KCAB1_MOUSE
ID KCAB1_MOUSE Reviewed; 401 AA.
AC P63143; P97380; Q61763; Q63277; Q91WM5;
DT 13-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Voltage-gated potassium channel subunit beta-1;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P63144};
DE AltName: Full=K(+) channel subunit beta-1;
DE AltName: Full=Kv-beta-1;
GN Name=Kcnab1; Synonyms=Kvb1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Hippocampus;
RX PubMed=9468385;
RX DOI=10.1002/(sici)1097-4695(19980205)34:2<135::aid-neu4>3.0.co;2-3;
RA Butler D.M., Ono J.K., Chang T., McCaman R.E., Barish M.E.;
RT "Mouse brain potassium channel beta1 subunit mRNA: cloning and distribution
RT during development.";
RL J. Neurobiol. 34:135-150(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=8824288; DOI=10.1074/jbc.271.42.26341;
RA Fink M., Duprat F., Lesage F., Heurteaux C., Romey G., Barhanin J.,
RA Lazdunski M.;
RT "A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK)
RT expression.";
RL J. Biol. Chem. 271:26341-26348(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RA Metzler M., Repp R., Kreuder J., Borkhardt A., Koschinski A., Lampert F.,
RA Dreyer F., Repp H.;
RT "Expression of a potassium channel beta-subunit in mouse fibroblasts.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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 [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=10454353;
RA Giese K.P., Storm J.F., Reuter D., Fedorov N.B., Shao L.R., Leicher T.,
RA Pongs O., Silva A.J.;
RT "Reduced K+ channel inactivation, spike broadening, and after-
RT hyperpolarization in Kvbeta1.1-deficient mice with impaired learning.";
RL Learn. Memory 5:257-273(1998).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=14511342; DOI=10.1046/j.1460-9568.2003.02889.x;
RA Need A.C., Irvine E.E., Giese K.P.;
RT "Learning and memory impairments in Kv beta 1.1-null mutants are rescued by
RT environmental enrichment or ageing.";
RL Eur. J. Neurosci. 18:1640-1644(2003).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=15530391; DOI=10.1016/j.cub.2004.10.021;
RA Murphy G.G., Fedorov N.B., Giese K.P., Ohno M., Friedman E., Chen R.,
RA Silva A.J.;
RT "Increased neuronal excitability, synaptic plasticity, and learning in aged
RT Kvbeta1.1 knockout mice.";
RL Curr. Biol. 14:1907-1915(2004).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits
CC (PubMed:10454353). Modulates action potentials via its effect on the
CC pore-forming alpha subunits (PubMed:10454353). Promotes expression of
CC the pore-forming alpha subunits at the cell membrane, and thereby
CC increases channel activity (PubMed:8824288). Mediates closure of
CC delayed rectifier potassium channels by physically obstructing the pore
CC via its N-terminal domain and increases the speed of channel closure
CC for other family members (By similarity). Promotes the closure of
CC KCNA1, KCNA2 and KCNA5 channels (By similarity). Accelerates KCNA4
CC channel closure (By similarity). Accelerates the closure of heteromeric
CC channels formed by KCNA1 and KCNA4 (By similarity). Accelerates the
CC closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By
CC similarity). Enhances KCNB1 and KCNB2 channel activity
CC (PubMed:8824288). Binds NADPH; this is required for efficient down-
CC regulation of potassium channel activity (By similarity). Has NADPH-
CC dependent aldoketoreductase activity (By similarity). Oxidation of the
CC bound NADPH strongly decreases N-type inactivation of potassium channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P63144,
CC ECO:0000250|UniProtKB:Q14722, ECO:0000269|PubMed:10454353,
CC ECO:0000269|PubMed:8824288}.
CC -!- SUBUNIT: Homotetramer (By similarity). 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 (By similarity).
CC Interacts with KCNA1 (By similarity). Interacts with the dimer formed
CC by GNB1 and GNG2; this enhances KCNA1 binding (By similarity).
CC Interacts with KCNA4 (By similarity). Interacts with KCNB2 and KCNA5
CC (PubMed:8824288). Interacts with SQSTM1 (By similarity). Part of a
CC complex containing KCNA1, KCNA4 and LGI1; interaction with LGI1
CC inhibits down-regulation of KCNA1 channel activity (By similarity).
CC {ECO:0000250|UniProtKB:P63144, ECO:0000250|UniProtKB:Q14722,
CC ECO:0000269|PubMed:8824288, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14722}.
CC Membrane {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P63144}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P63144}. Cell membrane
CC {ECO:0000250|UniProtKB:Q14722}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q14722}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:Q14722}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. {ECO:0000250|UniProtKB:Q14722}.
CC -!- TISSUE SPECIFICITY: Detected in brain, in hippocampus and striatum (at
CC protein level) (PubMed:10454353). Predominantly expressed in brain. No
CC expression found in heart, skeletal muscle or kidney. In the late
CC embryonic and early neonatal brain, highly expressed in hippocampus,
CC cerebral cortex, caudate putamen, colliculus and cerebellum.
CC {ECO:0000269|PubMed:10454353, ECO:0000269|PubMed:9468385}.
CC -!- DEVELOPMENTAL STAGE: Expressed from embryonic day 16. Expressed
CC throughout embryonic development, in neonate and in adult.
CC {ECO:0000269|PubMed:9468385}.
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:0000250|UniProtKB:P63144}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show subtle defects in learning
CC (PubMed:10454353). Such learning impairments are not detectable in
CC older mice and are not observed when mice are kept in a stimulating
CC environment (PubMed:14511342, PubMed:15530391).
CC {ECO:0000269|PubMed:10454353, ECO:0000269|PubMed:14511342,
CC ECO:0000269|PubMed:15530391}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; AF033003; AAB87085.1; -; mRNA.
DR EMBL; U65591; AAB37262.1; -; mRNA.
DR EMBL; X97281; CAA65936.1; -; mRNA.
DR EMBL; AK138467; BAE23670.1; -; mRNA.
DR EMBL; CH466547; EDL15543.1; -; Genomic_DNA.
DR EMBL; BC014701; AAH14701.1; -; mRNA.
DR CCDS; CCDS38447.1; -.
DR RefSeq; NP_034727.3; NM_010597.4.
DR AlphaFoldDB; P63143; -.
DR SMR; P63143; -.
DR BioGRID; 200883; 8.
DR IntAct; P63143; 4.
DR MINT; P63143; -.
DR STRING; 10090.ENSMUSP00000047480; -.
DR iPTMnet; P63143; -.
DR PhosphoSitePlus; P63143; -.
DR SwissPalm; P63143; -.
DR jPOST; P63143; -.
DR MaxQB; P63143; -.
DR PaxDb; P63143; -.
DR PeptideAtlas; P63143; -.
DR PRIDE; P63143; -.
DR ProteomicsDB; 301755; -.
DR ABCD; P63143; 3 sequenced antibodies.
DR Antibodypedia; 18386; 419 antibodies from 33 providers.
DR DNASU; 16497; -.
DR Ensembl; ENSMUST00000049230; ENSMUSP00000047480; ENSMUSG00000027827.
DR GeneID; 16497; -.
DR KEGG; mmu:16497; -.
DR UCSC; uc008pkj.2; mouse.
DR CTD; 7881; -.
DR MGI; MGI:109155; Kcnab1.
DR VEuPathDB; HostDB:ENSMUSG00000027827; -.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000156760; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; P63143; -.
DR OMA; VDLWQVH; -.
DR OrthoDB; 1106773at2759; -.
DR PhylomeDB; P63143; -.
DR TreeFam; TF324563; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16497; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Kcnab1; mouse.
DR PRO; PR:P63143; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; P63143; protein.
DR Bgee; ENSMUSG00000027827; Expressed in caudate-putamen and 172 other tissues.
DR ExpressionAtlas; P63143; baseline and differential.
DR Genevisible; P63143; MM.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; ISO:MGI.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; ISO:MGI.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0043204; C:perikaryon; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0034705; C:potassium channel complex; ISS:UniProtKB.
DR GO; GO:1990635; C:proximal dendrite; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0007611; P:learning or memory; IMP:MGI.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISO:MGI.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IMP:MGI.
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_0000148740"
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 CONFLICT 28
FT /note="N -> T (in Ref. 1; AAB87085 and 3; CAA65936)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="H -> D (in Ref. 2; AAB37262)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="K -> N (in Ref. 3; CAA65936)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="A -> S (in Ref. 2; AAB37262)"
FT /evidence="ECO:0000305"
FT CONFLICT 282
FT /note="C -> Y (in Ref. 2; AAB37262)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="I -> F (in Ref. 2; AAB37262)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="E -> D (in Ref. 2; AAB37262)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 401 AA; 44723 MW; 09F7860DCD3728B6 CRC64;
MQVSIACTEH NLKSRNGEDR LLSKQSSNAP 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
