KCNAS_DROME
ID KCNAS_DROME Reviewed; 655 AA.
AC P08510; A4V4Q2; B6IDJ2; M9MSC0; M9NEM4; M9PF21; P08511; P08512; P08513;
AC Q24277; Q24521; Q7KUW5; Q8IQY9; Q8MT41; Q9VWZ5; Q9VWZ9; Q9VX00;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 3.
DT 03-AUG-2022, entry version 232.
DE RecName: Full=Potassium voltage-gated channel protein Shaker;
DE AltName: Full=Protein minisleep;
GN Name=Sh; Synonyms=mns; ORFNames=CG12348;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA), AND RNA EDITING OF POSITIONS
RP 464; 489 AND 491.
RX PubMed=2441471; DOI=10.1126/science.2441471;
RA Tempel B.L., Papazian D.M., Schwarz T.L., Jan Y.N., Jan L.Y.;
RT "Sequence of a probable potassium channel component encoded at Shaker locus
RT of Drosophila.";
RL Science 237:770-775(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM DELTA).
RC STRAIN=Canton-S, and Oregon-R;
RX PubMed=16453805; DOI=10.1002/j.1460-2075.1987.tb02665.x;
RA Baumann A., Krah-Jentgens I., Mueller R., Mueller-Holtkamp F., Seidel R.,
RA Kecskemethy N., Casal J., Ferrus A., Pongs O.;
RT "Molecular organization of the maternal effect region of the Shaker complex
RT of Drosophila: characterization of an I(A) channel transcript with homology
RT to vertebrate Na(+) channel.";
RL EMBO J. 6:3419-3429(1987).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA; DELTA AND EPSILON), AND
RP RNA EDITING OF POSITIONS 464; 489 AND 491.
RC STRAIN=Canton-S; TISSUE=Larva;
RX PubMed=2456921; DOI=10.1002/j.1460-2075.1988.tb02917.x;
RA Pongs O., Kecskemethy N., Mueller R., Krah-Jentgens I., Baumann A.,
RA Kiltz H.H., Canal I., Llamazares S., Ferrus A.;
RT "Shaker encodes a family of putative potassium channel proteins in the
RT nervous system of Drosophila.";
RL EMBO J. 7:1087-1096(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND E).
RX PubMed=2448635; DOI=10.1038/331137a0;
RA Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.;
RT "Multiple potassium-channel components are produced by alternative splicing
RT at the Shaker locus in Drosophila.";
RL Nature 331:137-142(1988).
RN [5]
RP ERRATUM OF PUBMED:2448635.
RA Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.;
RL Nature 332:740-740(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [7]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D), AND RNA EDITING OF
RP POSITION 360.
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM D).
RC STRAIN=Berkeley;
RA Carlson J., Booth B., Frise E., Park S., Wan K., Yu C., Celniker S.;
RL Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-257 (ISOFORM BETA).
RC TISSUE=Larva;
RX PubMed=2440582; DOI=10.1016/0092-8674(87)90494-6;
RA Kamb A., Iverson L.E., Tanouye M.A.;
RT "Molecular characterization of Shaker, a Drosophila gene that encodes a
RT potassium channel.";
RL Cell 50:405-413(1987).
RN [11]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 450-534.
RC STRAIN=H4;
RX PubMed=3272175; DOI=10.1016/0896-6273(88)90192-4;
RA Kamb A., Tseng-Crank J., Tanouye M.A.;
RT "Multiple products of the Drosophila Shaker gene may contribute to
RT potassium channel diversity.";
RL Neuron 1:421-430(1988).
RN [12]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2448636; DOI=10.1038/331143a0;
RA Timpe L.C., Schwarz T.L., Tempel B.L., Papazian D.M., Jan Y.N., Jan L.Y.;
RT "Expression of functional potassium channels from Shaker cDNA in Xenopus
RT oocytes.";
RL Nature 331:143-145(1988).
RN [13]
RP RNA EDITING.
RX PubMed=12907802; DOI=10.1126/science.1086763;
RA Hoopengardner B., Bhalla T., Staber C., Reenan R.;
RT "Nervous system targets of RNA editing identified by comparative
RT genomics.";
RL Science 301:832-836(2003).
RN [14]
RP FUNCTION, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF THR-248.
RX PubMed=15858564; DOI=10.1038/nature03486;
RA Cirelli C., Bushey D., Hill S., Huber R., Kreber R., Ganetzky B.,
RA Tononi G.;
RT "Reduced sleep in Drosophila Shaker mutants.";
RL Nature 434:1087-1092(2005).
RN [15]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-259 AND ASN-263, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=Oregon-R; TISSUE=Head;
RX PubMed=17893096; DOI=10.1093/glycob/cwm097;
RA Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,
RA Panin V.;
RT "Identification of N-glycosylated proteins from the central nervous system
RT of Drosophila melanogaster.";
RL Glycobiology 17:1388-1403(2007).
RN [16]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=22292044; DOI=10.1371/journal.pone.0030799;
RA Houot B., Fraichard S., Greenspan R.J., Ferveur J.F.;
RT "Genes involved in sex pheromone discrimination in Drosophila melanogaster
RT and their background-dependent effect.";
RL PLoS ONE 7:e30799-e30799(2012).
RN [17]
RP STRUCTURE BY NMR OF 378-397.
RX PubMed=12023222; DOI=10.1016/s0006-3495(02)75640-3;
RA Ohlenschlaeger O., Hojo H., Ramachandran R., Goerlach M., Haris P.I.;
RT "Three-dimensional structure of the S4-S5 segment of the Shaker potassium
RT channel.";
RL Biophys. J. 82:2995-3002(2002).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes. The channel alternates
CC between opened and closed conformations in response to the voltage
CC difference across the membrane. Forms rapidly inactivating tetrameric
CC potassium-selective channels through which potassium ions pass in
CC accordance with their electrochemical gradient and may contribute to A-
CC type currents (PubMed:2448636). Plays a role in the regulation of sleep
CC need or efficiency (PubMed:15858564). Plays a role in sexual behavior,
CC where it is important for male sex discrimination (PubMed:22292044).
CC {ECO:0000269|PubMed:15858564, ECO:0000269|PubMed:22292044,
CC ECO:0000269|PubMed:2448636}.
CC -!- SUBUNIT: Homotetramer or heterotetramer of potassium channel proteins.
CC {ECO:0000305}.
CC -!- INTERACTION:
CC P08510; P31007: dlg1; NbExp=3; IntAct=EBI-85074, EBI-389374;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2448636};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Name=E;
CC IsoId=P08510-1; Sequence=Displayed;
CC Name=Alpha; Synonyms=B, Adult;
CC IsoId=P08510-2; Sequence=VSP_017889, VSP_000959;
CC Name=Beta; Synonyms=C, I, J, Late population;
CC IsoId=P08510-3; Sequence=VSP_000954;
CC Name=Delta; Synonyms=Larval, A, H;
CC IsoId=P08510-5; Sequence=VSP_000956, VSP_000957, VSP_000958;
CC Name=Epsilon; Synonyms=Larval, F;
CC IsoId=P08510-6; Sequence=VSP_000957, VSP_000958;
CC Name=D;
CC IsoId=P08510-7; Sequence=VSP_000956, VSP_017889, VSP_000959;
CC Name=N;
CC IsoId=P08510-8; Sequence=VSP_054719;
CC Name=L;
CC IsoId=P08510-9; Sequence=VSP_000954, VSP_054720;
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC -!- RNA EDITING: Modified_positions=178 {ECO:0000269|PubMed:12907802}, 360
CC {ECO:0000269|PubMed:12537569, ECO:0000269|PubMed:12907802}, 464
CC {ECO:0000269|PubMed:12907802, ECO:0000269|PubMed:2441471,
CC ECO:0000269|PubMed:2456921}, 489 {ECO:0000269|PubMed:12907802,
CC ECO:0000269|PubMed:2441471, ECO:0000269|PubMed:2456921}, 491
CC {ECO:0000269|PubMed:12907802, ECO:0000269|PubMed:2441471,
CC ECO:0000269|PubMed:2456921}; Note=Partially edited.;
CC -!- DISRUPTION PHENOTYPE: Reduced sleep (PubMed:15858564). Flies sleep for
CC one-third of the wild-type amount (PubMed:15858564). They perform
CC normally in a number of tasks, have preserved sleep homeostasis, but
CC are not impaired by sleep deprivation (PubMed:15858564). They also have
CC a reduced lifespan (PubMed:15858564). Males are able to discriminate
CC between males and females during courtship but their courtship of
CC females is reduced, suggesting that their perception and/or response to
CC wild-type female pheromones is decreased (PubMed:22292044). RNAi-
CC mediated knockdown in all neurons or specifically in the mushroom
CC bodies of adult males, impairs their ability to discriminate between
CC males and females (PubMed:22292044). However, knockdown in various
CC chemosensory peripheral neurons has no effect on male sex
CC discrimination (PubMed:22292044). {ECO:0000269|PubMed:15858564,
CC ECO:0000269|PubMed:22292044}.
CC -!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
CC 1.A.1.2) subfamily. Shaker sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA70217.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M17211; AAA28417.1; -; mRNA.
DR EMBL; X06184; CAA29549.1; -; mRNA.
DR EMBL; X07131; CAA30143.1; -; mRNA.
DR EMBL; X07132; CAA30144.1; -; mRNA.
DR EMBL; X07133; CAA30145.1; -; mRNA.
DR EMBL; X07134; CAA30146.1; -; mRNA.
DR EMBL; X06742; CAA29917.1; -; mRNA.
DR EMBL; AE014298; AAF48785.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF48786.3; -; Genomic_DNA.
DR EMBL; AE014298; AAF48790.2; -; Genomic_DNA.
DR EMBL; AE014298; AAN09451.1; -; Genomic_DNA.
DR EMBL; AE014298; AAN09452.1; -; Genomic_DNA.
DR EMBL; AE014298; AAS65395.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65396.1; -; Genomic_DNA.
DR EMBL; AE014298; ADV37750.1; -; Genomic_DNA.
DR EMBL; AE014298; AFH07440.1; -; Genomic_DNA.
DR EMBL; AE014298; AGB95507.1; -; Genomic_DNA.
DR EMBL; AY118398; AAM48427.1; -; mRNA.
DR EMBL; BT050432; ACJ13139.1; -; mRNA.
DR EMBL; M17155; AAA70217.1; ALT_FRAME; mRNA.
DR EMBL; X78908; CAA55519.1; -; Genomic_DNA.
DR PIR; A27159; A27159.
DR PIR; JH0193; JH0193.
DR PIR; S00480; S00480.
DR PIR; S02284; S02284.
DR RefSeq; NP_001162788.1; NM_001169317.1. [P08510-5]
DR RefSeq; NP_001188668.1; NM_001201739.2. [P08510-3]
DR RefSeq; NP_001245727.1; NM_001258798.2. [P08510-9]
DR RefSeq; NP_001259665.2; NM_001272736.2. [P08510-2]
DR RefSeq; NP_523393.3; NM_078669.5. [P08510-2]
DR RefSeq; NP_728120.1; NM_167592.4. [P08510-7]
DR RefSeq; NP_728122.1; NM_167594.4. [P08510-3]
DR RefSeq; NP_728123.1; NM_167595.4. [P08510-1]
DR RefSeq; NP_728124.1; NM_167596.5. [P08510-5]
DR RefSeq; NP_996497.1; NM_206774.2. [P08510-6]
DR RefSeq; NP_996498.2; NM_206775.5. [P08510-3]
DR PDB; 1HO2; NMR; -; A=378-397.
DR PDB; 1HO7; NMR; -; A=378-397.
DR PDB; 7SIP; EM; 3.00 A; A/B/C/D=47-655.
DR PDB; 7SJ1; EM; 2.90 A; A/B/C/D=47-655.
DR PDBsum; 1HO2; -.
DR PDBsum; 1HO7; -.
DR PDBsum; 7SIP; -.
DR PDBsum; 7SJ1; -.
DR AlphaFoldDB; P08510; -.
DR BMRB; P08510; -.
DR SMR; P08510; -.
DR BioGRID; 59101; 16.
DR DIP; DIP-41151N; -.
DR IntAct; P08510; 5.
DR MINT; P08510; -.
DR STRING; 7227.FBpp0088599; -.
DR TCDB; 1.A.1.2.6; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P08510; 2 sites.
DR iPTMnet; P08510; -.
DR MetOSite; P08510; -.
DR PaxDb; P08510; -.
DR PRIDE; P08510; -.
DR EnsemblMetazoa; FBtr0089657; FBpp0088599; FBgn0003380. [P08510-1]
DR EnsemblMetazoa; FBtr0089658; FBpp0088600; FBgn0003380. [P08510-2]
DR EnsemblMetazoa; FBtr0089659; FBpp0088601; FBgn0003380. [P08510-5]
DR EnsemblMetazoa; FBtr0089660; FBpp0088602; FBgn0003380. [P08510-7]
DR EnsemblMetazoa; FBtr0089661; FBpp0088603; FBgn0003380. [P08510-3]
DR EnsemblMetazoa; FBtr0089663; FBpp0088605; FBgn0003380. [P08510-6]
DR EnsemblMetazoa; FBtr0301955; FBpp0291167; FBgn0003380. [P08510-5]
DR EnsemblMetazoa; FBtr0302902; FBpp0292033; FBgn0003380. [P08510-3]
DR EnsemblMetazoa; FBtr0302903; FBpp0292034; FBgn0003380. [P08510-3]
DR EnsemblMetazoa; FBtr0308200; FBpp0300520; FBgn0003380. [P08510-9]
DR EnsemblMetazoa; FBtr0346703; FBpp0312316; FBgn0003380. [P08510-2]
DR GeneID; 32780; -.
DR KEGG; dme:Dmel_CG12348; -.
DR UCSC; CG12348-RG; d. melanogaster.
DR CTD; 32780; -.
DR FlyBase; FBgn0003380; Sh.
DR VEuPathDB; VectorBase:FBgn0003380; -.
DR eggNOG; KOG1545; Eukaryota.
DR GeneTree; ENSGT00940000170670; -.
DR InParanoid; P08510; -.
DR OMA; HPLDYDP; -.
DR PhylomeDB; P08510; -.
DR Reactome; R-DME-1296072; Voltage gated Potassium channels.
DR SignaLink; P08510; -.
DR BioGRID-ORCS; 32780; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Sh; fly.
DR EvolutionaryTrace; P08510; -.
DR GenomeRNAi; 32780; -.
DR PRO; PR:P08510; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0003380; Expressed in brain and 15 other tissues.
DR ExpressionAtlas; P08510; baseline and differential.
DR Genevisible; P08510; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IPI:FlyBase.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022843; F:voltage-gated cation channel activity; IDA:FlyBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0001508; P:action potential; IMP:FlyBase.
DR GO; GO:0048675; P:axon extension; IMP:FlyBase.
DR GO; GO:0048150; P:behavioral response to ether; NAS:FlyBase.
DR GO; GO:1903351; P:cellular response to dopamine; IMP:FlyBase.
DR GO; GO:0007619; P:courtship behavior; TAS:FlyBase.
DR GO; GO:0009584; P:detection of visible light; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0007611; P:learning or memory; NAS:FlyBase.
DR GO; GO:0048047; P:mating behavior, sex discrimination; IDA:FlyBase.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0045838; P:positive regulation of membrane potential; IMP:FlyBase.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; TAS:FlyBase.
DR GO; GO:0007637; P:proboscis extension reflex; IMP:FlyBase.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0045187; P:regulation of circadian sleep/wake cycle, sleep; IMP:FlyBase.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0060025; P:regulation of synaptic activity; IMP:FlyBase.
DR GO; GO:0050909; P:sensory perception of taste; NAS:FlyBase.
DR GO; GO:0030431; P:sleep; IMP:FlyBase.
DR DisProt; DP01495; -.
DR Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003972; K_chnl_volt-dep_Kv1.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01496; SHAKERCHANEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Behavior; Cell membrane; Glycoprotein;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; RNA editing; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..655
FT /note="Potassium voltage-gated channel protein Shaker"
FT /id="PRO_0000053963"
FT TOPO_DOM 1..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 225..246
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 247..278
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 279..300
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 301..311
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 312..332
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 333..357
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 358..378
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 379..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 394..415
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 416..429
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 430..441
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 442..449
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 450..456
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 457..485
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 486..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..188
FT /note="Tetramerization domain"
FT /evidence="ECO:0000250|UniProtKB:P10499"
FT REGION 1..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 380..393
FT /note="S4-S5 linker"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 515..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 442..447
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT COMPBIAS 11..49
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 259
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT CARBOHYD 263
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17893096"
FT VAR_SEQ 1..61
FT /note="MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQL
FT QRNSLDGYG -> MTMWQSGGMGGHGSQNNPWMKLMGIVHKERRHTENVQSQSGSNERN
FT LNQ (in isoform Beta and isoform L)"
FT /evidence="ECO:0000303|PubMed:2440582,
FT ECO:0000303|PubMed:2448635, ECO:0000303|PubMed:2456921"
FT /id="VSP_000954"
FT VAR_SEQ 1..61
FT /note="MAAVAGLYGLGEDRQHRKKQQQQQQHQKEQLEQKEEQKKIAERKLQLREQQL
FT QRNSLDGYG -> MAHITTTHGSLSQATR (in isoform Delta and isoform
FT D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:16453805, ECO:0000303|PubMed:2456921,
FT ECO:0000303|Ref.9"
FT /id="VSP_000956"
FT VAR_SEQ 349
FT /note="D -> V (in isoform Delta and isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:16453805,
FT ECO:0000303|PubMed:2456921"
FT /id="VSP_000957"
FT VAR_SEQ 350..655
FT /note="Missing (in isoform Delta and isoform Epsilon)"
FT /evidence="ECO:0000303|PubMed:16453805,
FT ECO:0000303|PubMed:2456921"
FT /id="VSP_000958"
FT VAR_SEQ 407..655
FT /note="VVLFSSAVYFAEAGSENSFFKSIPDAFWWAVVTMTTVGYGDMTPVGVWGKIV
FT GSLCAIAGVLTIALPVPVIVSNFNYFYHRETDQEEMQSQNFNHVTSCPYLPGTLGQHMK
FT KSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGAQQQQQQPVASSLSMSIDKQ
FT LQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQQQQSHTINASAAAATSGSG
FT SSGLTMRHNNALAVSIETDV -> KFHTVNKKKKNNIPHLLIDLRVLFKQHQKQKRNTA
FT KRLRPSRQTYPRYPAPSKDIFSTTSHCPKVLIHILTVNRSKTTYNYSGIVQRSRIKTTT
FT KDTYI (in isoform N)"
FT /evidence="ECO:0000305"
FT /id="VSP_054719"
FT VAR_SEQ 453..463
FT /note="VWGKIVGSLCA -> FWGKIVGSLCV (in isoform Alpha and
FT isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2441471, ECO:0000303|PubMed:2448635,
FT ECO:0000303|PubMed:2456921, ECO:0000303|Ref.9"
FT /id="VSP_017889"
FT VAR_SEQ 506..655
FT /note="PYLPGTLGQHMKKSSLSESSSDMMDLDDGVESTPGLTETHPGRSAVAPFLGA
FT QQQQQQPVASSLSMSIDKQLQHPLQQLTQTQLYQQQQQQQQQQQNGFKQQQQQTQQQLQ
FT QQQSHTINASAAAATSGSGSSGLTMRHNNALAVSIETDV -> SYLPGALGQHLKKSSL
FT SESSSDIMDLDDGIDATTPGLTDHTGRHMVPFLRTQQSFEKQQLQLQLQLQQQSQSPHG
FT QQMTQQQQLGQNGLRSTNSLQLRHNNAMAVSIETDV (in isoform Alpha and
FT isoform D)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:2441471, ECO:0000303|PubMed:2448635,
FT ECO:0000303|PubMed:2456921, ECO:0000303|Ref.9"
FT /id="VSP_000959"
FT VAR_SEQ 512
FT /note="L -> LV (in isoform L)"
FT /evidence="ECO:0000305"
FT /id="VSP_054720"
FT VARIANT 178
FT /note="K -> E (in RNA edited version)"
FT VARIANT 178
FT /note="K -> G (in RNA edited version)"
FT VARIANT 178
FT /note="K -> R (in RNA edited version)"
FT VARIANT 360
FT /note="I -> M (in RNA edited version)"
FT VARIANT 464
FT /note="I -> V (in RNA edited version)"
FT VARIANT 489
FT /note="T -> A (in RNA edited version)"
FT VARIANT 491
FT /note="Q -> R (in RNA edited version)"
FT MUTAGEN 248
FT /note="T->I: In mns; flies display reduced sleep."
FT /evidence="ECO:0000269|PubMed:15858564"
FT CONFLICT 563
FT /note="Q -> QQ (in Ref. 4; CAA29917)"
FT /evidence="ECO:0000305"
FT CONFLICT 583..584
FT /note="QL -> HV (in Ref. 4; CAA29917)"
FT /evidence="ECO:0000305"
FT HELIX 380..394
FT /evidence="ECO:0007829|PDB:1HO2"
SQ SEQUENCE 655 AA; 74193 MW; 5833E3052C9D19B3 CRC64;
MAAVAGLYGL GEDRQHRKKQ QQQQQHQKEQ LEQKEEQKKI AERKLQLREQ QLQRNSLDGY
GSLPKLSSQD EEGGAGHGFG GGPQHFEPIP HDHDFCERVV INVSGLRFET QLRTLNQFPD
TLLGDPARRL RYFDPLRNEY FFDRSRPSFD AILYYYQSGG RLRRPVNVPL DVFSEEIKFY
ELGDQAINKF REDEGFIKEE ERPLPDNEKQ RKVWLLFEYP ESSQAARVVA IISVFVILLS
IVIFCLETLP EFKHYKVFNT TTNGTKIEED EVPDITDPFF LIETLCIIWF TFELTVRFLA
CPNKLNFCRD VMNVIDIIAI IPYFITLATV VAEEEDTLNL PKAPVSPQDK SSNQAMSLAI
LRVIRLVRVF RIFKLSRHSK GLQILGRTLK ASMRELGLLI FFLFIGVVLF SSAVYFAEAG
SENSFFKSIP DAFWWAVVTM TTVGYGDMTP VGVWGKIVGS LCAIAGVLTI ALPVPVIVSN
FNYFYHRETD QEEMQSQNFN HVTSCPYLPG TLGQHMKKSS LSESSSDMMD LDDGVESTPG
LTETHPGRSA VAPFLGAQQQ QQQPVASSLS MSIDKQLQHP LQQLTQTQLY QQQQQQQQQQ
QNGFKQQQQQ TQQQLQQQQS HTINASAAAA TSGSGSSGLT MRHNNALAVS IETDV
