KCAB2_RAT
ID KCAB2_RAT Reviewed; 367 AA.
AC P62483; P97381; Q60942; Q64284;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Voltage-gated potassium channel subunit beta-2;
DE EC=1.1.1.- {ECO:0000269|PubMed:18672894, ECO:0000269|PubMed:21209188};
DE AltName: Full=K(+) channel subunit beta-2;
DE AltName: Full=Kv-beta-2;
GN Name=Kcnab2; Synonyms=Ckbeta2, Kcnb3;
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].
RC TISSUE=Brain cortex;
RX PubMed=8183366; DOI=10.1038/369289a0;
RA Rettig J., Heinemann S.H., Wunder F., Lorra C., Parcej D.N., Dolly J.O.,
RA Pongs O.;
RT "Inactivation properties of voltage-gated K+ channels altered by presence
RT of beta-subunit.";
RL Nature 369:289-294(1994).
RN [2]
RP INTERACTION WITH KCNA1; KCNA2; KCNA4; KCNA6 AND KCNAB1, SUBUNIT, TISSUE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=9334400; DOI=10.1523/jneurosci.17-21-08246.1997;
RA Rhodes K.J., Strassle B.W., Monaghan M.M., Bekele-Arcuri Z., Matos M.F.,
RA Trimmer J.S.;
RT "Association and colocalization of the Kvbeta1 and Kvbeta2 beta-subunits
RT with Kv1 alpha-subunits in mammalian brain K+ channel complexes.";
RL J. Neurosci. 17:8246-8258(1997).
RN [3]
RP FUNCTION.
RX PubMed=9763623; DOI=10.1111/j.1469-7793.1998.325be.x;
RA Accili E.A., Kuryshev Y.A., Wible B.A., Brown A.M.;
RT "Separable effects of human Kvbeta1.2 N- and C-termini on inactivation and
RT expression of human Kv1.4.";
RL J. Physiol. (Lond.) 512:325-336(1998).
RN [4]
RP INTERACTION WITH SQSTM1 AND PRKCZ, AND PHOSPHORYLATION BY PRKCZ.
RX PubMed=10477520; DOI=10.1126/science.285.5433.1565;
RA Gong J., Xu J., Bezanilla M., van Huizen R., Derin R., Li M.;
RT "Differential stimulation of PKC phosphorylation of potassium channels by
RT ZIP1 and ZIP2.";
RL Science 285:1565-1569(1999).
RN [5]
RP FUNCTION.
RX PubMed=10896669; DOI=10.1074/jbc.m005010200;
RA Manganas L.N., Trimmer J.S.;
RT "Subunit composition determines Kv1 potassium channel surface expression.";
RL J. Biol. Chem. 275:29685-29693(2000).
RN [6]
RP INTERACTION WITH KCNA1 AND KCNA2, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11086297;
RX DOI=10.1002/1096-9861(20000101)429:1<166::aid-cne13>3.0.co;2-y;
RA Rasband M.N., Trimmer J.S.;
RT "Subunit composition and novel localization of K+ channels in spinal
RT cord.";
RL J. Comp. Neurol. 429:166-176(2001).
RN [7]
RP INTERACTION WITH KCNA4 AND KCND3.
RX PubMed=12860406; DOI=10.1016/s0014-5793(03)00705-1;
RA Wang L., Takimoto K., Levitan E.S.;
RT "Differential association of the auxiliary subunit Kvbeta2 with Kv1.4 and
RT Kv4.3 K+ channels.";
RL FEBS Lett. 547:162-164(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND TISSUE SPECIFICITY.
RX PubMed=15618540; DOI=10.1161/01.res.0000154070.06421.25;
RA Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T.,
RA Cole W.;
RT "Heteromultimeric Kv1 channels contribute to myogenic control of arterial
RT diameter.";
RL Circ. Res. 96:216-224(2005).
RN [9]
RP INTERACTION WITH SQSTM1; IKBKB AND TRAF6.
RX PubMed=16079148; DOI=10.1074/jbc.c500237200;
RA Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T.,
RA Moscat J.;
RT "The p62 scaffold regulates nerve growth factor-induced NF-kappaB
RT activation by influencing TRAF6 polyubiquitination.";
RL J. Biol. Chem. 280:35625-35629(2005).
RN [10]
RP FUNCTION.
RX PubMed=16770729; DOI=10.1007/s11064-006-9056-4;
RA Fujita T., Utsunomiya I., Ren J., Matsushita Y., Kawai M., Sasaki S.,
RA Hoshi K., Miyatake T., Taguchi K.;
RT "Glycosylation and cell surface expression of Kv1.2 potassium channel are
RT regulated by determinants in the pore region.";
RL Neurochem. Res. 31:589-596(2006).
RN [11]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-90, AND ACTIVE
RP SITE.
RX PubMed=18672894; DOI=10.1021/bi800301b;
RA Tipparaju S.M., Barski O.A., Srivastava S., Bhatnagar A.;
RT "Catalytic mechanism and substrate specificity of the beta-subunit of the
RT voltage-gated potassium channel.";
RL Biochemistry 47:8840-8854(2008).
RN [12]
RP FUNCTION, INTERACTION WITH KCNA2, AND SUBUNIT.
RX PubMed=18003609; DOI=10.1074/jbc.m708875200;
RA Connors E.C., Ballif B.A., Morielli A.D.;
RT "Homeostatic regulation of Kv1.2 potassium channel trafficking by cyclic
RT AMP.";
RL J. Biol. Chem. 283:3445-3453(2008).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNA2 AND MAPRE1, TISSUE
RP SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-9;
RP SER-20 AND SER-112, AND MUTAGENESIS OF SER-9; SER-20 AND SER-31.
RX PubMed=21357749; DOI=10.1083/jcb.201007113;
RA Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B.,
RA Trimmer J.S.;
RT "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates
RT Kv1 channel axonal targeting.";
RL J. Cell Biol. 192:813-824(2011).
RN [14]
RP FUNCTION, AND MUTAGENESIS OF TYR-90.
RX PubMed=21209188; DOI=10.1523/jneurosci.2634-10.2011;
RA Perkowski J.J., Murphy G.G.;
RT "Deletion of the mouse homolog of KCNAB2, a gene linked to monosomy 1p36,
RT results in associative memory impairments and amygdala hyperexcitability.";
RL J. Neurosci. 31:46-54(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-20, AND
RP 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 [16]
RP SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNA1 AND KCNA2, AND TISSUE
RP SPECIFICITY.
RX PubMed=23318870; DOI=10.1113/jphysiol.2012.249706;
RA Ovsepian S.V., Steuber V., Le Berre M., O'Hara L., O'Leary V.B.,
RA Dolly J.O.;
RT "A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking and
RT regulates the output of deep cerebellar nuclear neurons to thalamic
RT targets.";
RL J. Physiol. (Lond.) 591:1771-1791(2013).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP,
RP INTERACTION WITH KCNA1, AND SUBUNIT.
RX PubMed=10884227; DOI=10.1126/science.289.5476.123;
RA Gulbis J.M., Zhou M., Mann S., MacKinnon R.;
RT "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent
RT K+ channels.";
RL Science 289:123-127(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP AND
RP KCNA2, AND SUBUNIT.
RX PubMed=16002581; DOI=10.1126/science.1116269;
RA Long S.B., Campbell E.B., Mackinnon R.;
RT "Crystal structure of a mammalian voltage-dependent Shaker family K+
RT channel.";
RL Science 309:897-903(2005).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP AND
RP KCNA2, AND SUBUNIT.
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 [20]
RP X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 36-361 IN COMPLEX WITH KCNA2;
RP CORTISONE AND NADP, AND SUBUNIT.
RX PubMed=18806782; DOI=10.1038/nchembio.114;
RA Pan Y., Weng J., Kabaleeswaran V., Li H., Cao Y., Bhosle R.C., Zhou M.;
RT "Cortisone dissociates the Shaker family K+ channels from their beta
RT subunits.";
RL Nat. Chem. Biol. 4:708-714(2008).
RN [21]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH KCNA2 AND NADP, AND
RP SUBUNIT.
RX PubMed=20534430; DOI=10.1073/pnas.1000142107;
RA Chen X., Wang Q., Ni F., Ma J.;
RT "Structure of the full-length Shaker potassium channel Kv1.2 by normal-
RT mode-based X-ray crystallographic refinement.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:11352-11357(2010).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 36-367 IN COMPLEX WITH KCNA2 AND
RP NADP, AND SUBUNIT.
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 [23]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 36-367 IN COMPLEX WITH KCNA2 AND
RP NADP, AND SUBUNIT.
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: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits (PubMed:9763623,
CC PubMed:21357749). Contributes to the regulation of nerve signaling, and
CC prevents neuronal hyperexcitability (By similarity). Promotes
CC expression of the pore-forming alpha subunits at the cell membrane, and
CC thereby increases channel activity (PubMed:10896669, PubMed:16770729,
CC PubMed:18003609, PubMed:21357749). Promotes potassium channel closure
CC via a mechanism that does not involve physical obstruction of the
CC channel pore (PubMed:21357749). Modulates the functional properties of
CC KCNA4 (PubMed:9763623). Modulates the functional properties of KCNA5
CC (By similarity). Enhances KCNB2 channel activity (By similarity). Binds
CC NADPH and has NADPH-dependent aldoketoreductase activity
CC (PubMed:18672894, PubMed:21209188). Has broad substrate specificity and
CC can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone,
CC prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-
CC trans-2-nonenal (in vitro) (PubMed:18672894).
CC {ECO:0000250|UniProtKB:P62482, ECO:0000269|PubMed:10896669,
CC ECO:0000269|PubMed:18003609, ECO:0000269|PubMed:18672894,
CC ECO:0000269|PubMed:21209188, ECO:0000269|PubMed:21357749,
CC ECO:0000269|PubMed:9763623}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.2-7.4.;
CC -!- SUBUNIT: Homotetramer (PubMed:10884227, PubMed:16002581,
CC PubMed:18004376, PubMed:18806782, PubMed:20534430, PubMed:20360102,
CC PubMed:23705070). Interaction with tetrameric potassium channel alpha
CC subunits gives rise to a heterooctamer (PubMed:10884227,
CC PubMed:16002581, PubMed:18004376, PubMed:18806782, PubMed:20534430,
CC PubMed:20360102, PubMed:23705070). Identified in potassium channel
CC complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and
CC KCNAB2 (PubMed:9334400). Interacts with KCNA1 (PubMed:23318870,
CC PubMed:10884227). Interacts with KCNA2 (PubMed:18003609,
CC PubMed:21357749, PubMed:23318870, PubMed:16002581, PubMed:18004376,
CC PubMed:18806782, PubMed:20534430, PubMed:20360102, PubMed:23705070).
CC Interacts with KCNA4 and KCND3 (PubMed:12860406). Interacts with KCNA5
CC (By similarity). Interacts with KCNB2 (By similarity). Interacts (in
CC unphosphorylated form) with MAPRE1 (PubMed:21357749). Forms a ternary
CC complex with SQSTM1 and PRKCZ (PubMed:10477520).
CC {ECO:0000250|UniProtKB:P62482, ECO:0000269|PubMed:10477520,
CC ECO:0000269|PubMed:10884227, ECO:0000269|PubMed:12860406,
CC ECO:0000269|PubMed:16002581, ECO:0000269|PubMed:18003609,
CC ECO:0000269|PubMed:18004376, ECO:0000269|PubMed:18806782,
CC ECO:0000269|PubMed:20360102, ECO:0000269|PubMed:20534430,
CC ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:23318870,
CC ECO:0000269|PubMed:23705070, ECO:0000269|PubMed:9334400,
CC ECO:0000269|PubMed:9763623}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21357749}. Membrane
CC {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:9334400}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
CC membrane {ECO:0000269|PubMed:23318870}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell projection, axon
CC {ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:9334400}. Synapse,
CC synaptosome {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:21357749}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. Associates with microtubules when
CC unphosphorylated (PubMed:21357749). {ECO:0000269|PubMed:21357749,
CC ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Detected in brain (PubMed:9334400,
CC PubMed:21357749). Detected in the middle third of the molecular layer
CC of the dentate gyrus in hippocampus (PubMed:9334400). Detected in
CC neurons in the deep cerebellar nucleus (PubMed:23318870). Detected in
CC globus pallidus and pars reticulata of the substantia nigra
CC (PubMed:9334400). Detected in cerebellum (PubMed:23318870). Detected at
CC axon terminal plexuses of cerebellar granule cells (PubMed:9334400).
CC Detected in the juxtaparanodal region of nodes of Ranvier in cerebellum
CC (at protein level) (PubMed:9334400). Detected in mesenteric arteries
CC (PubMed:15618540). {ECO:0000269|PubMed:15618540,
CC ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:23318870,
CC ECO:0000269|PubMed:9334400}.
CC -!- DOMAIN: In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2
CC cannot mediate closure of delayed rectifier potassium channels by
CC physically obstructing the pore. {ECO:0000250|UniProtKB:Q13303}.
CC -!- PTM: Phosphorylated by PRKCZ; may be regulated by incorporation in a
CC complex composed of PRKCZ and SQSTM1. {ECO:0000269|PubMed:10477520}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; X76724; CAA54142.1; -; mRNA.
DR PIR; S45312; S45312.
DR RefSeq; NP_059000.1; NM_017304.2.
DR PDB; 1EXB; X-ray; 2.10 A; A=36-367.
DR PDB; 1QRQ; X-ray; 2.80 A; A/B/C/D=36-360.
DR PDB; 2A79; X-ray; 2.90 A; A=36-367.
DR PDB; 2R9R; X-ray; 2.40 A; A/G=36-367.
DR PDB; 3EAU; X-ray; 1.82 A; A=36-361.
DR PDB; 3EB3; X-ray; 2.00 A; A=36-361.
DR PDB; 3EB4; X-ray; 2.00 A; A=36-361.
DR PDB; 3LNM; X-ray; 2.90 A; A/C=36-367.
DR PDB; 3LUT; X-ray; 2.90 A; A=1-367.
DR PDB; 4JTA; X-ray; 2.50 A; A/P=36-367.
DR PDB; 4JTC; X-ray; 2.56 A; A/G=36-367.
DR PDB; 4JTD; X-ray; 2.54 A; A/G=36-367.
DR PDB; 5WIE; X-ray; 3.30 A; A/G=35-367.
DR PDB; 6CI1; EM; 4.90 A; A/B/C/D/E/F/G/H=36-361.
DR PDB; 6EBK; EM; 3.30 A; A/C/E/G=37-367.
DR PDB; 6EBL; EM; 3.00 A; A/C/E/G=37-367.
DR PDBsum; 1EXB; -.
DR PDBsum; 1QRQ; -.
DR PDBsum; 2A79; -.
DR PDBsum; 2R9R; -.
DR PDBsum; 3EAU; -.
DR PDBsum; 3EB3; -.
DR PDBsum; 3EB4; -.
DR PDBsum; 3LNM; -.
DR PDBsum; 3LUT; -.
DR PDBsum; 4JTA; -.
DR PDBsum; 4JTC; -.
DR PDBsum; 4JTD; -.
DR PDBsum; 5WIE; -.
DR PDBsum; 6CI1; -.
DR PDBsum; 6EBK; -.
DR PDBsum; 6EBL; -.
DR AlphaFoldDB; P62483; -.
DR SMR; P62483; -.
DR BioGRID; 248350; 7.
DR CORUM; P62483; -.
DR IntAct; P62483; 2.
DR MINT; P62483; -.
DR STRING; 10116.ENSRNOP00000015840; -.
DR iPTMnet; P62483; -.
DR PhosphoSitePlus; P62483; -.
DR PaxDb; P62483; -.
DR PRIDE; P62483; -.
DR ABCD; P62483; 3 sequenced antibodies.
DR GeneID; 29738; -.
DR KEGG; rno:29738; -.
DR UCSC; RGD:61828; rat.
DR CTD; 8514; -.
DR RGD; 61828; Kcnab2.
DR VEuPathDB; HostDB:ENSRNOG00000011550; -.
DR eggNOG; KOG1575; Eukaryota.
DR InParanoid; P62483; -.
DR OrthoDB; 1106773at2759; -.
DR PhylomeDB; P62483; -.
DR TreeFam; TF324563; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR EvolutionaryTrace; P62483; -.
DR PRO; PR:P62483; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000011550; Expressed in frontal cortex and 20 other tissues.
DR ExpressionAtlas; P62483; baseline and differential.
DR Genevisible; P62483; RN.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:UniProtKB.
DR GO; GO:0043194; C:axon initial segment; ISO:RGD.
DR GO; GO:0043679; C:axon terminus; ISO:RGD.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:RGD.
DR GO; GO:0043005; C:neuron projection; IDA:UniProtKB.
DR GO; GO:1990031; C:pinceau fiber; IDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:RGD.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:RGD.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
DR GO; GO:0070995; P:NADPH oxidation; IDA:UniProtKB.
DR GO; GO:0050905; P:neuromuscular process; ISO:RGD.
DR GO; GO:0098900; P:regulation of action potential; IBA:GO_Central.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; IMP:UniProtKB.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR InterPro; IPR005401; K_chnl_volt-dep_bsu_KCNAB2.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43150; PTHR43150; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR01579; KCNAB2CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cell membrane; Cell projection; Cytoplasm;
KW Cytoskeleton; Ion channel; Ion transport; Membrane; Methylation; NADP;
KW Oxidoreductase; Phosphoprotein; Potassium; Potassium transport;
KW Reference proteome; Synapse; Synaptosome; Transport; Voltage-gated channel.
FT CHAIN 1..367
FT /note="Voltage-gated potassium channel subunit beta-2"
FT /id="PRO_0000148748"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000305|PubMed:18672894"
FT BINDING 56..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC"
FT BINDING 85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581"
FT BINDING 188..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 243..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 262..264
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT BINDING 323..333
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|PubMed:16002581,
FT ECO:0007744|PDB:1EXB, ECO:0007744|PDB:1QRQ,
FT ECO:0007744|PDB:2A79, ECO:0007744|PDB:2R9R,
FT ECO:0007744|PDB:3EAU, ECO:0007744|PDB:3EB3,
FT ECO:0007744|PDB:3EB4, ECO:0007744|PDB:3LNM,
FT ECO:0007744|PDB:3LUT, ECO:0007744|PDB:4JTA,
FT ECO:0007744|PDB:4JTC, ECO:0007744|PDB:4JTD"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21357749,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21357749,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 28
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62482"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21357749"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13303"
FT MUTAGEN 9
FT /note="S->A: Impairs interaction with MAPRE1 and
FT association with microtubules."
FT /evidence="ECO:0000269|PubMed:21357749"
FT MUTAGEN 20
FT /note="S->A: No effect on interaction with MAPRE1 and
FT association with microtubules."
FT /evidence="ECO:0000269|PubMed:21357749"
FT MUTAGEN 31
FT /note="S->A: Impairs interaction with MAPRE1 and
FT association with microtubules."
FT /evidence="ECO:0000269|PubMed:21357749"
FT MUTAGEN 90
FT /note="Y->F: Abolishes enzyme activity, but has no effect
FT on NADPH binding."
FT /evidence="ECO:0000269|PubMed:18672894,
FT ECO:0000269|PubMed:21209188"
FT STRAND 38..42
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:3EAU"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 271..278
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 280..299
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 303..312
FT /evidence="ECO:0007829|PDB:3EAU"
FT STRAND 319..322
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:3EAU"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:3EAU"
SQ SEQUENCE 367 AA; 41021 MW; 5303FD1411B324FC CRC64;
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG
MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE IDSILGNKPY
SKKDYRS
