|PubMed:24477962}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The N-terminal and C-terminal cytoplasmic regions mediate
homooligomerization; self-association is required to regulate
trafficking, gating and C-terminal phosphorylation-dependent
modulation of the channel (PubMed:11852086, PubMed:12060745,
PubMed:12560340, PubMed:19074135, PubMed:24901643). The N-terminal
cytoplasmic region is important for interaction with other
channel-forming alpha subunits and with ancillary beta subunits
(PubMed:24901643). The C-terminus is necessary and sufficient for
the restricted localization to, and clustering within, both in
soma and proximal portions of dendrite of neurons and in lateral
membrane of non-neuronal polarized cells. The C-terminus is both
necessary and sufficient as a mediator of cholinergic and calcium-
stimulated modulation of channel cell membrane clustering
localization and activity in hippocampal neurons (By similarity).
{ECO:0000250|UniProtKB:P15387, ECO:0000269|PubMed:11852086,
ECO:0000269|PubMed:12060745, ECO:0000269|PubMed:12560340,
ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:24901643}.
-!- PTM: Phosphorylated. Differential C-terminal phosphorylation on a
subset of serines allows graded activity-dependent regulation of
channel gating in hippocampal neurons. Ser-607 and Tyr-128 are
significant sites of voltage-gated regulation through
phosphorylation/dephosphorylation activities. Tyr-128 can be
phosphorylated by Src and dephosphorylated by cytoplasmic form of
the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation
increases in response to acute blockade of neuronal activity.
Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK;
phosphorylations are necessary and sufficient for an increase in
plasma membrane insertion, apoptotic potassium current surge and
completion of the neuronal cell death program. Phosphorylated on
Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is
necessary for KCNB1 channel clustering formation. The Ser-607
phosphorylation state differs between KCNB1-containing clusters on
the proximal and distal portions of the axon initial segment
(AIS). Highly phosphorylated on serine residues in the C-terminal
cytoplasmic tail in resting neurons. Phosphorylated in pancreatic
beta cells in response to incretin hormones stimulation in a
PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta
cell survival. Phosphorylation on Ser-567 is reduced during
postnatal development with low levels at P2 and P5; levels then
increase to reach adult levels by P14. Phosphorylation on Ser-457,
Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-
terminal Ser-15 are sensitive to calcineurin-mediated
dephosphorylation contributing to the modulation of the voltage-
dependent gating properties. Dephosphorylation by phosphatase
PTPRE confers neuroprotection by its inhibitory influence on the
neuronal apoptotic potassium current surge in a Zn(2+)-dependent
manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA.
Hypoxia-, seizure- or glutamate-induced neuronal activity promote
calcium/calcineurin-dependent dephosphorylation resulting in a
loss of KCNB1-containing clustering and enhanced channel activity.
In response to brain ischemia, Ser-567 and Ser-607 are strongly
dephosphorylated while Ser-457 and Ser-720 are less
dephosphorylated. In response to brain seizures, phosphorylation
levels on Ser-567 and Ser-607 are greatly reduced.
Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein
kinases and tyrosine phosphatase PTPRE in primary Schwann cells
and sciatic nerve tissue (By similarity).
{ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717}.
-!- PTM: Acetylated. Acetylation occurs in pancreatic beta cells in
response to stimulation by incretin hormones in a histone
acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent
signaling pathway, promoting beta cell survival.
{ECO:0000250|UniProtKB:P15387}.
-!- PTM: Sumoylated on Lys-474, preferentially with SUMO1; sumoylation
induces a positive shift in the voltage-dependence of activation
and inhibits channel activity (PubMed:19223394). Sumoylation
increases the frequency of repetitive action potential firing at
the cell surface of hippocampal neurons and decreases its
frequency in pancreatic beta cells (PubMed:19223394). Desumoylated
by SENP1 (PubMed:19223394). {ECO:0000269|PubMed:19223394}.
-!- DISEASE: Epileptic encephalopathy, early infantile, 26 (EIEE26)
[MIM:616056]: A form of epileptic encephalopathy, a heterogeneous
group of severe childhood onset epilepsies characterized by
refractory seizures, neurodevelopmental impairment, and poor
prognosis. Development is normal prior to seizure onset, after
which cognitive and motor delays become apparent. EIEE26 patients
manifest multiple types of seizures, delayed psychomotor
development, poor or absent speech, hypotonia, hypsarrhythmia.
{ECO:0000269|PubMed:25164438, ECO:0000269|PubMed:26477325,
ECO:0000269|PubMed:26503721}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA36156.1; Type=Erroneous initiation; Evidence={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; X68302; CAA48374.1; -; Genomic_DNA.
EMBL; L02840; AAA36156.1; ALT_INIT; mRNA.
EMBL; AF026005; AAB88808.1; -; mRNA.
EMBL; AL035685; -; NOT_ANNOTATED_CDS; Genomic_DNA.
CCDS; CCDS13418.1; -.
PIR; S31761; S31761.
RefSeq; NP_004966.1; NM_004975.3.
RefSeq; XP_006723847.1; XM_006723784.3.
RefSeq; XP_011527101.1; XM_011528799.2.
UniGene; Hs.633143; -.
UniGene; Hs.84244; -.
ProteinModelPortal; Q14721; -.
BioGrid; 109947; 17.
IntAct; Q14721; 1.
STRING; 9606.ENSP00000360806; -.
BindingDB; Q14721; -.
ChEMBL; CHEMBL2363000; -.
DrugBank; DB06637; Dalfampridine.
GuidetoPHARMACOLOGY; 546; -.
TCDB; 1.A.1.2.11; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q14721; -.
PhosphoSitePlus; Q14721; -.
BioMuta; KCNB1; -.
DMDM; 24418854; -.
OGP; Q14721; -.
MaxQB; Q14721; -.
PaxDb; Q14721; -.
PeptideAtlas; Q14721; -.
PRIDE; Q14721; -.
ProteomicsDB; 60144; -.
DNASU; 3745; -.
Ensembl; ENST00000371741; ENSP00000360806; ENSG00000158445.
Ensembl; ENST00000635465; ENSP00000489193; ENSG00000158445.
GeneID; 3745; -.
KEGG; hsa:3745; -.
UCSC; uc002xur.2; human.
CTD; 3745; -.
DisGeNET; 3745; -.
EuPathDB; HostDB:ENSG00000158445.8; -.
GeneCards; KCNB1; -.
HGNC; HGNC:6231; KCNB1.
HPA; CAB001979; -.
HPA; HPA042434; -.
MalaCards; KCNB1; -.
MIM; 600397; gene.
MIM; 616056; phenotype.
neXtProt; NX_Q14721; -.
OpenTargets; ENSG00000158445; -.
Orphanet; 1934; Early infantile epileptic encephalopathy.
PharmGKB; PA209; -.
eggNOG; KOG3713; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118981; -.
HOGENOM; HOG000113206; -.
HOVERGEN; HBG052225; -.
InParanoid; Q14721; -.
KO; K04885; -.
OMA; HLSPNKW; -.
OrthoDB; EOG091G0FP3; -.
PhylomeDB; Q14721; -.
TreeFam; TF313103; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
SIGNOR; Q14721; -.
ChiTaRS; KCNB1; human.
GeneWiki; KCNB1; -.
GenomeRNAi; 3745; -.
PRO; PR:Q14721; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000158445; -.
CleanEx; HS_KCNB1; -.
ExpressionAtlas; Q14721; baseline and differential.
Genevisible; Q14721; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0001508; P:action potential; IDA:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
GO; GO:1900454; P:positive regulation of long term synaptic depression; ISS:UniProtKB.
GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:2000671; P:regulation of motor neuron apoptotic process; ISS:UniProtKB.
GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS: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; IPR003973; K_chnl_volt-dep_Kv2.
InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
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.
Pfam; PF03521; Kv2channel; 2.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01514; KV21CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01495; SHABCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Disease mutation; Epilepsy; Exocytosis; Ion channel; Ion transport;
Isopeptide bond; Membrane; Phosphoprotein; Polymorphism;
Postsynaptic cell membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Synapse; Synaptosome;
Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
Voltage-gated channel.
CHAIN 1 858 Potassium voltage-gated channel subfamily
B member 1.
/FTId=PRO_0000054042.
TOPO_DOM 1 186 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 187 208 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 209 228 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 229 250 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 251 259 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 260 280 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 281 294 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 295 316 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 317 330 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 331 351 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 352 364 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 365 376 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 377 384 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 385 391 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 392 420 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 421 858 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 59 75 Self-association.
{ECO:0000250|UniProtKB:P15387}.
REGION 448 481 Self-association.
{ECO:0000250|UniProtKB:P15387}.
MOTIF 377 382 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
COMPBIAS 517 520 Poly-Ser.
COMPBIAS 701 706 Poly-Ala.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 128 128 Phosphotyrosine; by Src.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q03717}.
MOD_RES 457 457 Phosphoserine.
{ECO:0000250|UniProtKB:Q03717}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 520 520 Phosphoserine; by CDK5; in vitro.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 607 607 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 656 656 Phosphoserine; by CDK5; in vitro.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 800 800 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 805 805 Phosphoserine; by CDK5, MAPK14; in vitro.
{ECO:0000250|UniProtKB:P15387}.
CROSSLNK 474 474 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P15387}.
VARIANT 306 306 R -> C (in EIEE26; reduces sensitivity
and cooperativity of the voltage sensor
for channel opening and greatly
suppresses repetitive firing in cultured
cortical neurons).
{ECO:0000269|PubMed:26477325}.
/FTId=VAR_075573.
VARIANT 347 347 S -> R (in EIEE26; inhibits ion
selectivity and gain of a depolarizing
inward cation conductance; trafficks
normally to the cell surface;
dbSNP:rs587777848).
{ECO:0000269|PubMed:25164438}.
/FTId=VAR_071991.
VARIANT 374 374 T -> I (in EIEE26; inhibits ion
selectivity and gain of a depolarizing
inward cation conductance; trafficks
normally to the cell surface;
dbSNP:rs587777849).
{ECO:0000269|PubMed:25164438}.
/FTId=VAR_071992.
VARIANT 378 378 V -> A (in EIEE26; change in the ion
selectivity from potassium-selective to
nonselective cation channels and
significant decrease in cell membrane
localization).
{ECO:0000269|PubMed:26503721}.
/FTId=VAR_075574.
VARIANT 379 379 G -> R (in EIEE26; inhibits ion
selectivity and gain of a depolarizing
inward cation conductance; trafficks
normally to the cell surface;
dbSNP:rs587777850).
{ECO:0000269|PubMed:25164438}.
/FTId=VAR_071993.
VARIANT 401 401 G -> R (in EIEE26; dominant-negative
mutation resulting in loss of endogenous
channel currents and greatly suppresses
repetitive firing in cultured cortical
neurons). {ECO:0000269|PubMed:26477325}.
/FTId=VAR_075575.
VARIANT 616 616 T -> N (in dbSNP:rs2229006).
/FTId=VAR_062182.
VARIANT 616 616 T -> S (in dbSNP:rs2229006).
/FTId=VAR_062183.
VARIANT 825 825 P -> S (in dbSNP:rs34467662).
/FTId=VAR_034049.
VARIANT 857 857 S -> N (in dbSNP:rs34280195).
/FTId=VAR_062184.
MUTAGEN 71 71 E->Q: No effect on channel activity.
{ECO:0000269|PubMed:12560340}.
MUTAGEN 74 74 D->R: Reduces interaction with KCNG1 and
self-interaction and impairs plasma
membrane subcellular localization,
homotetramerization and
hetetrotetramerization with KCNG4; when
associated with R-75.
{ECO:0000269|PubMed:19717558,
ECO:0000269|PubMed:24901643}.
MUTAGEN 75 75 D->R: Reduces interaction with KCNG1 and
self-interaction and impairs plasma
membrane subcellular localization,
homotetramerization and
hetetrotetramerization with KCNG4; when
associated with R-74.
{ECO:0000269|PubMed:19717558,
ECO:0000269|PubMed:24901643}.
MUTAGEN 79 79 D->E: Increases channel activity.
{ECO:0000269|PubMed:12560340}.
MUTAGEN 105 105 H->V,R: Reduces channel activity.
Inhibits interaction with KCNG4. Impairs
hetetrotetramerization with KCNG1, KCNG3
or KCNG4. Does not impair
homotetramerization.
{ECO:0000269|PubMed:19074135}.
SEQUENCE 858 AA; 95878 MW; C4B426174ED0DEE4 CRC64;
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
RDCNTHDSLL EVCDDYSLDD NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD
YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE
KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQSTDNPQLA HVEAVCIAWF
TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK
FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY
KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFARSIEM MDIVVEKNGE NMGKKDKVQD
NHLSPNKWKW TKRTLSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ
SQPILNTKES AAQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
ATRFSHSPLT SLPSKTGGST APEVGWRGAL GASGGRFVEA NPSPDASQHS SFFIESPKSS
MKTNNPLKLR ALKVNFMEGD PSPLLPVLGM YHDPLRNRGS AAAAVAGLEC ATLLDKAVLS
PESSIYTTAS AKTPPRSPEK HTAIAFNFEA GVHQYIDADT DDEGQLLYSV DSSPPKSLPG
STSPKFSTGT RSEKNHFESS PLPTSPKFLR QNCIYSTEAL TGKGPSGQEK CKLENHISPD
VRVLPGGGAH GSTRDQSI


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