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 18-JAN-2017, entry version 146.
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;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC Muroidea; Muridae; Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-857, FUNCTION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ENZYME 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
RT from 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;
RA Drewe J.A., Verma S., Frech G.C., Joho R.H.;
RT "Distinct spatial and temporal expression patterns of K+ channel mRNAs
RT from 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 ENZYME 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
RT rectifier 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;
RA Hwang P.M., Fotuhi M., Bredt D.S., Cunningham A.M., Snyder S.H.;
RT "Contrasting immunohistochemical localizations in rat brain of two
RT novel K+ channels of the Shab subfamily.";
RL J. Neurosci. 13:1569-1576(1993).
RN [9]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, PHOSPHORYLATION, ENZYME
RP REGULATION, SUBCELLULAR LOCATION, AND ABSENCE OF GLYCOSYLATION.
RX PubMed=8083226;
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 ABSENCE OF INTERACTION
RP WITH KCNAB1 AND KCNAB2.
RX PubMed=7623158;
RA Rhodes K.J., Keilbaugh S.A., Barrezueta N.X., Lopez K.L.,
RA 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 ENZYME 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
RT of a 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;
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
RT inhibitory 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
RT combine and express a novel current.";
RL FEBS Lett. 399:177-182(1996).
RN [15]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNS3, SUBCELLULAR LOCATION,
RP ENZYME 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
RT oxygen-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
RT 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;
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,
RT Kv1.5 and Kv2.1, in hypoxic pulmonary vasoconstriction and control of
RT resting 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,
RT 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;
RA Murakoshi H., Trimmer J.S.;
RT "Identification of the Kv2.1 K+ channel as a major component of the
RT delayed 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;
RA Baranauskas G., Tkatch T., Surmeier D.J.;
RT "Delayed rectifier currents in rat globus pallidus neurons are
RT attributable 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;
RP PHE-591 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+
RT channel 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.,
RA Gaisano H.Y., 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;
RA Malin S.A., Nerbonne J.M.;
RT "Delayed rectifier K+ currents, IK, are encoded by Kv2 alpha-subunits
RT and 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
RT delayed rectifier K(+) current in rat mesenteric artery smooth muscle
RT 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.,
RA Wheeler M.B., Cattral M.S., Lakey J.R., Salapatek A.M., Lotan I.,
RA Gaisano H.Y.;
RT "Synaptosome-associated protein of 25 kilodaltons modulates Kv2.1
RT voltage-dependent K(+) channels in neuroendocrine islet beta-cells
RT through an interaction with the channel N terminus.";
RL Mol. Endocrinol. 16:2452-2461(2002).
RN [32]
RP ENZYME 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
RP MUTAGENESIS 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
RT Kv2.1 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
RT tyrosine 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.,
RA Lotan I., 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;
RA Pal S., Hartnett K.A., Nerbonne J.M., Levitan E.S., Aizenman E.;
RT "Mediation of neuronal apoptosis by Kv2.1-encoded potassium
RT channels.";
RL J. Neurosci. 23:4798-4802(2003).
RN [38]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNE3, SUBCELLULAR LOCATION,
RP DOMAIN, AND TISSUE SPECIFICITY.
RX PubMed=12954870;
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
RT in 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
RP 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
RT neuronal 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
RT vascular 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
RT cell surface microdomains.";
RL J. Cell Sci. 118:2155-2166(2005).
RN [43]
RP FUNCTION, PHOSPHORYLATION, DEPHOSPHORYLATION, SUBCELLULAR LOCATION,
RP AND 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-
RT dependent Kv2.1 channel regulates neuronal excitability in response to
RT 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
RT phosphorylation-dependent localization, voltage-dependent gating, and
RT muscarinic modulation 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;
RP SER-520; SER-541; SER-567; SER-590; SER-607; SER-655; SER-719;
RP SER-771; SER-799; SER-804 AND THR-836, FUNCTION, IDENTIFICATION BY
RP MASS SPECTROMETRY, AND MUTAGENESIS OF SER-15; SER-457; SER-484;
RP SER-541; SER-567; SER-607; 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;
RP SER-719; SER-799; SER-804 AND THR-836, AND IDENTIFICATION BY MASS
RP 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
RT determining 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-
RT population of cell surface Kv2.1 channels.";
RL J. Cell Sci. 120:2413-2423(2007).
RN [51]
RP FUNCTION, INTERACTION WITH STX1A, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF 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
RP SER-804, 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.,
RA Rosenberg P.A., Levitan E.S., Aizenman E.;
RT "Apoptotic surge of potassium currents is mediated by p38
RT phosphorylation 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
RT hippocampal 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
RT trafficking, 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
RT channel 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
RT activity-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
RT Kv2.1 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
RP 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
RT induced by a membrane-anchored protein mediate modulations in Kv
RT channel gating.";
RL J. Biol. Chem. 284:28276-28291(2009).
RN [62]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNE1 AND KCNE2, SUBCELLULAR
RP LOCATION, 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
RT excitotoxicity.";
RL J. Neurochem. 108:909-919(2009).
RN [64]
RP FUNCTION, PHOSPHORYLATION AT TYR-128, DEPHOSPHORYLATION, AND
RP MUTAGENESIS OF 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-
RT dependent 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
RP IDENTIFICATION 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
RP MUTAGENESIS OF 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.,
RA 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,
RP DEPHOSPHORYLATION 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
RT channels by 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
RP MASS 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
RT the 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
RT involve post-translational modification of Kv2.1 delayed rectifier
RT channels.";
RL Cell Death Differ. 19:333-344(2012).
RN [70]
RP FUNCTION, INTERACTION WITH STX1A, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, 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.,
RA Shapiro A.M., Gaisano H.Y., Lotan I., Macdonald P.E.;
RT "The voltage-dependent potassium channel subunit Kv2.1 regulates
RT insulin secretion from rodent and human islets independently of its
RT electrical 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
RP AND SER-655, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
RA Lundby C., Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14
RT different rat 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
RP 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
RP 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
RT membrane-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
RT voltage-dependent K(+) channel.";
RL Elife 2:E00594-E00594(2013).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates
CC transmembrane potassium transport in excitable membranes,
CC primarily in the brain, but also in the pancreas and
CC cardiovascular system. Contributes to the regulation of the action
CC potential (AP) repolarization, duration and frequency of
CC repetitive AP firing in neurons, muscle cells and endocrine cells
CC and plays a role in homeostatic attenuation of electrical
CC excitability throughout the brain (PubMed:10024359,
CC PubMed:10618149, PubMed:12451110, PubMed:17379638,
CC PubMed:19276663, PubMed:23878373). Plays also a role in the
CC regulation of exocytosis independently of its electrical function
CC (PubMed:20484665). Forms tetrameric potassium-selective channels
CC through which potassium ions pass in accordance with their
CC electrochemical gradient. The channel alternates between opened
CC and closed conformations in response to the voltage difference
CC across the membrane. Homotetrameric channels mediate a delayed-
CC rectifier voltage-dependent outward potassium current that display
CC 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
CC KCNB2; channel properties depend on the type of alpha subunits
CC that are part of the channel (PubMed:20202934). Can also form
CC functional heterotetrameric channels with other alpha subunits
CC that are non-conducting when expressed alone, such as KCNF1,
CC KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1,
CC creating a functionally diverse range of channel complexes
CC (PubMed:8670833, PubMed:8980147, PubMed:9362476, PubMed:9079713,
CC PubMed:9305895, PubMed:9696692). Heterotetrameric channel activity
CC formed with KCNS3 show increased current amplitude with the
CC threshold for action potential activation shifted towards more
CC negative values in hypoxic-treated pulmonary artery smooth muscle
CC cells (PubMed:9362476). Channel properties are also modulated by
CC cytoplasmic ancillary beta subunits such as AMIGO1, KCNE1, KCNE2
CC and KCNE3, slowing activation and inactivation rate of the delayed
CC rectifier potassium channels (PubMed:12954870, PubMed:19219384).
CC In vivo, membranes probably contain a mixture of heteromeric
CC potassium channel complexes, making it difficult to assign
CC currents observed in intact tissues to any particular potassium
CC channel family member. Major contributor to the slowly
CC inactivating delayed-rectifier voltage-gated potassium current in
CC neurons of the central nervous system, sympathetic ganglion
CC neurons, neuroendocrine cells, pancreatic beta cells,
CC cardiomyocytes and smooth muscle cells (PubMed:9362476,
CC PubMed:9616203, PubMed:10024359, PubMed:10414968, PubMed:10618149,
CC PubMed:11463864, PubMed:12451110, PubMed:12127166,
CC PubMed:12403834, PubMed:12621036, PubMed:12807875,
CC PubMed:12832499, PubMed:12954870, PubMed:15322114,
CC PubMed:15195093, PubMed:16407566, PubMed:17301173,
CC PubMed:17379638, PubMed:18463252, PubMed:18167541,
CC PubMed:19276663, PubMed:20484665, PubMed:21518833,
CC PubMed:22411134, PubMed:23878373). Mediates the major part of the
CC somatodendritic delayed-rectifier potassium current in hippocampal
CC and cortical pyramidal neurons and sympathetic superior cervical
CC ganglion (CGC) neurons that acts to slow down periods of firing,
CC especially during high frequency stimulation (PubMed:10618149,
CC PubMed:12451110, PubMed:16319318, PubMed:17379638,
CC PubMed:19276663, PubMed:23878373, PubMed:16917065). Plays a role
CC in the induction of long-term potentiation (LTP) of neuron
CC excitability in the CA3 layer of the hippocampus (By similarity).
CC Contributes to the regulation of glucose-induced action potential
CC amplitude and duration in pancreatic beta cells, hence limiting
CC calcium influx and insulin secretion (PubMed:11463864). Plays a
CC role in the regulation of resting membrane potential and
CC contraction in hypoxia-treated pulmonary artery smooth muscle
CC cells (PubMed:9616203). May contribute to the regulation of the
CC duration of both the action potential of cardiomyocytes and the
CC heart ventricular repolarization QT interval (By similarity).
CC Contributes to the pronounced pro-apoptotic potassium current
CC surge during neuronal apoptotic cell death in response to
CC oxidative injury (PubMed:12832499, PubMed:16273079,
CC 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
CC to the cell surface membrane, presumably by forming
CC heterotetrameric channels with these subunits (By similarity).
CC Plays a role in the calcium-dependent recruitment and release of
CC fusion-competent vesicles from the soma of neurons, neuroendocrine
CC and glucose-induced pancreatic beta cells by binding key
CC components of the fusion machinery in a pore-independent manner
CC (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 -!- ENZYME REGULATION: Inhibited by 42 nM hanatoxin 1 (HaTx1), a
CC spider venom toxin of the tarantula G. spatulata (PubMed:7576642).
CC Inhibited by 100 nM stromatoxin 1 (ScTx1), a spider venom toxin of
CC the tarantula S. calceata (PubMed:12065754). Modestly sensitive to
CC millimolar levels of tetraethylammonium (TEA) and 4-aminopyridine
CC (4-AP) (PubMed:2770868, PubMed:1875913, PubMed:8083226,
CC PubMed:9362476). Completely insensitive to toxins such as
CC dendrotoxin (DTX) and charybdotoxin (CTX) (PubMed:9362476).
CC {ECO:0000269|PubMed:12065754, ECO:0000269|PubMed:1875913,
CC ECO:0000269|PubMed:2770868, ECO:0000269|PubMed:7576642,
CC ECO:0000269|PubMed:8083226, ECO:0000269|PubMed:9362476,
CC ECO:0000305|PubMed:10414301, 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
CC more than 5 sec (PubMed:2206531, PubMed:8083226). Their
CC activation requires low threshold potentials of about -20 to -30
CC mV, with a midpoint activation at about 10 mV (PubMed:2770868,
CC PubMed:2206531, PubMed:8083226). For inactivation, the voltage
CC at half-maximal amplitude is about -20 mV (PubMed:2206531,
CC PubMed:8083226). The time constant for recovery after
CC inactivation is about 1.6 sec. Channels have an unitary
CC conductance of about 8 pS (PubMed:10414301, PubMed:15858231).
CC The voltage-dependence of activation and inactivation and other
CC channel characteristics vary depending on the experimental
CC conditions, the expression system, the presence or absence of
CC 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
CC (PubMed:20202934). Heterotetramer with non-conducting channel-
CC forming alpha subunits such as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1,
CC KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1 (PubMed:8670833,
CC PubMed:8980147, PubMed:9362476, PubMed:9079713, PubMed:9305895,
CC PubMed:9696692). Channel activity is regulated by association with
CC ancillary beta subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3
CC (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
CC modulation of the channel (PubMed:12560340, PubMed:18463252,
CC PubMed:19690160). Interacts (via C-terminus) with STX1A (via C-
CC terminus); this decreases the rate of channel activation and
CC increases the rate of channel inactivation in pancreatic beta
CC cells, induces also neuronal apoptosis in response to oxidative
CC injury as well as pore-independent enhancement of exocytosis in
CC neuroendocrine cells, chromaffin cells, pancreatic beta cells and
CC from the soma of dorsal root ganglia (DRG) neurons
CC (PubMed:12621036, PubMed:12807875, PubMed:17301173,
CC PubMed:18167541, PubMed:19077057, PubMed:20484665,
CC PubMed:22411134, PubMed:24928958). Interacts (via N-terminus) with
CC SNAP25; this decreases the rate of channel inactivation in
CC pancreatic beta cells and also increases interaction during
CC neuronal apoptosis in a N-methyl-D-aspartate receptor (NMDAR)-
CC dependent manner (PubMed:12403834, PubMed:12807875,
CC PubMed:19077057). Interacts (via N-terminus and C-terminus) with
CC VAMP2 (via N-terminus); stimulates channel inactivation rate
CC (PubMed:18542995, PubMed:19690160, PubMed:19077057). Interacts
CC with CREB1; this promotes channel acetylation in response to
CC stimulation by incretin hormones (PubMed:21818121). Interacts (via
CC N-terminus and C-terminus) with MYL12B (PubMed:24569993).
CC Interacts (via N-terminus) with PIAS3; this increases the number
CC of functional channels at the cell surface (PubMed:9565597).
CC Interacts with SUMO1. Interacts (via phosphorylated form) with
CC PTPRE; this reduces phosphorylation and channel activity in
CC heterologous cells (By similarity). {ECO:0000250|UniProtKB:Q03717,
CC ECO:0000250|UniProtKB:Q14721, ECO:0000269|PubMed:12403834,
CC ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:12621036,
CC ECO:0000269|PubMed:12807875, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:17301173, ECO:0000269|PubMed:18167541,
CC ECO:0000269|PubMed:18463252, ECO:0000269|PubMed:18542995,
CC ECO:0000269|PubMed:19077057, ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:19690160, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:20484665, ECO:0000269|PubMed:21818121,
CC ECO:0000269|PubMed:22411134, ECO:0000269|PubMed:24569993,
CC ECO:0000269|PubMed:24928958, ECO:0000269|PubMed:8670833,
CC ECO:0000269|PubMed:8980147, ECO:0000269|PubMed:9079713,
CC ECO:0000269|PubMed:9305895, ECO:0000269|PubMed:9362476,
CC ECO:0000269|PubMed:9565597, 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}.
CC Perikaryon {ECO:0000269|PubMed:10024359,
CC ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893,
CC ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093,
CC ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566,
CC ECO:0000269|PubMed:16988031, 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:1961744, ECO:0000269|PubMed:20202934,
CC ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:21712386,
CC ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:23878373,
CC ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993,
CC ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8463836,
CC ECO:0000269|PubMed:8978827, ECO:0000269|PubMed:9522360}. Cell
CC projection, dendrite {ECO:0000269|PubMed:10024359,
CC ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893,
CC ECO:0000269|PubMed:12954870, ECO:0000269|PubMed:15195093,
CC ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566,
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:20202934,
CC ECO:0000269|PubMed:21518833, ECO:0000269|PubMed:21712386,
CC ECO:0000269|PubMed:22648171, ECO:0000269|PubMed:23878373,
CC ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:24569993,
CC ECO:0000269|PubMed:7623158, ECO:0000269|PubMed:8463836,
CC ECO:0000269|PubMed:9522360}. Cell projection, axon
CC {ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:22648171,
CC ECO:0000269|PubMed:24477962}. Cell junction, synapse, postsynaptic
CC cell membrane {ECO:0000269|PubMed:9522360}. Cell junction, synapse
CC {ECO:0000269|PubMed:9522360}. Cell junction, synapse, synaptosome
CC {ECO:0000269|PubMed:8508921}. Membrane
CC {ECO:0000269|PubMed:8508921}; Multi-pass membrane protein. Lateral
CC cell membrane {ECO:0000269|PubMed:8978827}. Cell membrane,
CC sarcolemma {ECO:0000269|PubMed:17965280}. Note=Localizes to high-
CC density somatodendritic clusters and non-clustered sites on the
CC surface of neocortical and hippocampal pyramidal neurons in a
CC cortical actin cytoskeleton-dependent manner (PubMed:1961744,
CC PubMed:8978827, PubMed:9522360, PubMed:10024359, PubMed:10719893,
CC PubMed:15195093, PubMed:16319318, PubMed:16407566,
CC PubMed:16988031, PubMed:17606996, PubMed:17379638,
CC PubMed:19014551, PubMed:18463252, PubMed:22648171,
CC PubMed:23878373, PubMed:24569993, PubMed:24477962). Localizes also
CC to high-density clusters in the axon initial segment (AIS), at
CC ankyrin-G-deficient sites, on the surface of neocortical and
CC hippocampal pyramidal neurons (PubMed:17379638, PubMed:19014551,
CC PubMed:22648171, PubMed:24477962). KCNB1-containing AIS clusters
CC localize either in close apposition to smooth endoplasmic
CC reticulum cisternal organelles or with GABA-A receptor-containing
CC synapses of hippocampal and cortical pyramidal neurons,
CC respectively (PubMed:24477962). Localizes to high-density clusters
CC on the cell surface of atrial and ventricular myocytes and at the
CC lateral plasma membrane in epithelial cells (PubMed:8978827,
CC PubMed:17965280). Localizes both to the axial and transverse
CC tubules (T tubule) and sarcolemma in ventricular myocytes
CC (PubMed:17965280). Associated with lipid raft domains
CC (PubMed:15855232). In cortical neurons, apoptotic injuries induce
CC de novo plasma membrane insertion in a SNARE-dependent manner
CC causing an apoptotic potassium current surge (PubMed:16273079,
CC 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,
CC PubMed:1961744, PubMed:8508921, PubMed:7623158, PubMed:12954870).
CC Expressed in the hippocampus, cerebral cortex, cerebellum,
CC thalamus, hypothalamus, olfactory bulb, corpus striatum and medial
CC hebenula (PubMed:8463836, PubMed:10414301, PubMed:16319318).
CC Expressed in pancreatic islets (PubMed:12403834). Expressed in
CC heart and skeletal muscle (PubMed:1740690, PubMed:19219384,
CC PubMed:10414301). Levels remain constant throughout postnatal
CC development (PubMed:17192433). Expressed in neocortical pyramidal
CC neurons and inhibitory interneurons (PubMed:1961744,
CC PubMed:9522360, PubMed:10618149, PubMed:12832499, PubMed:17192433,
CC PubMed:17379638, PubMed:19014551, PubMed:20202934,
CC PubMed:24477962). Expressed in the superior cervical ganglion
CC (SCG) neurons (PubMed:12451110). Expressed in globus pallidus
CC neurons (PubMed:10414968). Expressed in pancreatic beta cells
CC (PubMed:11463864, PubMed:22411134). Expressed in cardiomyocytes
CC (PubMed:17965280). Expressed in arterial smooth muscle, alveolar
CC epithelium and parenchyma (at protein level) (PubMed:9362476,
CC PubMed:9616203, PubMed:15322114). Expressed in brain, heart, lung,
CC liver, colon, kidney and adrenal gland (PubMed:8508921,
CC PubMed:9362476, PubMed:19074135). Expressed in pyramidal cells of
CC the cerebral cortex, in Purkinje and granule cells of the
CC cerebellum (PubMed:8463836). Expressed in CA1-CA3 pyramidal cells,
CC dentate granule cells and interneurons of the hippocampus
CC (PubMed:7623158, PubMed:10024359). Expressed in pulmonary artery
CC (PA) smooth muscle cells (PubMed:9362476).
CC {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10414968,
CC ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:11463864,
CC ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12451110,
CC ECO:0000269|PubMed:12832499, ECO:0000269|PubMed:12954870,
CC ECO:0000269|PubMed:15322114, ECO:0000269|PubMed:16319318,
CC ECO:0000269|PubMed:17192433, ECO:0000269|PubMed:17379638,
CC ECO:0000269|PubMed:1740690, ECO:0000269|PubMed:17965280,
CC ECO:0000269|PubMed:19014551, ECO:0000269|PubMed:19074135,
CC ECO:0000269|PubMed:19219384, ECO:0000269|PubMed:1961744,
CC ECO:0000269|PubMed:20202934, ECO:0000269|PubMed:22411134,
CC ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:7623158,
CC ECO:0000269|PubMed:8463836, ECO:0000269|PubMed:8508921,
CC ECO:0000269|PubMed:9362476, ECO:0000269|PubMed:9522360,
CC ECO:0000269|PubMed:9616203}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryonic brain at 14 dpc, and
CC thereafter (at protein level) (PubMed:8508921). Expressed in
CC embryonic 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
CC and is characterized by a series of positively charged amino acids
CC at every third position. Channel opening and closing is effected
CC by a conformation change that affects the position and orientation
CC of the voltage-sensor paddle formed by S3 and S4 within the
CC membrane. A transmembrane electric field that is positive inside
CC would push the positively charged S4 segment outwards, thereby
CC opening the pore, while a field that is negative inside would pull
CC the S4 segment inwards and close the pore. Changes in the position
CC and orientation of S4 are then transmitted to the activation gate
CC formed by the inner helix bundle via the S4-S5 linker region.
CC {ECO:0000250|UniProtKB:P63142}.
CC -!- 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
CC modulation of the channel (PubMed:12560340, PubMed:18463252,
CC PubMed:19690160). The N-terminal cytoplasmic region is important
CC for interaction with other channel-forming alpha subunits and with
CC ancillary beta subunits (PubMed:12954870, PubMed:19219384). The C-
CC terminus is necessary and sufficient for the restricted
CC localization to, and clustering within, both in soma and proximal
CC portions of dendrite of neurons and in lateral membrane of non-
CC neuronal polarized cells (PubMed:8978827, PubMed:10719893). The C-
CC terminus is both necessary and sufficient as a mediator of
CC cholinergic and calcium-stimulated modulation of channel cell
CC 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,
CC PubMed:16319318, PubMed:16407566, PubMed:18463252). Differential
CC C-terminal phosphorylation on a subset of serines allows graded
CC activity-dependent regulation of channel gating in hippocampal
CC neurons (PubMed:9351973, PubMed:17192433, PubMed:16917065). Ser-
CC 607 and Tyr-128 are significant sites of voltage-gated regulation
CC through phosphorylation/dephosphorylation activities
CC (PubMed:12615930, PubMed:17192433). Tyr-128 can be phosphorylated
CC by Src and dephosphorylated by cytoplasmic form of the phosphatase
CC PTPRE isoform 2 (PubMed:12615930). CDK5-induced Ser-607
CC phosphorylation increases in response to acute blockade of
CC neuronal activity (PubMed:21712386). Phosphorylated on Tyr-128 by
CC Src and on Ser-804 by MAPK14/P38MAPK; phosphorylations are
CC necessary and sufficient for an increase in plasma membrane
CC insertion, apoptotic potassium current surge and completion of the
CC 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
CC formation (PubMed:21712386). The Ser-607 phosphorylation state
CC differs between KCNB1-containing clusters on the proximal and
CC distal portions of the axon initial segment (AIS)
CC (PubMed:24477962). Highly phosphorylated on serine residues in the
CC C-terminal cytoplasmic tail in resting neurons (PubMed:9351973,
CC PubMed:16917065). Phosphorylated in pancreatic beta cells in
CC response to incretin hormones stimulation in a PKA- and
CC RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell
CC survival (PubMed:21818121). Phosphorylation on Ser-567 is reduced
CC during postnatal development with low levels at P2 and P5; levels
CC then increase to reach adult levels by P14 (PubMed:17192433).
CC Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-607, Ser-655 and
CC Ser-719 as well as the N-terminal Ser-15 are sensitive to
CC calcineurin-mediated dephosphorylation contributing to the
CC modulation of the voltage-dependent gating properties
CC (PubMed:17192433, PubMed:16917065). Dephosphorylation by
CC phosphatase PTPRE isoform 2 confers neuroprotection by its
CC inhibitory influence on the neuronal apoptotic potassium current
CC 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
CC neuronal activities promote calcium/calcineurin-dependent
CC dephosphorylation resulting in a loss of KCNB1-containing
CC clustering and enhanced channel activity (PubMed:15195093,
CC PubMed:16319318, PubMed:16407566, PubMed:17192433,
CC PubMed:16917065). In response to brain ischemia, Ser-567 and Ser-
CC 607 are strongly dephosphorylated while Ser-457 and Ser-719 are
CC less dephosphorylated (PubMed:17192433). In response to brain
CC seizures, phosphorylation levels on Ser-567 and Ser-607 are
CC greatly reduced (PubMed:17192433). Phosphorylated/dephosphorylated
CC by Src or FYN tyrosine-protein kinases and tyrosine phosphatase
CC PTPRE in primary Schwann cells and sciatic nerve tissue (By
CC similarity). {ECO:0000250|UniProtKB:Q03717,
CC ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:15195093,
CC ECO:0000269|PubMed:16319318, ECO:0000269|PubMed:16407566,
CC ECO:0000269|PubMed:16917065, ECO:0000269|PubMed:17192433,
CC ECO:0000269|PubMed:17360683, ECO:0000269|PubMed:18463252,
CC ECO:0000269|PubMed:18690023, ECO:0000269|PubMed:19622611,
CC ECO:0000269|PubMed:21712386, ECO:0000269|PubMed:21818121,
CC ECO:0000269|PubMed:24477962, ECO:0000269|PubMed:8083226,
CC 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
CC signaling 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
CC and inhibits channel activity (PubMed:21518833). Sumoylation
CC increases the frequency of repetitive action potential firing at
CC the cell surface of hippocampal neurons and decreases its
CC frequency in pancreatic beta cells (PubMed:21518833). Desumoylated
CC by SENP1 (PubMed:21518833). {ECO:0000269|PubMed:21518833}.
CC -!- PTM: Not glycosylated (PubMed:8083226).
CC {ECO:0000269|PubMed:8083226}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab)
CC (TC 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};
DR EMBL; X16476; CAA34497.1; ALT_INIT; mRNA.
DR PIR; S05448; CHRTD1.
DR RefSeq; NP_037318.1; NM_013186.1.
DR UniGene; Rn.26724; -.
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 ProteinModelPortal; P15387; -.
DR SMR; P15387; -.
DR BioGrid; 247764; 5.
DR IntAct; P15387; 4.
DR MINT; MINT-8283237; -.
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 GeneID; 25736; -.
DR KEGG; rno:25736; -.
DR UCSC; RGD:2954; rat.
DR CTD; 3745; -.
DR RGD; 2954; Kcnb1.
DR eggNOG; KOG3713; Eukaryota.
DR eggNOG; COG1226; LUCA.
DR HOVERGEN; HBG052225; -.
DR InParanoid; P15387; -.
DR KO; K04885; -.
DR OrthoDB; EOG091G0FP3; -.
DR PhylomeDB; P15387; -.
DR EvolutionaryTrace; P15387; -.
DR PRO; PR:P15387; -.
DR Proteomes; UP000002494; Unplaced.
DR Bgee; ENSRNOG00000046949; -.
DR Genevisible; P15387; RN.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
DR GO; GO:0032590; C:dendrite membrane; IDA:RGD.
DR GO; GO:0005622; C:intracellular; IEA:GOC.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; 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:0044325; F:ion channel binding; IPI: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:0005249; F:voltage-gated potassium channel activity; IDA:MGI.
DR GO; GO:0001508; P:action potential; IDA:UniProtKB.
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: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: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:0051259; P:protein oligomerization; IMP:RGD.
DR GO; GO:0072661; P:protein targeting to plasma membrane; IDA:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
DR GO; GO:2000671; P:regulation of motor neuron apoptotic process; IDA:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; IDA:UniProtKB.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR027359; Channel_four-helix_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.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 2.
DR PRINTS; PR00169; KCHANNEL.
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 junction; Cell membrane; Cell projection;
KW Complete proteome; Exocytosis; Ion channel; Ion transport;
KW Isopeptide bond; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1 857 Potassium voltage-gated channel subfamily
FT B member 1.
FT /FTId=PRO_0000054046.
FT TOPO_DOM 1 186 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 187 208 Helical; Name=Segment S1. {ECO:0000255}.
FT TOPO_DOM 209 228 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 229 250 Helical; Name=Segment S2. {ECO:0000255}.
FT TOPO_DOM 251 259 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 260 280 Helical; Name=Segment S3.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 281 294 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 295 316 Helical; Voltage-sensor; Name=Segment S4.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 317 330 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 331 351 Helical; Name=Segment S5.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 352 364 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT INTRAMEM 365 376 Helical; Name=Pore helix.
FT {ECO:0000250|UniProtKB:P63142}.
FT INTRAMEM 377 384 {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 385 391 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 392 420 Helical; Name=Segment S6.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 421 857 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT REGION 59 75 Self-association.
FT {ECO:0000269|PubMed:18463252,
FT ECO:0000269|PubMed:19690160}.
FT REGION 448 481 Self-association.
FT {ECO:0000269|PubMed:18463252,
FT ECO:0000269|PubMed:19690160}.
FT MOTIF 377 382 Selectivity filter.
FT {ECO:0000250|UniProtKB:P63142}.
FT COMPBIAS 517 520 Poly-Ser.
FT COMPBIAS 700 705 Poly-Ala.
FT MOD_RES 15 15 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023}.
FT MOD_RES 128 128 Phosphotyrosine; by Src.
FT {ECO:0000269|PubMed:12615930,
FT ECO:0000269|PubMed:19622611}.
FT MOD_RES 444 444 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q03717}.
FT MOD_RES 457 457 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433,
FT ECO:0000269|PubMed:18690023}.
FT MOD_RES 484 484 Phosphoserine.
FT {ECO:0000244|PubMed:22673903,
FT ECO:0000269|PubMed:16917065}.
FT MOD_RES 496 496 Phosphoserine.
FT {ECO:0000269|PubMed:16917065}.
FT MOD_RES 503 503 Phosphoserine.
FT {ECO:0000269|PubMed:16917065}.
FT MOD_RES 519 519 Phosphoserine.
FT {ECO:0000244|PubMed:22673903}.
FT MOD_RES 520 520 Phosphoserine; by CDK5; in vitro.
FT {ECO:0000244|PubMed:22673903,
FT ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:21712386}.
FT MOD_RES 541 541 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023}.
FT MOD_RES 567 567 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433}.
FT MOD_RES 590 590 Phosphoserine.
FT {ECO:0000269|PubMed:16917065}.
FT MOD_RES 607 607 Phosphoserine; by CDK5.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433,
FT ECO:0000269|PubMed:18690023,
FT ECO:0000269|PubMed:21712386,
FT ECO:0000269|PubMed:24477962}.
FT MOD_RES 655 655 Phosphoserine; by CDK5; in vitro.
FT {ECO:0000244|PubMed:22673903,
FT ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023,
FT ECO:0000269|PubMed:21712386}.
FT MOD_RES 719 719 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17192433,
FT ECO:0000269|PubMed:18690023}.
FT MOD_RES 771 771 Phosphoserine.
FT {ECO:0000269|PubMed:16917065}.
FT MOD_RES 799 799 Phosphoserine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023}.
FT MOD_RES 804 804 Phosphoserine; by CDK5, MAPK14; in vitro.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17360683,
FT ECO:0000269|PubMed:18690023,
FT ECO:0000269|PubMed:21712386}.
FT MOD_RES 836 836 Phosphothreonine.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:18690023}.
FT CROSSLNK 474 474 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT {ECO:0000269|PubMed:21518833}.
FT MUTAGEN 15 15 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation. Additive
FT effect on activation and steady-state
FT inactivation; when associated with A-457.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 15 15 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 71 71 Q->E: Reduces channel activity.
FT {ECO:0000269|PubMed:12560340}.
FT MUTAGEN 79 79 E->D: No effect on channel activity.
FT {ECO:0000269|PubMed:12560340}.
FT MUTAGEN 128 128 Y->F: Reduces the increase of plasma
FT membrane insertion and apoptotic
FT enhancement of potassium current during
FT cell death program. Significant loss of
FT Src-mediated phosphorylation and channel
FT activity. Reduces interaction with PTPRE.
FT Increases cell viability against
FT apoptotic insults. Abolishes the increase
FT of plasma membrane insertion and
FT apoptotic enhancement of potassium
FT current during cell death program; when
FT associated with D-804.
FT {ECO:0000269|PubMed:12615930,
FT ECO:0000269|PubMed:19622611}.
FT MUTAGEN 149 149 K->Q: No loss of SUMO-dependent channel
FT activity modulation in hippocampal
FT neurons. {ECO:0000269|PubMed:21518833}.
FT MUTAGEN 259 259 K->Q: No loss of SUMO-dependent channel
FT activity modulation in hippocampal
FT neurons. {ECO:0000269|PubMed:21518833}.
FT MUTAGEN 369 369 W->C: Reduces channel activity. Does not
FT inhibit membrane plasma subcellular
FT localization, interaction with STX1A,
FT pore-independent exocytosis activity and
FT apoptotic enhancement of potassium
FT current during cell death program; when
FT associated with T-384.
FT {ECO:0000269|PubMed:12451110,
FT ECO:0000269|PubMed:12832499,
FT ECO:0000269|PubMed:17301173,
FT ECO:0000269|PubMed:17360683,
FT ECO:0000269|PubMed:20202934,
FT ECO:0000269|PubMed:20484665,
FT ECO:0000269|PubMed:22411134}.
FT MUTAGEN 384 384 Y->T: Reduces channel activity. Does not
FT inhibit membrane plasma subcellular
FT localization, interaction with STX1A,
FT pore-independent exocytosis activity and
FT apoptotic enhancement of potassium
FT current during cell death program; when
FT associated with C-369.
FT {ECO:0000269|PubMed:12451110,
FT ECO:0000269|PubMed:12832499,
FT ECO:0000269|PubMed:17301173,
FT ECO:0000269|PubMed:20202934,
FT ECO:0000269|PubMed:20484665,
FT ECO:0000269|PubMed:22411134}.
FT MUTAGEN 444 444 S->A: No effect on Src-mediated
FT phosphorylation.
FT {ECO:0000269|PubMed:9351973}.
FT MUTAGEN 457 457 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation. Additive
FT effect on activation and steady-state
FT inactivation; when associated with A-15.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 457 457 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 474 474 K->Q: Loss of SUMO-dependent channel
FT activity modulation in hippocampal
FT neurons. {ECO:0000269|PubMed:21518833}.
FT MUTAGEN 484 484 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 484 484 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 496 496 S->A: No effect on Src-mediated
FT phosphorylation.
FT {ECO:0000269|PubMed:9351973}.
FT MUTAGEN 541 541 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 541 541 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 567 567 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation. Larger effect
FT on activation and steady-state
FT inactivation; when associated with A-607.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 567 567 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 587 587 S->A: Abolishes clustered subcellular
FT distribution in neurons.
FT {ECO:0000269|PubMed:10719893}.
FT MUTAGEN 590 590 S->A: Abolishes clustered subcellular
FT distribution in neurons. Does not affect
FT KCNB1-containing vesicles motility.
FT {ECO:0000269|PubMed:10719893,
FT ECO:0000269|PubMed:24569993}.
FT MUTAGEN 591 591 F->A: Abolishes clustered subcellular
FT distribution in neurons.
FT {ECO:0000269|PubMed:10719893}.
FT MUTAGEN 593 593 S->A: Abolishes clustered subcellular
FT distribution in neurons.
FT {ECO:0000269|PubMed:10719893}.
FT MUTAGEN 607 607 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation. Larger effect
FT on activation and steady-state
FT inactivation; when associated with A-567.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 607 607 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 655 655 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 655 655 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 719 719 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 719 719 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 771 771 S->A: Shift in voltage-dependent gating
FT on calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 771 771 S->D: Resists voltage-dependent gating on
FT calcineurin-dependent activation and
FT steady-state inactivation.
FT {ECO:0000269|PubMed:16917065}.
FT MUTAGEN 804 804 S->A: Reduces the increase of plasma
FT membrane insertion and apoptotic
FT enhancement of potassium current during
FT cell death program. No change in
FT calcineurin-dependent regulation of
FT voltage-dependent gating. Abolishes the
FT increase of plasma membrane insertion and
FT apoptotic enhancement of potassium
FT current during cell death program; when
FT associated with F-128.
FT {ECO:0000269|PubMed:16917065,
FT ECO:0000269|PubMed:17360683,
FT ECO:0000269|PubMed:19622611}.
FT MUTAGEN 804 804 S->D: Does not reduce apoptotic
FT enhancement of potassium current during
FT the cell death program.
FT {ECO:0000269|PubMed:17360683}.
FT HELIX 274 281 {ECO:0000244|PDB:4JTA}.
FT HELIX 286 302 {ECO:0000244|PDB:4JTA}.
FT HELIX 303 306 {ECO:0000244|PDB:4JTA}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 189 423 ipfam:Ion_trans [T]
FT MYHIT 33 132 ipfam:BTB_2 [T]
FT MYHIT 648 678 ipfam:Kv2channel [T]
FT MYHIT 31 140 ismart:BTB [T]
FT MYHIT 467 613 ipfam:Kv2channel [T]
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
//
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