KCAB1_RAT
ID KCAB1_RAT Reviewed; 401 AA.
AC P63144; P97380; Q5FWS9; Q61763; Q63277;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Voltage-gated potassium channel subunit beta-1;
DE EC=1.1.1.- {ECO:0000269|PubMed:18222921};
DE AltName: Full=K(+) channel subunit beta-1;
DE AltName: Full=Kv-beta-1;
GN Name=Kcnab1; Synonyms=Kvb1;
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], FUNCTION, TISSUE SPECIFICITY, AND DOMAIN.
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP INTERACTION WITH KCNA1; KCNA2; KCNA4; KCNA6 AND KCNAB2, 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 [4]
RP FUNCTION, SUBUNIT, AND INTERACTION WITH KCNA1; GNB1 AND GNG2.
RX PubMed=10064591; DOI=10.1093/emboj/18.5.1245;
RA Jing J., Chikvashvili D., Singer-Lahat D., Thornhill W.B., Reuveny E.,
RA Lotan I.;
RT "Fast inactivation of a brain K+ channel composed of Kv1.1 and Kvbeta1.1
RT subunits modulated by G protein beta gamma subunits.";
RL EMBO J. 18:1245-1256(1999).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=10650996; DOI=10.1007/s004249900139;
RA Singer-Lahat D., Dascal N., Lotan I.;
RT "Modal behavior of the Kv1.1 channel conferred by the Kvbeta1.1 subunit and
RT its regulation by dephosphorylation of Kv1.1.";
RL Pflugers Arch. 439:18-26(1999).
RN [6]
RP INTERACTION WITH SQSTM1.
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 [7]
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 [8]
RP FUNCTION, INTERACTION WITH LGI1; KCNA1 AND KCNA4, SUBCELLULAR LOCATION,
RP SUBUNIT, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16504945; DOI=10.1016/j.neuron.2006.01.033;
RA Schulte U., Thumfart J.-O., Kloecker N., Sailer C.A., Bildl W.,
RA Biniossek M., Dehn D., Deller T., Eble S., Abbass K., Wangler T.,
RA Knaus H.-G., Fakler B.;
RT "The epilepsy-linked Lgi1 protein assembles into presynaptic Kv1 channels
RT and inhibits inactivation by Kvbeta1.";
RL Neuron 49:697-706(2006).
RN [9]
RP FUNCTION, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LYS-152.
RX PubMed=18222921; DOI=10.1074/jbc.m709304200;
RA Pan Y., Weng J., Cao Y., Bhosle R.C., Zhou M.;
RT "Functional coupling between the Kv1.1 channel and aldoketoreductase
RT Kvbeta1.";
RL J. Biol. Chem. 283:8634-8642(2008).
RN [10]
RP INTERACTION WITH KCNA2.
RX PubMed=19713757; DOI=10.4161/chan.3.5.9558;
RA Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.;
RT "The molecular basis for the actions of Kvbeta1.2 on the opening and
RT closing of the Kv1.2 delayed rectifier channel.";
RL Channels 3:314-322(2009).
RN [11]
RP FUNCTION, AND DOMAIN.
RX PubMed=21436029; DOI=10.1073/pnas.1100316108;
RA Pan Y., Weng J., Levin E.J., Zhou M.;
RT "Oxidation of NADPH on Kvbeta1 inhibits ball-and-chain type inactivation by
RT restraining the chain.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:5885-5890(2011).
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits. Modulates action
CC potentials via its effect on the pore-forming alpha subunits
CC (Probable). Promotes expression of the pore-forming alpha subunits at
CC the cell membrane, and thereby increases channel activity (By
CC similarity). Mediates closure of delayed rectifier potassium channels
CC by physically obstructing the pore via its N-terminal domain and
CC increases the speed of channel closure for other family members
CC (PubMed:8183366, PubMed:15618540, PubMed:18222921). Promotes the
CC closure of KCNA1, KCNA2 and KCNA5 channels (PubMed:10064591,
CC PubMed:10650996, PubMed:16504945). Accelerates KCNA4 channel closure
CC (PubMed:8183366). Accelerates the closure of heteromeric channels
CC formed by KCNA1 and KCNA4 (PubMed:16504945). Accelerates the closure of
CC heteromeric channels formed by KCNA2, KCNA5 and KCNA6
CC (PubMed:15618540). Enhances KCNB1 and KCNB2 channel activity (By
CC similarity). Binds NADPH; this is required for efficient down-
CC regulation of potassium channel activity. Has NADPH-dependent
CC aldoketoreductase activity (PubMed:18222921). Oxidation of the bound
CC NADPH strongly decreases N-type inactivation of potassium channel
CC activity (PubMed:18222921, PubMed:21436029).
CC {ECO:0000250|UniProtKB:P63143, ECO:0000269|PubMed:10064591,
CC ECO:0000269|PubMed:10650996, ECO:0000269|PubMed:15618540,
CC ECO:0000269|PubMed:16504945, ECO:0000269|PubMed:18222921,
CC ECO:0000269|PubMed:21436029, ECO:0000269|PubMed:8183366, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer (PubMed:18222921). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer
CC (Probable). Identified in potassium channel complexes containing KCNA1,
CC KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (PubMed:9334400,
CC PubMed:16504945). Interacts with KCNA1 (PubMed:10064591). Interacts
CC with the dimer formed by GNB1 and GNG2; this enhances KCNA1 binding
CC (PubMed:10064591). Interacts with KCNA4 (By similarity). Interacts with
CC KCNB2 and KCNA5 (By similarity). Interacts with SQSTM1
CC (PubMed:10477520). Part of a complex containing KCNA1, KCNA4 and LGI1;
CC interaction with LGI1 inhibits down-regulation of KCNA1 channel
CC activity (PubMed:16504945). {ECO:0000250|UniProtKB:P63143,
CC ECO:0000250|UniProtKB:Q14722, ECO:0000269|PubMed:10064591,
CC ECO:0000269|PubMed:10477520, ECO:0000269|PubMed:16504945,
CC ECO:0000269|PubMed:18222921, ECO:0000269|PubMed:9334400, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14722}.
CC Membrane {ECO:0000269|PubMed:15618540}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:16504945}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to the
CC cytoplasmic side of the cell membrane via its interaction with pore-
CC forming potassium channel alpha subunits.
CC {ECO:0000250|UniProtKB:Q14722}.
CC -!- TISSUE SPECIFICITY: Detected in brain (PubMed:9334400). Detected in
CC hippocampus, in the middle third of the molecular layer of the dentate
CC gyrus and in the mossy fiber zone of the CA3 region (PubMed:9334400).
CC Detected in globus pallidus and pars reticulata of the substantia nigra
CC (at protein level) (PubMed:9334400). Specifically expressed in the
CC nervous system (PubMed:8183366). Detected in mesenteric arteries
CC (PubMed:15618540). {ECO:0000269|PubMed:15618540,
CC ECO:0000269|PubMed:8183366, ECO:0000269|PubMed:9334400}.
CC -!- DOMAIN: The N-terminal domain of the beta subunit mediates closure of
CC delayed rectifier potassium channels by physically obstructing the
CC pore. {ECO:0000269|PubMed:18222921, ECO:0000269|PubMed:21436029,
CC ECO:0000269|PubMed:8183366}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; X70662; CAA50000.1; -; mRNA.
DR EMBL; BC089219; AAH89219.1; -; mRNA.
DR RefSeq; NP_058999.1; NM_017303.2.
DR AlphaFoldDB; P63144; -.
DR SMR; P63144; -.
DR BioGRID; 248349; 2.
DR CORUM; P63144; -.
DR IntAct; P63144; 1.
DR MINT; P63144; -.
DR STRING; 10116.ENSRNOP00000051084; -.
DR TCDB; 8.A.5.1.3; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR PhosphoSitePlus; P63144; -.
DR PaxDb; P63144; -.
DR PRIDE; P63144; -.
DR ABCD; P63144; 3 sequenced antibodies.
DR Ensembl; ENSRNOT00000077973; ENSRNOP00000072289; ENSRNOG00000056697.
DR GeneID; 29737; -.
DR KEGG; rno:29737; -.
DR UCSC; RGD:61827; rat.
DR CTD; 7881; -.
DR RGD; 61827; Kcnab1.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000156760; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; P63144; -.
DR OMA; VDLWQVH; -.
DR OrthoDB; 1106773at2759; -.
DR PhylomeDB; P63144; -.
DR TreeFam; TF324563; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:P63144; -.
DR Proteomes; UP000002494; Chromosome 2.
DR Bgee; ENSRNOG00000056697; Expressed in cerebellum and 18 other tissues.
DR Genevisible; P63144; RN.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:RGD.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0043025; C:neuronal cell body; IDA:RGD.
DR GO; GO:0043204; C:perikaryon; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:1990635; C:proximal dendrite; IDA:RGD.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:RGD.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; IDA:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO: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:0007420; P:brain development; IEP:RGD.
DR GO; GO:0060539; P:diaphragm development; IEP:RGD.
DR GO; GO:0007507; P:heart development; IEP:RGD.
DR GO; GO:0007611; P:learning or memory; ISO:RGD.
DR GO; GO:0045445; P:myoblast differentiation; IEP:RGD.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:RGD.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0007519; P:skeletal muscle tissue development; IEP:RGD.
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; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
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; PR01578; KCNAB1CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Ion channel; Ion transport; Membrane; NADP;
KW Oxidoreductase; Potassium; Potassium transport; Reference proteome;
KW Transport; Voltage-gated channel.
FT CHAIN 1..401
FT /note="Voltage-gated potassium channel subunit beta-1"
FT /id="PRO_0000148743"
FT ACT_SITE 124
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 90..91
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 97
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 119
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 124
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 222..223
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 277..282
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 288
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 357..363
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT MUTAGEN 152
FT /note="K->M: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:18222921"
SQ SEQUENCE 401 AA; 44710 MW; F9F17404DF35FDA1 CRC64;
MQVSIACTEH NLKSRNGEDR LLSKQSSTAP NVVNAARAKF RTVAIIARSL GTFTPQHHIS
LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD EVAERLMTIA YESGVNLFDT
AEVYAAGKAE VILGSIIKKK GWRRSSLVIT TKLYWGGKAE TERGLSRKHI IEGLKGSLQR
LQLEYVDVVF ANRPDSNTPM EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN
MIPPVCEQAE YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAS
LKCYQWLKER IVSEEGRKQQ NKLKDLSPIA ERLGCTLPQL AVAWCLRNEG VSSVLLGSST
PEQLIENLGA IQVLPKMTSH VVNEIDNILR NKPYSKKDYR S
