KCNB1_RAT
ID KCNB1_RAT Reviewed; 857 AA.
AC P15387;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2002, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 1 {ECO:0000250|UniProtKB:Q14721};
DE AltName: Full=Delayed rectifier potassium channel 1 {ECO:0000303|PubMed:2770868};
DE Short=DRK1 {ECO:0000303|PubMed:2770868};
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.1;
GN Name=Kcnb1 {ECO:0000312|RGD:2954};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-857, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RC TISSUE=Brain;
RX PubMed=2770868; DOI=10.1038/340642a0;
RA Frech G.C., Vandongen A.M.J., Schuster G., Brown A.M., Joho R.H.;
RT "A novel potassium channel with delayed rectifier properties isolated from
RT rat brain by expression cloning.";
RL Nature 340:642-645(1989).
RN [2]
RP SEQUENCE REVISION.
RA Frech G.C.;
RL Submitted (FEB-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-575, AND TISSUE SPECIFICITY.
RX PubMed=1740690; DOI=10.1523/jneurosci.12-02-00538.1992;
RA Drewe J.A., Verma S., Frech G.C., Joho R.H.;
RT "Distinct spatial and temporal expression patterns of K+ channel mRNAs from
RT different subfamilies.";
RL J. Neurosci. 12:538-548(1992).
RN [4]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2206531; DOI=10.1016/0896-6273(90)90082-q;
RA VanDongen A.M., Frech G.C., Drewe J.A., Joho R.H., Brown A.M.;
RT "Alteration and restoration of K+ channel function by deletions at the
RT N- and C-termini.";
RL Neuron 5:433-443(1990).
RN [5]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=1875913;
RA Taglialatela M., Vandongen A.M., Drewe J.A., Joho R.H., Brown A.M.,
RA Kirsch G.E.;
RT "Patterns of internal and external tetraethylammonium block in four
RT homologous K+ channels.";
RL Mol. Pharmacol. 40:299-307(1991).
RN [6]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=1961744; DOI=10.1073/pnas.88.23.10764;
RA Trimmer J.S.;
RT "Immunological identification and characterization of a delayed rectifier
RT K+ channel polypeptide in rat brain.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:10764-10768(1991).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8508921; DOI=10.1016/0014-5793(93)81394-f;
RA Trimmer J.S.;
RT "Expression of Kv2.1 delayed rectifier K+ channel isoforms in the
RT developing rat brain.";
RL FEBS Lett. 324:205-210(1993).
RN [8]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8463836; DOI=10.1523/jneurosci.13-04-01569.1993;
RA Hwang P.M., Fotuhi M., Bredt D.S., Cunningham A.M., Snyder S.H.;
RT "Contrasting immunohistochemical localizations in rat brain of two novel K+
RT channels of the Shab subfamily.";
RL J. Neurosci. 13:1569-1576(1993).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, ACTIVITY
RP REGULATION, SUBCELLULAR LOCATION, AND LACK OF GLYCOSYLATION.
RX PubMed=8083226; DOI=10.1016/s0021-9258(17)31640-x;
RA Shi G., Kleinklaus A.K., Marrion N.V., Trimmer J.S.;
RT "Properties of Kv2.1 K+ channels expressed in transfected mammalian
RT cells.";
RL J. Biol. Chem. 269:23204-23211(1994).
RN [10]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND LACK OF INTERACTION WITH
RP KCNAB1 AND KCNAB2.
RX PubMed=7623158; DOI=10.1523/jneurosci.15-07-05360.1995;
RA Rhodes K.J., Keilbaugh S.A., Barrezueta N.X., Lopez K.L., Trimmer J.S.;
RT "Association and colocalization of K+ channel alpha- and beta-subunit
RT polypeptides in rat brain.";
RL J. Neurosci. 15:5360-5371(1995).
RN [11]
RP ACTIVITY REGULATION.
RX PubMed=7576642; DOI=10.1016/0896-6273(95)90184-1;
RA Swartz K.J., MacKinnon R.;
RT "An inhibitor of the Kv2.1 potassium channel isolated from the venom of a
RT Chilean tarantula.";
RL Neuron 15:941-949(1995).
RN [12]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8978827; DOI=10.1083/jcb.135.6.1619;
RA Scannevin R.H., Murakoshi H., Rhodes K.J., Trimmer J.S.;
RT "Identification of a cytoplasmic domain important in the polarized
RT expression and clustering of the Kv2.1 K+ channel.";
RL J. Cell Biol. 135:1619-1632(1996).
RN [13]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNV1, AND SUBCELLULAR LOCATION.
RX PubMed=8670833; DOI=10.1002/j.1460-2075.1996.tb00697.x;
RA Hugnot J.-P., Salinas M., Lesage F., Guillemare E., de Weille J.,
RA Heurteaux C., Mattei M.-G., Lazdunski M.;
RT "Kv8.1, a new neuronal potassium channel subunit with specific inhibitory
RT properties towards Shab and Shaw channels.";
RL EMBO J. 15:3322-3331(1996).
RN [14]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNG1, AND SUBCELLULAR LOCATION.
RX PubMed=8980147; DOI=10.1016/s0014-5793(96)01316-6;
RA Post M.A., Kirsch G.E., Brown A.M.;
RT "Kv2.1 and electrically silent Kv6.1 potassium channel subunits combine and
RT express a novel current.";
RL FEBS Lett. 399:177-182(1996).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNS3, SUBCELLULAR LOCATION, ACTIVITY
RP REGULATION, AND TISSUE SPECIFICITY.
RX PubMed=9362476; DOI=10.1093/emboj/16.22.6615;
RA Patel A.J., Lazdunski M., Honore E.;
RT "Kv2.1/Kv9.3, a novel ATP-dependent delayed-rectifier K+ channel in oxygen-
RT sensitive pulmonary artery myocytes.";
RL EMBO J. 16:6615-6625(1997).
RN [16]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9079713; DOI=10.1074/jbc.272.13.8774;
RA Salinas M., de Weille J., Guillemare E., Lazdunski M., Hugnot J.-P.;
RT "Modes of regulation of shab K+ channel activity by the Kv8.1 subunit.";
RL J. Biol. Chem. 272:8774-8780(1997).
RN [17]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=9305895; DOI=10.1074/jbc.272.39.24371;
RA Salinas M., Duprat F., Heurteaux C., Hugnot J.-P., Lazdunski M.;
RT "New modulatory alpha subunits for mammalian Shab K+ channels.";
RL J. Biol. Chem. 272:24371-24379(1997).
RN [18]
RP PHOSPHORYLATION, FUNCTION, AND MUTAGENESIS OF SER-444 AND SER-496.
RX PubMed=9351973; DOI=10.1124/mol.52.5.821;
RA Murakoshi H., Shi G., Scannevin R.H., Trimmer J.S.;
RT "Phosphorylation of the Kv2.1 K+ channel alters voltage-dependent
RT activation.";
RL Mol. Pharmacol. 52:821-828(1997).
RN [19]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNF1 AND KCNG1, AND SUBCELLULAR
RP LOCATION.
RX PubMed=9696692; DOI=10.1152/ajpcell.1998.274.6.c1501;
RA Kramer J.W., Post M.A., Brown A.M., Kirsch G.E.;
RT "Modulation of potassium channel gating by coexpression of Kv2.1 with
RT regulatory Kv5.1 or Kv6.1 alpha-subunits.";
RL Am. J. Physiol. 274:C1501-C1510(1998).
RN [20]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9616203; DOI=10.1172/jci333;
RA Archer S.L., Souil E., Dinh-Xuan A.T., Schremmer B., Mercier J.C.,
RA El Yaagoubi A., Nguyen-Huu L., Reeve H.L., Hampl V.;
RT "Molecular identification of the role of voltage-gated K+ channels, Kv1.5
RT and Kv2.1, in hypoxic pulmonary vasoconstriction and control of resting
RT membrane potential in rat pulmonary artery myocytes.";
RL J. Clin. Invest. 101:2319-2330(1998).
RN [21]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH PIAS3.
RX PubMed=9565597; DOI=10.1074/jbc.273.19.11745;
RA Wible B.A., Yang Q., Kuryshev Y.A., Accili E.A., Brown A.M.;
RT "Cloning and expression of a novel K+ channel regulatory protein, KChAP.";
RL J. Biol. Chem. 273:11745-11751(1998).
RN [22]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9522360; DOI=10.1016/s0306-4522(97)00519-8;
RA Du J., Tao-Cheng J.H., Zerfas P., McBain C.J.;
RT "The K+ channel, Kv2.1, is apposed to astrocytic processes and is
RT associated with inhibitory postsynaptic membranes in hippocampal and
RT cortical principal neurons and inhibitory interneurons.";
RL Neuroscience 84:37-48(1998).
RN [23]
RP REVIEW.
RX PubMed=10414301; DOI=10.1111/j.1749-6632.1999.tb11293.x;
RA Coetzee W.A., Amarillo Y., Chiu J., Chow A., Lau D., McCormack T.,
RA Moreno H., Nadal M.S., Ozaita A., Pountney D., Saganich M.,
RA Vega-Saenz de Miera E., Rudy B.;
RT "Molecular diversity of K+ channels.";
RL Ann. N. Y. Acad. Sci. 868:233-285(1999).
RN [24]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10024359; DOI=10.1523/jneurosci.19-05-01728.1999;
RA Murakoshi H., Trimmer J.S.;
RT "Identification of the Kv2.1 K+ channel as a major component of the delayed
RT rectifier K+ current in rat hippocampal neurons.";
RL J. Neurosci. 19:1728-1735(1999).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10414968; DOI=10.1523/jneurosci.19-15-06394.1999;
RA Baranauskas G., Tkatch T., Surmeier D.J.;
RT "Delayed rectifier currents in rat globus pallidus neurons are attributable
RT to Kv2.1 and Kv3.1/3.2 K(+) channels.";
RL J. Neurosci. 19:6394-6404(1999).
RN [26]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10618149; DOI=10.1111/j.1469-7793.2000.t01-2-00019.xm;
RA Du J., Haak L.L., Phillips-Tansey E., Russell J.T., McBain C.J.;
RT "Frequency-dependent regulation of rat hippocampal somato-dendritic
RT excitability by the K+ channel subunit Kv2.1.";
RL J. Physiol. (Lond.) 522:19-31(2000).
RN [27]
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF SER-587; SER-590; PHE-591
RP AND SER-593.
RX PubMed=10719893; DOI=10.1016/s0896-6273(00)80902-2;
RA Lim S.T., Antonucci D.E., Scannevin R.H., Trimmer J.S.;
RT "A novel targeting signal for proximal clustering of the Kv2.1 K+ channel
RT in hippocampal neurons.";
RL Neuron 25:385-397(2000).
RN [28]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=11463864; DOI=10.1210/mend.15.8.0685;
RA MacDonald P.E., Ha X.F., Wang J., Smukler S.R., Sun A.M., Gaisano H.Y.,
RA Salapatek A.M., Backx P.H., Wheeler M.B.;
RT "Members of the Kv1 and Kv2 voltage-dependent K(+) channel families
RT regulate insulin secretion.";
RL Mol. Endocrinol. 15:1423-1435(2001).
RN [29]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP TRP-369 AND TYR-384.
RX PubMed=12451110; DOI=10.1523/jneurosci.22-23-10094.2002;
RA Malin S.A., Nerbonne J.M.;
RT "Delayed rectifier K+ currents, IK, are encoded by Kv2 alpha-subunits and
RT regulate tonic firing in mammalian sympathetic neurons.";
RL J. Neurosci. 22:10094-10105(2002).
RN [30]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12127166; DOI=10.1016/s0024-3205(02)01922-7;
RA Lu Y., Hanna S.T., Tang G., Wang R.;
RT "Contributions of Kv1.2, Kv1.5 and Kv2.1 subunits to the native delayed
RT rectifier K(+) current in rat mesenteric artery smooth muscle cells.";
RL Life Sci. 71:1465-1473(2002).
RN [31]
RP FUNCTION, INTERACTION WITH SNAP25, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=12403834; DOI=10.1210/me.2002-0058;
RA MacDonald P.E., Wang G., Tsuk S., Dodo C., Kang Y., Tang L., Wheeler M.B.,
RA Cattral M.S., Lakey J.R., Salapatek A.M., Lotan I., Gaisano H.Y.;
RT "Synaptosome-associated protein of 25 kilodaltons modulates Kv2.1 voltage-
RT dependent K(+) channels in neuroendocrine islet beta-cells through an
RT interaction with the channel N terminus.";
RL Mol. Endocrinol. 16:2452-2461(2002).
RN [32]
RP ACTIVITY REGULATION.
RX PubMed=12065754; DOI=10.1124/mol.62.1.48;
RA Escoubas P., Diochot S., Celerier M.-L., Nakajima T., Lazdunski M.;
RT "Novel tarantula toxins for subtypes of voltage-dependent potassium
RT channels in the Kv2 and Kv4 subfamilies.";
RL Mol. Pharmacol. 62:48-57(2002).
RN [33]
RP FUNCTION, SELF-ASSOCIATION, DOMAIN, SUBCELLULAR LOCATION, AND MUTAGENESIS
RP OF GLN-71 AND GLU-79.
RX PubMed=12560340; DOI=10.1074/jbc.m212973200;
RA Ju M., Stevens L., Leadbitter E., Wray D.;
RT "The Roles of N- and C-terminal determinants in the activation of the Kv2.1
RT potassium channel.";
RL J. Biol. Chem. 278:12769-12778(2003).
RN [34]
RP PHOSPHORYLATION AT TYR-128, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TYR-128.
RX PubMed=12615930; DOI=10.1074/jbc.m212766200;
RA Tiran Z., Peretz A., Attali B., Elson A.;
RT "Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine
RT 124 by Src and by protein-tyrosine phosphatase epsilon.";
RL J. Biol. Chem. 278:17509-17514(2003).
RN [35]
RP FUNCTION, INTERACTION WITH STX1A, AND SUBCELLULAR LOCATION.
RX PubMed=12621036; DOI=10.1074/jbc.m213088200;
RA Leung Y.M., Kang Y., Gao X., Xia F., Xie H., Sheu L., Tsuk S., Lotan I.,
RA Tsushima R.G., Gaisano H.Y.;
RT "Syntaxin 1A binds to the cytoplasmic C terminus of Kv2.1 to regulate
RT channel gating and trafficking.";
RL J. Biol. Chem. 278:17532-17538(2003).
RN [36]
RP FUNCTION, INTERACTION WITH SNP25 AND STX1A, AND SUBCELLULAR LOCATION.
RX PubMed=12807875; DOI=10.1074/jbc.m304943200;
RA Michaelevski I., Chikvashvili D., Tsuk S., Singer-Lahat D., Kang Y.,
RA Linial M., Gaisano H.Y., Fili O., Lotan I.;
RT "Direct interaction of target SNAREs with the Kv2.1 channel. Modal
RT regulation of channel activation and inactivation gating.";
RL J. Biol. Chem. 278:34320-34330(2003).
RN [37]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP TRP-369 AND TYR-384.
RX PubMed=12832499; DOI=10.1523/jneurosci.23-12-04798.2003;
RA Pal S., Hartnett K.A., Nerbonne J.M., Levitan E.S., Aizenman E.;
RT "Mediation of neuronal apoptosis by Kv2.1-encoded potassium channels.";
RL J. Neurosci. 23:4798-4802(2003).
RN [38]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNE3, SUBCELLULAR LOCATION, DOMAIN,
RP AND TISSUE SPECIFICITY.
RX PubMed=12954870; DOI=10.1523/jneurosci.23-22-08077.2003;
RA McCrossan Z.A., Lewis A., Panaghie G., Jordan P.N., Christini D.J.,
RA Lerner D.J., Abbott G.W.;
RT "MinK-related peptide 2 modulates Kv2.1 and Kv3.1 potassium channels in
RT mammalian brain.";
RL J. Neurosci. 23:8077-8091(2003).
RN [39]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=15322114; DOI=10.1074/jbc.m408789200;
RA Amberg G.C., Rossow C.F., Navedo M.F., Santana L.F.;
RT "NFATc3 regulates Kv2.1 expression in arterial smooth muscle.";
RL J. Biol. Chem. 279:47326-47334(2004).
RN [40]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, AND SUBCELLULAR LOCATION.
RX PubMed=15195093; DOI=10.1038/nn1260;
RA Misonou H., Mohapatra D.P., Park E.W., Leung V., Zhen D., Misonou K.,
RA Anderson A.E., Trimmer J.S.;
RT "Regulation of ion channel localization and phosphorylation by neuronal
RT activity.";
RL Nat. Neurosci. 7:711-718(2004).
RN [41]
RP REVIEW.
RX PubMed=15858231; DOI=10.1385/cbb:42:2:167;
RA Cox R.H.;
RT "Molecular determinants of voltage-gated potassium currents in vascular
RT smooth muscle.";
RL Cell Biochem. Biophys. 42:167-195(2005).
RN [42]
RP SUBCELLULAR LOCATION.
RX PubMed=15855232; DOI=10.1242/jcs.02348;
RA O'Connell K.M., Tamkun M.M.;
RT "Targeting of voltage-gated potassium channel isoforms to distinct cell
RT surface microdomains.";
RL J. Cell Sci. 118:2155-2166(2005).
RN [43]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RX PubMed=16319318; DOI=10.1523/jneurosci.3370-05.2005;
RA Misonou H., Mohapatra D.P., Menegola M., Trimmer J.S.;
RT "Calcium- and metabolic state-dependent modulation of the voltage-dependent
RT Kv2.1 channel regulates neuronal excitability in response to ischemia.";
RL J. Neurosci. 25:11184-11193(2005).
RN [44]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16273079; DOI=10.1038/sj.cdd.4401792;
RA Pal S.K., Takimoto K., Aizenman E., Levitan E.S.;
RT "Apoptotic surface delivery of K+ channels.";
RL Cell Death Differ. 13:661-667(2006).
RN [45]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, DOMAIN, AND SUBCELLULAR
RP LOCATION.
RX PubMed=16407566; DOI=10.1523/jneurosci.4620-05.2006;
RA Mohapatra D.P., Trimmer J.S.;
RT "The Kv2.1 C terminus can autonomously transfer Kv2.1-like phosphorylation-
RT dependent localization, voltage-dependent gating, and muscarinic modulation
RT to diverse Kv channels.";
RL J. Neurosci. 26:685-695(2006).
RN [46]
RP SUBCELLULAR LOCATION.
RX PubMed=16988031; DOI=10.1523/jneurosci.1825-06.2006;
RA O'Connell K.M., Rolig A.S., Whitesell J.D., Tamkun M.M.;
RT "Kv2.1 potassium channels are retained within dynamic cell surface
RT microdomains that are defined by a perimeter fence.";
RL J. Neurosci. 26:9609-9618(2006).
RN [47]
RP PHOSPHORYLATION AT SER-457; SER-567; SER-607 AND SER-719, SUBCELLULAR
RP LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND FUNCTION.
RX PubMed=17192433; DOI=10.1523/jneurosci.3970-06.2006;
RA Misonou H., Menegola M., Mohapatra D.P., Guy L.K., Park K.-S.,
RA Trimmer J.S.;
RT "Bidirectional activity-dependent regulation of neuronal ion channel
RT phosphorylation.";
RL J. Neurosci. 26:13505-13514(2006).
RN [48]
RP PHOSPHORYLATION AT SER-15; SER-457; SER-484; SER-496; SER-503; SER-520;
RP SER-541; SER-567; SER-590; SER-607; SER-655; SER-719; SER-771; SER-799;
RP SER-804 AND THR-836, FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP MUTAGENESIS OF SER-15; SER-457; SER-484; SER-541; SER-567; SER-607;
RP SER-655; SER-719; SER-771 AND SER-804.
RX PubMed=16917065; DOI=10.1126/science.1124254;
RA Park K.-S., Mohapatra D.P., Misonou H., Trimmer J.S.;
RT "Graded regulation of the Kv2.1 potassium channel by variable
RT phosphorylation.";
RL Science 313:976-979(2006).
RN [49]
RP PHOSPHORYLATION AT SER-15; SER-457; SER-541; SER-607; SER-655; SER-719;
RP SER-799; SER-804 AND THR-836, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18690023; DOI=10.4161/chan.4388;
RA Park K.S., Mohapatra D.P., Trimmer J.S.;
RT "Proteomic analyses of K(v)2.1 channel phosphorylation sites determining
RT cell background specific differences in function.";
RL Channels 1:59-61(2007).
RN [50]
RP SUBCELLULAR LOCATION.
RX PubMed=17606996; DOI=10.1242/jcs.007351;
RA Tamkun M.M., O'connell K.M., Rolig A.S.;
RT "A cytoskeletal-based perimeter fence selectively corrals a sub-population
RT of cell surface Kv2.1 channels.";
RL J. Cell Sci. 120:2413-2423(2007).
RN [51]
RP FUNCTION, INTERACTION WITH STX1A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TRP-369 AND TYR-384.
RX PubMed=17301173; DOI=10.1523/jneurosci.4006-06.2007;
RA Singer-Lahat D., Sheinin A., Chikvashvili D., Tsuk S., Greitzer D.,
RA Friedrich R., Feinshreiber L., Ashery U., Benveniste M., Levitan E.S.,
RA Lotan I.;
RT "K+ channel facilitation of exocytosis by dynamic interaction with
RT syntaxin.";
RL J. Neurosci. 27:1651-1658(2007).
RN [52]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17379638; DOI=10.1113/jphysiol.2007.128454;
RA Guan D., Tkatch T., Surmeier D.J., Armstrong W.E., Foehring R.C.;
RT "Kv2 subunits underlie slowly inactivating potassium current in rat
RT neocortical pyramidal neurons.";
RL J. Physiol. (Lond.) 581:941-960(2007).
RN [53]
RP PHOSPHORYLATION AT SER-804, MUTAGENESIS OF TRP-369; TYR-384 AND SER-804,
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17360683; DOI=10.1073/pnas.0610159104;
RA Redman P.T., He K., Hartnett K.A., Jefferson B.S., Hu L., Rosenberg P.A.,
RA Levitan E.S., Aizenman E.;
RT "Apoptotic surge of potassium currents is mediated by p38 phosphorylation
RT of Kv2.1.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:3568-3573(2007).
RN [54]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17965280; DOI=10.1152/ajpheart.01038.2007;
RA O'Connell K.M., Whitesell J.D., Tamkun M.M.;
RT "Localization and mobility of the delayed-rectifer K+ channel Kv2.1 in
RT adult cardiomyocytes.";
RL Am. J. Physiol. 294:H229-H237(2008).
RN [55]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=19014551; DOI=10.1186/1471-2202-9-112;
RA Sarmiere P.D., Weigle C.M., Tamkun M.M.;
RT "The Kv2.1 K+ channel targets to the axon initial segment of hippocampal
RT and cortical neurons in culture and in situ.";
RL BMC Neurosci. 9:112-112(2008).
RN [56]
RP FUNCTION, SELF-ASSOCIATION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND
RP DOMAIN.
RX PubMed=18463252; DOI=10.1523/jneurosci.0186-08.2008;
RA Mohapatra D.P., Siino D.F., Trimmer J.S.;
RT "Interdomain cytoplasmic interactions govern the intracellular trafficking,
RT gating, and modulation of the Kv2.1 channel.";
RL J. Neurosci. 28:4982-4994(2008).
RN [57]
RP INTERACTION WITH VAMP2, AND SUBCELLULAR LOCATION.
RX PubMed=18542995; DOI=10.1007/s00424-008-0468-7;
RA Lvov A., Chikvashvili D., Michaelevski I., Lotan I.;
RT "VAMP2 interacts directly with the N terminus of Kv2.1 to enhance channel
RT inactivation.";
RL Pflugers Arch. 456:1121-1136(2008).
RN [58]
RP FUNCTION, INTERACTION WITH STX1A, AND SUBCELLULAR LOCATION.
RX PubMed=18167541; DOI=10.1371/journal.pone.0001381;
RA Singer-Lahat D., Chikvashvili D., Lotan I.;
RT "Direct interaction of endogenous Kv channels with syntaxin enhances
RT exocytosis by neuroendocrine cells.";
RL PLoS ONE 3:E1381-E1381(2008).
RN [59]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=19276663; DOI=10.4161/chan.3.1.7655;
RA Mohapatra D.P., Misonou H., Pan S.J., Held J.E., Surmeier D.J.,
RA Trimmer J.S.;
RT "Regulation of intrinsic excitability in hippocampal neurons by activity-
RT dependent modulation of the KV2.1 potassium channel.";
RL Channels 3:46-56(2009).
RN [60]
RP TISSUE SPECIFICITY.
RX PubMed=19074135; DOI=10.1074/jbc.m808786200;
RA Mederos y Schnitzler M., Rinne S., Skrobek L., Renigunta V.,
RA Schlichthorl G., Derst C., Gudermann T., Daut J., Preisig-Muller R.;
RT "Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1
RT disrupts heteromerization with Kv6.3 and Kv6.4.";
RL J. Biol. Chem. 284:4695-4704(2009).
RN [61]
RP INTERACTION WITH VAMP2, SELF-ASSOCIATION, DOMAIN, AND SUBCELLULAR LOCATION.
RX PubMed=19690160; DOI=10.1074/jbc.m109.028761;
RA Lvov A., Greitzer D., Berlin S., Chikvashvili D., Tsuk S., Lotan I.,
RA Michaelevski I.;
RT "Rearrangements in the relative orientation of cytoplasmic domains induced
RT by a membrane-anchored protein mediate modulations in Kv channel gating.";
RL J. Biol. Chem. 284:28276-28291(2009).
RN [62]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNE1 AND KCNE2, SUBCELLULAR LOCATION,
RP DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=19219384; DOI=10.1007/s00232-009-9154-8;
RA McCrossan Z.A., Roepke T.K., Lewis A., Panaghie G., Abbott G.W.;
RT "Regulation of the Kv2.1 potassium channel by MinK and MiRP1.";
RL J. Membr. Biol. 228:1-14(2009).
RN [63]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SNAP25; STX1A AND
RP VAMP2.
RX PubMed=19077057; DOI=10.1111/j.1471-4159.2008.05834.x;
RA Yao H., Zhou K., Yan D., Li M., Wang Y.;
RT "The Kv2.1 channels mediate neuronal apoptosis induced by excitotoxicity.";
RL J. Neurochem. 108:909-919(2009).
RN [64]
RP FUNCTION, PHOSPHORYLATION AT TYR-128, DEPHOSPHORYLATION, AND MUTAGENESIS OF
RP TYR-128 AND SER-804.
RX PubMed=19622611; DOI=10.1113/jphysiol.2009.176321;
RA Redman P.T., Hartnett K.A., Aras M.A., Levitan E.S., Aizenman E.;
RT "Regulation of apoptotic potassium currents by coordinated zinc-dependent
RT signalling.";
RL J. Physiol. (Lond.) 587:4393-4404(2009).
RN [65]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNB2, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF TRP-369 AND TYR-384, TISSUE SPECIFICITY, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=20202934; DOI=10.1074/jbc.m109.074260;
RA Kihira Y., Hermanstyne T.O., Misonou H.;
RT "Formation of heteromeric Kv2 channels in mammalian brain neurons.";
RL J. Biol. Chem. 285:15048-15055(2010).
RN [66]
RP FUNCTION, INTERACTION WITH STX1A, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP TRP-369 AND TYR-384.
RX PubMed=20484665; DOI=10.1242/jcs.063719;
RA Feinshreiber L., Singer-Lahat D., Friedrich R., Matti U., Sheinin A.,
RA Yizhar O., Nachman R., Chikvashvili D., Rettig J., Ashery U., Lotan I.;
RT "Non-conducting function of the Kv2.1 channel enables it to recruit
RT vesicles for release in neuroendocrine and nerve cells.";
RL J. Cell Sci. 123:1940-1947(2010).
RN [67]
RP PHOSPHORYLATION AT SER-520; SER-655; SER-607 AND SER-804, DEPHOSPHORYLATION
RP AT SER-607, AND SUBCELLULAR LOCATION.
RX PubMed=21712386; DOI=10.1074/jbc.m111.251942;
RA Cerda O., Trimmer J.S.;
RT "Activity-dependent phosphorylation of neuronal Kv2.1 potassium channels by
RT CDK5.";
RL J. Biol. Chem. 286:28738-28748(2011).
RN [68]
RP FUNCTION, SUMOYLATION AT LYS-474, DESUMOYLATION, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF LYS-149; LYS-259 AND LYS-474, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=21518833; DOI=10.1085/jgp.201110604;
RA Plant L.D., Dowdell E.J., Dementieva I.S., Marks J.D., Goldstein S.A.;
RT "SUMO modification of cell surface Kv2.1 potassium channels regulates the
RT activity of rat hippocampal neurons.";
RL J. Gen. Physiol. 137:441-454(2011).
RN [69]
RP PHOSPHORYLATION, ACETYLATION, AND INTERACTION WITH CREB1.
RX PubMed=21818121; DOI=10.1038/cdd.2011.102;
RA Kim S.J., Widenmaier S.B., Choi W.S., Nian C., Ao Z., Warnock G.,
RA McIntosh C.H.;
RT "Pancreatic beta-cell prosurvival effects of the incretin hormones involve
RT post-translational modification of Kv2.1 delayed rectifier channels.";
RL Cell Death Differ. 19:333-344(2012).
RN [70]
RP FUNCTION, INTERACTION WITH STX1A, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP AND MUTAGENESIS OF TRP-369 AND TYR-384.
RX PubMed=22411134; DOI=10.1007/s00125-012-2512-6;
RA Dai X.Q., Manning Fox J.E., Chikvashvili D., Casimir M., Plummer G.,
RA Hajmrle C., Spigelman A.F., Kin T., Singer-Lahat D., Kang Y., Shapiro A.M.,
RA Gaisano H.Y., Lotan I., Macdonald P.E.;
RT "The voltage-dependent potassium channel subunit Kv2.1 regulates insulin
RT secretion from rodent and human islets independently of its electrical
RT function.";
RL Diabetologia 55:1709-1720(2012).
RN [71]
RP SUBCELLULAR LOCATION.
RX PubMed=22648171; DOI=10.1091/mbc.e12-01-0047;
RA Deutsch E., Weigel A.V., Akin E.J., Fox P., Hansen G., Haberkorn C.J.,
RA Loftus R., Krapf D., Tamkun M.M.;
RT "Kv2.1 cell surface clusters are insertion platforms for ion channel
RT delivery to the plasma membrane.";
RL Mol. Biol. Cell 23:2917-2929(2012).
RN [72]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-484; SER-519; SER-520 AND
RP SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [73]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=23878373; DOI=10.1113/jphysiol.2013.257253;
RA Guan D., Armstrong W.E., Foehring R.C.;
RT "Kv2 channels regulate firing rate in pyramidal neurons from rat
RT sensorimotor cortex.";
RL J. Physiol. (Lond.) 591:4807-4825(2013).
RN [74]
RP INTERACTION WITH MYL12B, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-590.
RX PubMed=24569993; DOI=10.1074/jbc.m113.534495;
RA Jensen C.S., Watanabe S., Rasmussen H.B., Schmitt N., Olesen S.P.,
RA Frost N.A., Blanpied T.A., Misonou H.;
RT "Specific sorting and post-Golgi trafficking of dendritic potassium
RT channels in living neurons.";
RL J. Biol. Chem. 289:10566-10581(2014).
RN [75]
RP PHOSPHORYLATION AT SER-607, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=24477962; DOI=10.1002/cne.23551;
RA King A.N., Manning C.F., Trimmer J.S.;
RT "A unique ion channel clustering domain on the axon initial segment of
RT mammalian neurons.";
RL J. Comp. Neurol. 522:2594-2608(2014).
RN [76]
RP FUNCTION, INTERACTION WITH STX1A, AND SUBCELLULAR LOCATION.
RX PubMed=24928958; DOI=10.1113/jphysiol.2014.276964;
RA McCord M.C., Kullmann P.H., He K., Hartnett K.A., Horn J.P., Lotan I.,
RA Aizenman E.;
RT "Syntaxin-binding domain of Kv2.1 is essential for the expression of
RT apoptotic K+ currents.";
RL J. Physiol. (Lond.) 592:3511-3521(2014).
RN [77]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 272-304.
RX PubMed=18004376; DOI=10.1038/nature06265;
RA Long S.B., Tao X., Campbell E.B., MacKinnon R.;
RT "Atomic structure of a voltage-dependent K+ channel in a lipid membrane-
RT like environment.";
RL Nature 450:376-382(2007).
RN [78]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 272-304.
RX PubMed=20360102; DOI=10.1126/science.1185954;
RA Tao X., Lee A., Limapichat W., Dougherty D.A., MacKinnon R.;
RT "A gating charge transfer center in voltage sensors.";
RL Science 328:67-73(2010).
RN [79]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 272-304.
RX PubMed=23705070; DOI=10.7554/elife.00594;
RA Banerjee A., Lee A., Campbell E., Mackinnon R.;
RT "Structure of a pore-blocking toxin in complex with a eukaryotic voltage-
RT dependent K(+) channel.";
RL Elife 2:E00594-E00594(2013).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes, primarily in the brain, but
CC also in the pancreas and cardiovascular system. Contributes to the
CC regulation of the action potential (AP) repolarization, duration and
CC frequency of repetitive AP firing in neurons, muscle cells and
CC endocrine cells and plays a role in homeostatic attenuation of
CC electrical excitability throughout the brain (PubMed:10024359,
CC PubMed:10618149, PubMed:12451110, PubMed:17379638, PubMed:19276663,
CC PubMed:23878373). Also plays a role in the regulation of exocytosis
CC independently of its electrical function (PubMed:20484665). Forms
CC tetrameric potassium-selective channels through which potassium ions
CC pass in accordance with their electrochemical gradient. The channel
CC alternates between opened and closed conformations in response to the
CC voltage difference across the membrane. Homotetrameric channels mediate
CC a delayed-rectifier voltage-dependent outward potassium current that
CC display rapid activation and slow inactivation in response to membrane
CC depolarization (PubMed:2770868, PubMed:2206531, PubMed:1875913,
CC PubMed:8083226, PubMed:8978827, PubMed:9351973, PubMed:9565597,
CC PubMed:12560340). Can form functional homotetrameric and
CC heterotetrameric channels that contain variable proportions of KCNB2;
CC channel properties depend on the type of alpha subunits that are part
CC of the channel (PubMed:20202934). Can also form functional
CC heterotetrameric channels with other alpha subunits that are non-
CC conducting when expressed alone, such as KCNF1, KCNG1, KCNG3, KCNG4,
CC KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a functionally
CC diverse range of channel complexes (PubMed:8670833, PubMed:8980147,
CC PubMed:9362476, PubMed:9079713, PubMed:9305895, PubMed:9696692).
CC Heterotetrameric channel activity formed with KCNS3 show increased
CC current amplitude with the threshold for action potential activation
CC shifted towards more negative values in hypoxic-treated pulmonary
CC artery smooth muscle cells (PubMed:9362476). Channel properties are
CC also modulated by cytoplasmic ancillary beta subunits such as AMIGO1,
CC KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate of the
CC delayed rectifier potassium channels (PubMed:12954870,
CC PubMed:19219384). In vivo, membranes probably contain a mixture of
CC heteromeric potassium channel complexes, making it difficult to assign
CC currents observed in intact tissues to any particular potassium channel
CC family member. Major contributor to the slowly inactivating delayed-
CC rectifier voltage-gated potassium current in neurons of the central
CC nervous system, sympathetic ganglion neurons, neuroendocrine cells,
CC pancreatic beta cells, cardiomyocytes and smooth muscle cells
CC (PubMed:9362476, PubMed:9616203, PubMed:10024359, PubMed:10414968,
CC PubMed:10618149, PubMed:11463864, PubMed:12451110, PubMed:12127166,
CC PubMed:12403834, PubMed:12621036, PubMed:12807875, PubMed:12832499,
CC PubMed:12954870, PubMed:15322114, PubMed:15195093, PubMed:16407566,
CC PubMed:17301173, PubMed:17379638, PubMed:18463252, PubMed:18167541,
CC PubMed:19276663, PubMed:20484665, PubMed:21518833, PubMed:22411134,
CC PubMed:23878373). Mediates the major part of the somatodendritic
CC delayed-rectifier potassium current in hippocampal and cortical
CC pyramidal neurons and sympathetic superior cervical ganglion (CGC)
CC neurons that acts to slow down periods of firing, especially during
CC high frequency stimulation (PubMed:10618149, PubMed:12451110,
CC PubMed:16319318, PubMed:17379638, PubMed:19276663, PubMed:23878373,
CC PubMed:16917065). Plays a role in the induction of long-term
CC potentiation (LTP) of neuron excitability in the CA3 layer of the
CC hippocampus (By similarity). Contributes to the regulation of glucose-
CC induced action potential amplitude and duration in pancreatic beta
CC cells, hence limiting calcium influx and insulin secretion
CC (PubMed:11463864). Plays a role in the regulation of resting membrane
CC potential and contraction in hypoxia-treated pulmonary artery smooth
CC muscle cells (PubMed:9616203). May contribute to the regulation of the
CC duration of both the action potential of cardiomyocytes and the heart
CC ventricular repolarization QT interval (By similarity). Contributes to
CC the pronounced pro-apoptotic potassium current surge during neuronal
CC apoptotic cell death in response to oxidative injury (PubMed:12832499,
CC PubMed:16273079, PubMed:17360683, PubMed:19077057, PubMed:19622611,
CC PubMed:24928958). May confer neuroprotection in response to
CC hypoxia/ischemic insults by suppressing pyramidal neurons
CC hyperexcitability in hippocampal and cortical regions
CC (PubMed:16319318). Promotes trafficking of KCNG3, KCNH1 and KCNH2 to
CC the cell surface membrane, presumably by forming heterotetrameric
CC channels with these subunits (By similarity). Plays a role in the
CC calcium-dependent recruitment and release of fusion-competent vesicles
CC from the soma of neurons, neuroendocrine and glucose-induced pancreatic
CC beta cells by binding key components of the fusion machinery in a pore-
CC independent manner (PubMed:11463864, PubMed:17301173, PubMed:18167541,
CC PubMed:20484665, PubMed:22411134). {ECO:0000250|UniProtKB:Q03717,
CC ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10414968,
CC ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:11463864,
CC ECO:0000269|PubMed:12127166, ECO:0000269|PubMed:12403834,
CC ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12560340,
CC ECO:0000269|PubMed:12621036, ECO:0000269|PubMed:12807875,
CC ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15322114,
CC ECO:0000269|PubMed:16273079, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16917065,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17360683,
CC ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:1875913,
CC ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:19276663, ECO:0000269|PubMed:19622611,
CC ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665,
CC ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:2206531,
CC ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:23878373,
CC ECO:0000269|PubMed:24928958, ECO:0000269|PubMed:2770868,
CC ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:8670833,
CC ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:8980147,
CC ECO:0000269|PubMed:9079713, ECO:0000269|PubMed:9305895,
CC ECO:0000269|PubMed:9351973, ECO:0000269|PubMed:9362476,
CC ECO:0000269|PubMed:9565597, ECO:0000269|PubMed:9616203,
CC ECO:0000269|PubMed:9696692}.
CC -!- ACTIVITY REGULATION: Inhibited by 42 nM hanatoxin 1 (HaTx1), a spider
CC venom toxin of the tarantula G. spatulata (PubMed:7576642). Inhibited
CC by 100 nM stromatoxin 1 (ScTx1), a spider venom toxin of the tarantula
CC S. calceata (PubMed:12065754). Modestly sensitive to millimolar levels
CC of tetraethylammonium (TEA) and 4-aminopyridine (4-AP) (PubMed:2770868,
CC PubMed:1875913, PubMed:8083226, PubMed:9362476). Completely insensitive
CC to toxins such as dendrotoxin (DTX) and charybdotoxin (CTX)
CC (PubMed:9362476). {ECO:0000269|PubMed:12065754,
CC ECO:0000269|PubMed:1875913, ECO:0000269|PubMed:2770868,
CC ECO:0000269|PubMed:7576642, ECO:0000269|PubMed:8083226,
CC ECO:0000269|PubMed:9362476, ECO:0000305|PubMed:10414301,
CC ECO:0000305|PubMed:15858231}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Homotetrameric channels expressed in xenopus oocytes or in
CC mammalian non-neuronal cells display delayed-rectifier voltage-
CC dependent potassium currents which are activated during membrane
CC depolarization, i.e within a risetime of about 20 msec
CC (PubMed:2770868). After that, inactivate very slowly, i.e within more
CC than 5 sec (PubMed:2206531, PubMed:8083226). Their activation
CC requires low threshold potentials of about -20 to -30 mV, with a
CC midpoint activation at about 10 mV (PubMed:2770868, PubMed:2206531,
CC PubMed:8083226). For inactivation, the voltage at half-maximal
CC amplitude is about -20 mV (PubMed:2206531, PubMed:8083226). The time
CC constant for recovery after inactivation is about 1.6 sec. Channels
CC have an unitary conductance of about 8 pS (PubMed:10414301,
CC PubMed:15858231). The voltage-dependence of activation and
CC inactivation and other channel characteristics vary depending on the
CC experimental conditions, the expression system, the presence or
CC absence of ancillary subunits and post-translational modifications.
CC {ECO:0000269|PubMed:2206531, ECO:0000269|PubMed:2770868,
CC ECO:0000269|PubMed:8083226, ECO:0000305|PubMed:10414301,
CC ECO:0000305|PubMed:15858231};
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCNB2 (PubMed:20202934).
CC Heterotetramer with non-conducting channel-forming alpha subunits such
CC as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and
CC KCNV1 (PubMed:8670833, PubMed:8980147, PubMed:9362476, PubMed:9079713,
CC PubMed:9305895, PubMed:9696692). Channel activity is regulated by
CC association with ancillary beta subunits such as AMIGO1, KCNE1, KCNE2
CC and KCNE3 (PubMed:12954870, PubMed:19219384). Self-associates (via N-
CC terminus and C-terminus); self-association is required to regulate
CC trafficking, gating and C-terminal phosphorylation-dependent modulation
CC of the channel (PubMed:12560340, PubMed:18463252, PubMed:19690160).
CC Interacts (via C-terminus) with STX1A (via C-terminus); this decreases
CC the rate of channel activation and increases the rate of channel
CC inactivation in pancreatic beta cells, induces also neuronal apoptosis
CC in response to oxidative injury as well as pore-independent enhancement
CC of exocytosis in neuroendocrine cells, chromaffin cells, pancreatic
CC beta cells and from the soma of dorsal root ganglia (DRG) neurons
CC (PubMed:12621036, PubMed:12807875, PubMed:17301173, PubMed:18167541,
CC PubMed:19077057, PubMed:20484665, PubMed:22411134, PubMed:24928958).
CC Interacts (via N-terminus) with SNAP25; this decreases the rate of
CC channel inactivation in pancreatic beta cells and also increases
CC interaction during neuronal apoptosis in a N-methyl-D-aspartate
CC receptor (NMDAR)-dependent manner (PubMed:12403834, PubMed:12807875,
CC PubMed:19077057). Interacts (via N-terminus and C-terminus) with VAMP2
CC (via N-terminus); stimulates channel inactivation rate
CC (PubMed:18542995, PubMed:19690160, PubMed:19077057). Interacts with
CC CREB1; this promotes channel acetylation in response to stimulation by
CC incretin hormones (PubMed:21818121). Interacts (via N-terminus and C-
CC terminus) with MYL12B (PubMed:24569993). Interacts (via N-terminus)
CC with PIAS3; this increases the number of functional channels at the
CC cell surface (PubMed:9565597). Interacts with SUMO1. Interacts (via
CC phosphorylated form) with PTPRE; this reduces phosphorylation and
CC channel activity in heterologous cells (By similarity).
CC {ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721,
CC ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12560340,
CC ECO:0000269|PubMed:12621036, ECO:0000269|PubMed:12807875,
CC ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:17301173,
CC ECO:0000269|PubMed:18167541, ECO:0000269|PubMed:18463252,
CC ECO:0000269|PubMed:18542995, ECO:0000269|PubMed:19077057,
CC ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:19690160,
CC ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665,
CC ECO:0000269|PubMed:21818121, ECO:0000269|PubMed:22411134,
CC ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:24928958,
CC ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:8980147,
CC ECO:0000269|PubMed:9079713, ECO:0000269|PubMed:9305895,
CC ECO:0000269|PubMed:9362476, ECO:0000269|PubMed:9565597,
CC ECO:0000269|PubMed:9696692}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10024359,
CC ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10618149,
CC ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12127166,
CC ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12451110,
CC ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:12615930,
CC ECO:0000269|PubMed:12621036, ECO:0000269|PubMed:12807875,
CC ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15322114,
CC ECO:0000269|PubMed:15855232, ECO:0000269|PubMed:16273079,
CC ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566,
CC ECO:0000269|PubMed:16988031, ECO:0000269|PubMed:17192433,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17360683,
CC ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17606996,
CC ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:18542995,
CC ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057,
CC ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:19276663,
CC ECO:0000269|PubMed:19690160, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:21518833,
CC ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22411134,
CC ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:24928958,
CC ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8083226,
CC ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:8508921,
CC ECO:0000269|PubMed:8670833, ECO:0000269|PubMed:8978827,
CC ECO:0000269|PubMed:8980147, ECO:0000269|PubMed:9079713,
CC ECO:0000269|PubMed:9305895, ECO:0000269|PubMed:9362476,
CC ECO:0000269|PubMed:9522360, ECO:0000269|PubMed:9565597,
CC ECO:0000269|PubMed:9616203, ECO:0000269|PubMed:9696692}. Perikaryon
CC {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10618149,
CC ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16988031,
CC ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:17965280,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19014551,
CC ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:1961744,
CC ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:21518833,
CC ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22648171,
CC ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:7623158,
CC ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:8978827,
CC ECO:0000269|PubMed:9522360}. Cell projection, dendrite
CC {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10618149,
CC ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:17379638,
CC ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:18463252,
CC ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19077057,
CC ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:21518833,
CC ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:22648171,
CC ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:7623158,
CC ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:9522360}. Cell
CC projection, axon {ECO:0000269|PubMed:19014551,
CC ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:24477962}. Postsynaptic
CC cell membrane {ECO:0000269|PubMed:9522360}. Synapse
CC {ECO:0000269|PubMed:9522360}. Synapse, synaptosome
CC {ECO:0000269|PubMed:8508921}. Membrane {ECO:0000269|PubMed:8508921};
CC Multi-pass membrane protein. Lateral cell membrane
CC {ECO:0000269|PubMed:8978827}. Cell membrane, sarcolemma
CC {ECO:0000269|PubMed:17965280}. Note=Localizes to high-density
CC somatodendritic clusters and non-clustered sites on the surface of
CC neocortical and hippocampal pyramidal neurons in a cortical actin
CC cytoskeleton-dependent manner (PubMed:1961744, PubMed:8978827,
CC PubMed:9522360, PubMed:10024359, PubMed:10719893, PubMed:15195093,
CC PubMed:16319318, PubMed:16407566, PubMed:16988031, PubMed:17606996,
CC PubMed:17379638, PubMed:19014551, PubMed:18463252, PubMed:22648171,
CC PubMed:23878373, PubMed:24569993, PubMed:24477962). Localizes also to
CC high-density clusters in the axon initial segment (AIS), at ankyrin-G-
CC deficient sites, on the surface of neocortical and hippocampal
CC pyramidal neurons (PubMed:17379638, PubMed:19014551, PubMed:22648171,
CC PubMed:24477962). KCNB1-containing AIS clusters localize either in
CC close apposition to smooth endoplasmic reticulum cisternal organelles
CC or with GABA-A receptor-containing synapses of hippocampal and cortical
CC pyramidal neurons, respectively (PubMed:24477962). Localizes to high-
CC density clusters on the cell surface of atrial and ventricular myocytes
CC and at the lateral plasma membrane in epithelial cells (PubMed:8978827,
CC PubMed:17965280). Localizes both to the axial and transverse tubules (T
CC tubule) and sarcolemma in ventricular myocytes (PubMed:17965280).
CC Associated with lipid raft domains (PubMed:15855232). In cortical
CC neurons, apoptotic injuries induce de novo plasma membrane insertion in
CC a SNARE-dependent manner causing an apoptotic potassium current surge
CC (PubMed:16273079, PubMed:19077057). {ECO:0000250|UniProtKB:Q03717,
CC ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:10024359,
CC ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12615930,
CC ECO:0000269|PubMed:12807875, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:15855232,
CC ECO:0000269|PubMed:16273079, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16988031,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:17379638,
CC ECO:0000269|PubMed:17606996, ECO:0000269|PubMed:17965280,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19014551,
CC ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:1961744, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:22648171,
CC ECO:0000269|PubMed:23878373, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:24569993, ECO:0000269|PubMed:8508921,
CC ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:9522360}.
CC -!- TISSUE SPECIFICITY: Expressed in brain (PubMed:1740690, PubMed:1961744,
CC PubMed:8508921, PubMed:7623158, PubMed:12954870). Expressed in the
CC hippocampus, cerebral cortex, cerebellum, thalamus, hypothalamus,
CC olfactory bulb, corpus striatum and medial hebenula (PubMed:8463836,
CC PubMed:10414301, PubMed:16319318). Expressed in pancreatic islets
CC (PubMed:12403834). Expressed in heart and skeletal muscle
CC (PubMed:1740690, PubMed:19219384, PubMed:10414301). Levels remain
CC constant throughout postnatal development (PubMed:17192433). Expressed
CC in neocortical pyramidal neurons and inhibitory interneurons
CC (PubMed:1961744, PubMed:9522360, PubMed:10618149, PubMed:12832499,
CC PubMed:17192433, PubMed:17379638, PubMed:19014551, PubMed:20202934,
CC PubMed:24477962). Expressed in the superior cervical ganglion (SCG)
CC neurons (PubMed:12451110). Expressed in globus pallidus neurons
CC (PubMed:10414968). Expressed in pancreatic beta cells (PubMed:11463864,
CC PubMed:22411134). Expressed in cardiomyocytes (PubMed:17965280).
CC Expressed in arterial smooth muscle, alveolar epithelium and parenchyma
CC (at protein level) (PubMed:9362476, PubMed:9616203, PubMed:15322114).
CC Expressed in brain, heart, lung, liver, colon, kidney and adrenal gland
CC (PubMed:8508921, PubMed:9362476, PubMed:19074135). Expressed in
CC pyramidal cells of the cerebral cortex, in Purkinje and granule cells
CC of the cerebellum (PubMed:8463836). Expressed in CA1-CA3 pyramidal
CC cells, dentate granule cells and interneurons of the hippocampus
CC (PubMed:7623158, PubMed:10024359). Expressed in pulmonary artery (PA)
CC smooth muscle cells (PubMed:9362476). {ECO:0000269|PubMed:10024359,
CC ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10618149,
CC ECO:0000269|PubMed:11463864, ECO:0000269|PubMed:12403834,
CC ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12832499,
CC ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15322114,
CC ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:17192433,
CC ECO:0000269|PubMed:17379638, ECO:0000269|PubMed:1740690,
CC ECO:0000269|PubMed:17965280, ECO:0000269|PubMed:19014551,
CC ECO:0000269|PubMed:19074135, ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:1961744, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8463836,
CC ECO:0000269|PubMed:8508921, ECO:0000269|PubMed:9362476,
CC ECO:0000269|PubMed:9522360, ECO:0000269|PubMed:9616203}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic brain at 14 dpc, and
CC thereafter (at protein level) (PubMed:8508921). Expressed in embryonic
CC brain at 14 dpc, and thereafter (PubMed:8508921).
CC {ECO:0000269|PubMed:8508921}.
CC -!- INDUCTION: Down-regulated by angiotensin II in a NFATC3-dependent
CC manner (PubMed:15322114). {ECO:0000269|PubMed:15322114}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- DOMAIN: The N-terminal and C-terminal cytoplasmic regions mediate
CC homooligomerization; self-association is required to regulate
CC trafficking, gating and C-terminal phosphorylation-dependent modulation
CC of the channel (PubMed:12560340, PubMed:18463252, PubMed:19690160). The
CC N-terminal cytoplasmic region is important for interaction with other
CC channel-forming alpha subunits and with ancillary beta subunits
CC (PubMed:12954870, PubMed:19219384). The C-terminus is necessary and
CC sufficient for the restricted localization to, and clustering within,
CC both in soma and proximal portions of dendrite of neurons and in
CC lateral membrane of non-neuronal polarized cells (PubMed:8978827,
CC PubMed:10719893). The C-terminus is both necessary and sufficient as a
CC mediator of cholinergic and calcium-stimulated modulation of channel
CC cell membrane clustering localization and activity in hippocampal
CC neurons (PubMed:16407566). {ECO:0000250|UniProtKB:Q14721,
CC ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12560340,
CC ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:16407566,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:19690160, ECO:0000269|PubMed:8978827}.
CC -!- PTM: Phosphorylated (PubMed:8083226, PubMed:15195093, PubMed:16319318,
CC PubMed:16407566, PubMed:18463252). Differential C-terminal
CC phosphorylation on a subset of serines allows graded activity-dependent
CC regulation of channel gating in hippocampal neurons (PubMed:9351973,
CC PubMed:17192433, PubMed:16917065). Ser-607 and Tyr-128 are significant
CC sites of voltage-gated regulation through
CC phosphorylation/dephosphorylation activities (PubMed:12615930,
CC PubMed:17192433). Tyr-128 can be phosphorylated by Src and
CC dephosphorylated by cytoplasmic form of the phosphatase PTPRE isoform 2
CC (PubMed:12615930). CDK5-induced Ser-607 phosphorylation increases in
CC response to acute blockade of neuronal activity (PubMed:21712386).
CC Phosphorylated on Tyr-128 by Src and on Ser-804 by MAPK14/P38MAPK;
CC phosphorylations are necessary and sufficient for an increase in plasma
CC membrane insertion, apoptotic potassium current surge and completion of
CC the neuronal cell death program (PubMed:17360683, PubMed:19622611).
CC Phosphorylated on Ser-520, Ser-607, Ser-655 and Ser-804 by CDK5;
CC phosphorylation is necessary for KCNB1 channel clustering formation
CC (PubMed:21712386). The Ser-607 phosphorylation state differs between
CC KCNB1-containing clusters on the proximal and distal portions of the
CC axon initial segment (AIS) (PubMed:24477962). Highly phosphorylated on
CC serine residues in the C-terminal cytoplasmic tail in resting neurons
CC (PubMed:9351973, PubMed:16917065). Phosphorylated in pancreatic beta
CC cells in response to incretin hormones stimulation in a PKA- and
CC RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell survival
CC (PubMed:21818121). Phosphorylation on Ser-567 is reduced during
CC postnatal development with low levels at P2 and P5; levels then
CC increase to reach adult levels by P14 (PubMed:17192433).
CC Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and Ser-
CC 719 as well as the N-terminal Ser-15 are sensitive to calcineurin-
CC mediated dephosphorylation contributing to the modulation of the
CC voltage-dependent gating properties (PubMed:17192433, PubMed:16917065).
CC Dephosphorylation by phosphatase PTPRE isoform 2 confers
CC neuroprotection by its inhibitory influence on the neuronal apoptotic
CC potassium current surge in a Zn(2+)-dependent manner (PubMed:19622611).
CC Dephosphorylated at Ser-607 by protein phosphatase PPP1CA
CC (PubMed:21712386). Hypoxia-, seizure- or glutamate-induced neuronal
CC activities promote calcium/calcineurin-dependent dephosphorylation
CC resulting in a loss of KCNB1-containing clustering and enhanced channel
CC activity (PubMed:15195093, PubMed:16319318, PubMed:16407566,
CC PubMed:17192433, PubMed:16917065). In response to brain ischemia, Ser-
CC 567 and Ser-607 are strongly dephosphorylated while Ser-457 and Ser-719
CC are less dephosphorylated (PubMed:17192433). In response to brain
CC seizures, phosphorylation levels on Ser-567 and Ser-607 are greatly
CC reduced (PubMed:17192433). Phosphorylated/dephosphorylated by Src or
CC FYN tyrosine-protein kinases and tyrosine phosphatase PTPRE in primary
CC Schwann cells and sciatic nerve tissue (By similarity).
CC {ECO:0000250|UniProtKB:Q03717, ECO:0000269|PubMed:12615930,
CC ECO:0000269|PubMed:15195093, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:16407566, ECO:0000269|PubMed:16917065,
CC ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:17360683,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:18690023,
CC ECO:0000269|PubMed:19622611, ECO:0000269|PubMed:21712386,
CC ECO:0000269|PubMed:21818121, ECO:0000269|PubMed:24477962,
CC ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:9351973}.
CC -!- PTM: Acetylated. Acetylation occurs in pancreatic beta cells in
CC response to stimulation by incretin hormones in a histone
CC acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent signaling
CC pathway, promoting beta cell survival (PubMed:21818121).
CC {ECO:0000269|PubMed:21818121}.
CC -!- PTM: Sumoylated on Lys-474, preferentially with SUMO1; sumoylation
CC induces a positive shift in the voltage-dependence of activation and
CC inhibits channel activity (PubMed:21518833). Sumoylation increases the
CC frequency of repetitive action potential firing at the cell surface of
CC hippocampal neurons and decreases its frequency in pancreatic beta
CC cells (PubMed:21518833). Desumoylated by SENP1 (PubMed:21518833).
CC {ECO:0000269|PubMed:21518833}.
CC -!- PTM: Not glycosylated (PubMed:8083226). {ECO:0000269|PubMed:8083226}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
CC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA34497.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; X16476; CAA34497.1; ALT_INIT; mRNA.
DR PIR; S05448; CHRTD1.
DR RefSeq; NP_037318.1; NM_013186.1.
DR PDB; 2R9R; X-ray; 2.40 A; B/H=272-304.
DR PDB; 3LNM; X-ray; 2.90 A; B/D=272-304.
DR PDB; 4JTA; X-ray; 2.50 A; B/Q=274-306.
DR PDB; 4JTC; X-ray; 2.56 A; B/H=274-306.
DR PDB; 4JTD; X-ray; 2.54 A; B/H=274-306.
DR PDBsum; 2R9R; -.
DR PDBsum; 3LNM; -.
DR PDBsum; 4JTA; -.
DR PDBsum; 4JTC; -.
DR PDBsum; 4JTD; -.
DR AlphaFoldDB; P15387; -.
DR SMR; P15387; -.
DR BioGRID; 247764; 6.
DR CORUM; P15387; -.
DR IntAct; P15387; 4.
DR MINT; P15387; -.
DR STRING; 10116.ENSRNOP00000065961; -.
DR BindingDB; P15387; -.
DR ChEMBL; CHEMBL1075226; -.
DR GuidetoPHARMACOLOGY; 546; -.
DR iPTMnet; P15387; -.
DR PhosphoSitePlus; P15387; -.
DR PaxDb; P15387; -.
DR PRIDE; P15387; -.
DR ABCD; P15387; 8 sequenced antibodies.
DR Ensembl; ENSRNOT00000074023; ENSRNOP00000065961; ENSRNOG00000046949.
DR GeneID; 25736; -.
DR KEGG; rno:25736; -.
DR UCSC; RGD:2954; rat.
DR CTD; 3745; -.
DR RGD; 2954; Kcnb1.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000154899; -.
DR HOGENOM; CLU_011722_2_1_1; -.
DR InParanoid; P15387; -.
DR OrthoDB; 203440at2759; -.
DR PhylomeDB; P15387; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR EvolutionaryTrace; P15387; -.
DR PRO; PR:P15387; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Genevisible; P15387; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IMP:RGD.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
DR GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IDA:RGD.
DR GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
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:0015271; F:outward rectifier potassium channel activity; IMP:RGD.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:RGD.
DR GO; GO:0000149; F:SNARE binding; IPI:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0001508; P:action potential; IDA:UniProtKB.
DR GO; GO:0071277; P:cellular response to calcium ion; IDA:RGD.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IDA:UniProtKB.
DR GO; GO:0045163; P:clustering of voltage-gated potassium channels; IDA:RGD.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; IDA:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long-term synaptic depression; ISS:UniProtKB.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IMP:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0072659; P:protein localization to plasma membrane; IDA:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:2000671; P:regulation of motor neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0048678; P:response to axon injury; IEP:RGD.
DR GO; GO:1902065; P:response to L-glutamate; IEP:RGD.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:UniProtKB.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 2.
DR PRINTS; PR01514; KV21CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01495; SHABCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Exocytosis; Ion channel;
KW Ion transport; Isopeptide bond; Membrane; Phosphoprotein;
KW Postsynaptic cell membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Synaptosome;
KW Transmembrane; Transmembrane helix; Transport; Ubl conjugation;
KW Voltage-gated channel.
FT CHAIN 1..857
FT /note="Potassium voltage-gated channel subfamily B member
FT 1"
FT /id="PRO_0000054046"
FT TOPO_DOM 1..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 187..208
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..228
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 229..250
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 251..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 260..280
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 281..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 295..316
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 317..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 331..351
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 352..364
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 365..376
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 377..384
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 385..391
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 392..420
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 421..857
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..75
FT /note="Self-association"
FT /evidence="ECO:0000269|PubMed:18463252,
FT ECO:0000269|PubMed:19690160"
FT REGION 448..481
FT /note="Self-association"
FT /evidence="ECO:0000269|PubMed:18463252,
FT ECO:0000269|PubMed:19690160"
FT REGION 476..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..569
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 610..658
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 770..802
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..382
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT COMPBIAS 491..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..658
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023"
FT MOD_RES 128
FT /note="Phosphotyrosine; by Src"
FT /evidence="ECO:0000269|PubMed:12615930,
FT ECO:0000269|PubMed:19622611"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03717"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:18690023"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 520
FT /note="Phosphoserine; by CDK5; in vitro"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:21712386, ECO:0007744|PubMed:22673903"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065"
FT MOD_RES 607
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:18690023,
FT ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:24477962"
FT MOD_RES 655
FT /note="Phosphoserine; by CDK5; in vitro"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023, ECO:0000269|PubMed:21712386,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 719
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:18690023"
FT MOD_RES 771
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065"
FT MOD_RES 799
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023"
FT MOD_RES 804
FT /note="Phosphoserine; by CDK5, MAPK14; in vitro"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:18690023,
FT ECO:0000269|PubMed:21712386"
FT MOD_RES 836
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023"
FT CROSSLNK 474
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000269|PubMed:21518833"
FT MUTAGEN 15
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation. Additive effect on activation and steady-
FT state inactivation; when associated with A-457."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 15
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 71
FT /note="Q->E: Reduces channel activity."
FT /evidence="ECO:0000269|PubMed:12560340"
FT MUTAGEN 79
FT /note="E->D: No effect on channel activity."
FT /evidence="ECO:0000269|PubMed:12560340"
FT MUTAGEN 128
FT /note="Y->F: Reduces the increase of plasma membrane
FT insertion and apoptotic enhancement of potassium current
FT during cell death program. Significant loss of Src-mediated
FT phosphorylation and channel activity. Reduces interaction
FT with PTPRE. Increases cell viability against apoptotic
FT insults. Abolishes the increase of plasma membrane
FT insertion and apoptotic enhancement of potassium current
FT during cell death program; when associated with D-804."
FT /evidence="ECO:0000269|PubMed:12615930,
FT ECO:0000269|PubMed:19622611"
FT MUTAGEN 149
FT /note="K->Q: No loss of SUMO-dependent channel activity
FT modulation in hippocampal neurons."
FT /evidence="ECO:0000269|PubMed:21518833"
FT MUTAGEN 259
FT /note="K->Q: No loss of SUMO-dependent channel activity
FT modulation in hippocampal neurons."
FT /evidence="ECO:0000269|PubMed:21518833"
FT MUTAGEN 369
FT /note="W->C: Reduces channel activity. Does not inhibit
FT membrane plasma subcellular localization, interaction with
FT STX1A, pore-independent exocytosis activity and apoptotic
FT enhancement of potassium current during cell death program;
FT when associated with T-384."
FT /evidence="ECO:0000269|PubMed:12451110,
FT ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:17301173,
FT ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:20202934,
FT ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:22411134"
FT MUTAGEN 384
FT /note="Y->T: Reduces channel activity. Does not inhibit
FT membrane plasma subcellular localization, interaction with
FT STX1A, pore-independent exocytosis activity and apoptotic
FT enhancement of potassium current during cell death program;
FT when associated with C-369."
FT /evidence="ECO:0000269|PubMed:12451110,
FT ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:17301173,
FT ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:20484665,
FT ECO:0000269|PubMed:22411134"
FT MUTAGEN 444
FT /note="S->A: No effect on Src-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:9351973"
FT MUTAGEN 457
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation. Additive effect on activation and steady-
FT state inactivation; when associated with A-15."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 457
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 474
FT /note="K->Q: Loss of SUMO-dependent channel activity
FT modulation in hippocampal neurons."
FT /evidence="ECO:0000269|PubMed:21518833"
FT MUTAGEN 484
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 484
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 496
FT /note="S->A: No effect on Src-mediated phosphorylation."
FT /evidence="ECO:0000269|PubMed:9351973"
FT MUTAGEN 541
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 541
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 567
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation. Larger effect on activation and steady-state
FT inactivation; when associated with A-607."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 567
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 587
FT /note="S->A: Abolishes clustered subcellular distribution
FT in neurons."
FT /evidence="ECO:0000269|PubMed:10719893"
FT MUTAGEN 590
FT /note="S->A: Abolishes clustered subcellular distribution
FT in neurons. Does not affect KCNB1-containing vesicles
FT motility."
FT /evidence="ECO:0000269|PubMed:10719893,
FT ECO:0000269|PubMed:24569993"
FT MUTAGEN 591
FT /note="F->A: Abolishes clustered subcellular distribution
FT in neurons."
FT /evidence="ECO:0000269|PubMed:10719893"
FT MUTAGEN 593
FT /note="S->A: Abolishes clustered subcellular distribution
FT in neurons."
FT /evidence="ECO:0000269|PubMed:10719893"
FT MUTAGEN 607
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation. Larger effect on activation and steady-state
FT inactivation; when associated with A-567."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 607
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 655
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 655
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 719
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 719
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 771
FT /note="S->A: Shift in voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 771
FT /note="S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and steady-state
FT inactivation."
FT /evidence="ECO:0000269|PubMed:16917065"
FT MUTAGEN 804
FT /note="S->A: Reduces the increase of plasma membrane
FT insertion and apoptotic enhancement of potassium current
FT during cell death program. No change in calcineurin-
FT dependent regulation of voltage-dependent gating. Abolishes
FT the increase of plasma membrane insertion and apoptotic
FT enhancement of potassium current during cell death program;
FT when associated with F-128."
FT /evidence="ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:19622611"
FT MUTAGEN 804
FT /note="S->D: Does not reduce apoptotic enhancement of
FT potassium current during the cell death program."
FT /evidence="ECO:0000269|PubMed:17360683"
FT HELIX 274..281
FT /evidence="ECO:0007829|PDB:4JTA"
FT HELIX 286..302
FT /evidence="ECO:0007829|PDB:4JTA"
FT HELIX 303..307
FT /evidence="ECO:0007829|PDB:4JTA"
SQ SEQUENCE 857 AA; 95637 MW; B3C5B0839AB15FD0 CRC64;
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
RDCNTHDSLL QVCDDYSLED 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 SIAKKDKVQD
NHLSPNKWKW TKRALSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYSKMAKTQ
SQPILNTKEM APQSKPPEEL EMSSMPSPVA PLPARTEGVI DMRSMSSIDS FISCATDFPE
ATRFSHSPLA SLSSKAGSST APEVGWRGAL GASGGRLTET NPIPETSRSG FFVESPRSSM
KTNNPLKLRA LKVNFVEGDP TPLLPSLGLY HDPLRNRGGA AAAVAGLECA SLLDKPVLSP
ESSIYTTASA RTPPRSPEKH TAIAFNFEAG VHHYIDTDTD DEGQLLYSVD SSPPKSLHGS
TSPKFSTGAR TEKNHFESSP LPTSPKFLRP NCVYSSEGLT GKGPGAQEKC KLENHTPPDV
HMLPGGGAHG STRDQSI
