SLO_DROME
ID SLO_DROME Reviewed; 1200 AA.
AC Q03720; A4V3D4; Q24369; Q24384; Q24385; Q59DU0; Q59DU1; Q59DU2; Q59DU3;
AC Q59DU4; Q59DU5; Q59DU6; Q59DU7; Q59DU8; Q59DU9; Q59DV0; Q59DV1; Q59DV2;
AC Q7JP74; Q7KS13; Q86NK5; Q8IMV9; Q9TWA1; Q9VC51;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 3.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Calcium-activated potassium channel slowpoke;
DE Short=dSlo;
DE AltName: Full=BK channel;
DE AltName: Full=Maxi K channel;
DE Short=MaxiK;
GN Name=slo; ORFNames=CG10693;
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 B), NUCLEOTIDE SEQUENCE [MRNA] OF
RP 17-1200 (ISOFORMS 2 AND 3), AND FUNCTION.
RC TISSUE=Head;
RX PubMed=1857984; DOI=10.1126/science.1857984;
RA Atkinson N.S., Robertson G.A., Ganetzky B.;
RT "A component of calcium-activated potassium channels encoded by the
RT Drosophila slo locus.";
RL Science 253:551-555(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; A; D; E; H; I; J; L; N; P AND Q),
RP AND FUNCTION.
RC STRAIN=Canton-S; TISSUE=Head;
RX PubMed=1497890; DOI=10.1016/0896-6273(92)90160-f;
RA Adelman J.P., Shen K.-Z., Kavanaugh M.P., Warren R.A., Wu Y.-N.,
RA Lagrutta A., Bond C.T., North R.A.;
RT "Calcium-activated potassium channels expressed from cloned complementary
RT DNAs.";
RL Neuron 9:209-216(1992).
RN [3]
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82, AND TISSUE SPECIFICITY.
RC STRAIN=Iso-1;
RX PubMed=8774450; DOI=10.1523/jneurosci.16-05-01827.1996;
RA Brenner R., Thomas T.O., Becker M.N., Atkinson N.S.;
RT "Tissue-specific expression of a Ca(2+)-activated K+ channel is controlled
RT by multiple upstream regulatory elements.";
RL J. Neurosci. 16:1827-1835(1996).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=7666207; DOI=10.1523/jneurosci.15-09-06250.1995;
RA Becker M.N., Brenner R., Atkinson N.S.;
RT "Tissue-specific expression of a Drosophila calcium-activated potassium
RT channel.";
RL J. Neurosci. 15:6250-6259(1995).
RN [8]
RP INTERACTION WITH SLIP1.
RX PubMed=9502797; DOI=10.1523/jneurosci.18-07-02360.1998;
RA Xia X.-M., Hirschberg B., Smolik S., Forte M., Adelman J.P.;
RT "dSLo interacting protein 1, a novel protein that interacts with large-
RT conductance calcium-activated potassium channels.";
RL J. Neurosci. 18:2360-2369(1998).
RN [9]
RP INTERACTION WITH SLOB.
RX PubMed=9539129; DOI=10.1016/s0896-6273(00)80995-2;
RA Schopperle W.M., Holmqvist M.H., Zhou Y., Wang J., Wang Z., Griffith L.C.,
RA Keselman I., Kusinitz F., Dagan D., Levitan I.B.;
RT "Slob, a novel protein that interacts with the Slowpoke calcium-dependent
RT potassium channel.";
RL Neuron 20:565-573(1998).
RN [10]
RP INTERACTION WITH PKA AND SRC, PHOSPHORYLATION AT SER-978, AND MUTAGENESIS
RP OF TYR-552; SER-978 AND TYR-1012.
RX PubMed=10234050; DOI=10.1523/jneurosci.19-10-j0005.1999;
RA Wang J., Zhou Y., Wen H., Levitan I.B.;
RT "Simultaneous binding of two protein kinases to a calcium-dependent
RT potassium channel.";
RL J. Neurosci. 19:RC4-RC4(1999).
RN [11]
RP INDIRECT INTERACTION WITH 14-3-3-ZETA.
RX PubMed=10230800; DOI=10.1016/s0896-6273(00)80739-4;
RA Zhou Y., Schopperle W.M., Murrey H., Jaramillo A., Dagan D., Griffith L.C.,
RA Levitan I.B.;
RT "A dynamically regulated 14-3-3, Slob, and Slowpoke potassium channel
RT complex in Drosophila presynaptic nerve terminals.";
RL Neuron 22:809-818(1999).
RN [12]
RP DOMAIN CALCIUM BOWL, AND MUTAGENESIS OF 1002-ASP--ASP-1006.
RX PubMed=11274367; DOI=10.1073/pnas.081072398;
RA Bian S., Favre I., Moczydlowski E.;
RT "Ca2+-binding activity of a COOH-terminal fragment of the Drosophila BK
RT channel involved in Ca2+-dependent activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4776-4781(2001).
RN [13]
RP PHOSPHORYLATION.
RX PubMed=12019304; DOI=10.1523/jneurosci.22-10-03855.2002;
RA Zhou Y., Wang J., Wen H., Kucherovsky O., Levitan I.B.;
RT "Modulation of Drosophila slowpoke calcium-dependent potassium channel
RT activity by bound protein kinase a catalytic subunit.";
RL J. Neurosci. 22:3855-3863(2002).
CC -!- FUNCTION: Potassium channel activated by both membrane depolarization
CC or increase in cytosolic Ca(2+) that mediates export of K(+). Its
CC activation dampens the excitatory events that elevate the cytosolic
CC Ca(2+) concentration and/or depolarize the cell membrane. It therefore
CC contributes to repolarization of the membrane potential. Kinetics are
CC determined by alternative splicing, phosphorylation status and its
CC combination interaction with Slob and 14-3-3-zeta. While the
CC interaction with Slob1 alone increases its activity, its interaction
CC with both Slob1 and 14-3-3-zeta decreases its activity.
CC {ECO:0000269|PubMed:1497890, ECO:0000269|PubMed:1857984}.
CC -!- SUBUNIT: Homotetramer; which constitutes the calcium-activated
CC potassium channel (By similarity). Interacts with Slip1. Interacts with
CC Slob, and, indirectly with 14-3-3-zeta via its interaction with Slob.
CC Interacts with Pka-C1 and Src kinases, which can bind simultaneously to
CC it. {ECO:0000250, ECO:0000269|PubMed:10234050,
CC ECO:0000269|PubMed:9502797, ECO:0000269|PubMed:9539129}.
CC -!- INTERACTION:
CC Q03720; P12370: Pka-C1; NbExp=5; IntAct=EBI-426805, EBI-82224;
CC Q03720; Q8MR31: Slip1; NbExp=5; IntAct=EBI-426805, EBI-123875;
CC Q03720; Q8IPH9-1: Slob; NbExp=2; IntAct=EBI-426805, EBI-424896;
CC Q03720; P00528: Src64B; NbExp=3; IntAct=EBI-426805, EBI-87092;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=20;
CC Comment=Additional isoforms seem to exist.;
CC Name=N;
CC IsoId=Q03720-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q03720-2; Sequence=VSP_050267, VSP_050268;
CC Name=3;
CC IsoId=Q03720-4; Sequence=VSP_050268;
CC Name=5;
CC IsoId=Q03720-6; Sequence=VSP_010001, VSP_010002, VSP_050267,
CC VSP_050268;
CC Name=6;
CC IsoId=Q03720-3; Sequence=VSP_009999, VSP_010000, VSP_010001,
CC VSP_010003, VSP_050268;
CC Name=A; Synonyms=G;
CC IsoId=Q03720-5; Sequence=VSP_010004;
CC Name=B;
CC IsoId=Q03720-7; Sequence=VSP_009999;
CC Name=C;
CC IsoId=Q03720-8; Sequence=VSP_009999, VSP_010002;
CC Name=D;
CC IsoId=Q03720-9; Sequence=VSP_020625, VSP_010004;
CC Name=E;
CC IsoId=Q03720-10; Sequence=VSP_010000, VSP_010004;
CC Name=F;
CC IsoId=Q03720-11; Sequence=VSP_010001, VSP_010004;
CC Name=H;
CC IsoId=Q03720-12; Sequence=VSP_010002, VSP_010004;
CC Name=I;
CC IsoId=Q03720-13; Sequence=VSP_050267;
CC Name=J;
CC IsoId=Q03720-14; Sequence=VSP_020627;
CC Name=K;
CC IsoId=Q03720-15; Sequence=VSP_020628;
CC Name=L;
CC IsoId=Q03720-16; Sequence=VSP_020626;
CC Name=M;
CC IsoId=Q03720-17; Sequence=VSP_010004, VSP_050268;
CC Name=O;
CC IsoId=Q03720-18; Sequence=VSP_010002, VSP_020628;
CC Name=P;
CC IsoId=Q03720-19; Sequence=VSP_010000, VSP_010002, VSP_020628;
CC Name=Q;
CC IsoId=Q03720-20; Sequence=VSP_010000, VSP_010002, VSP_010004;
CC -!- TISSUE SPECIFICITY: Expressed in muscle cells, neurons of the CNS and
CC PNS, mushroom bodies, a limited number of cells in embryonic and larval
CC midgut and in epithelial-derived tracheal cells. During pupariation and
CC embryogenesis, it is expressed in muscles many hours prior to the
CC appearance of functional channels. {ECO:0000269|PubMed:7666207,
CC ECO:0000269|PubMed:8774450}.
CC -!- DOMAIN: The S4 segment, which is characterized by a series of
CC positively charged amino acids at every third position, is part of the
CC voltage-sensor. {ECO:0000250}.
CC -!- DOMAIN: The pore-forming domain (also referred as P region) is imbedded
CC into the membrane, and forms the selectivity filter of the pore. It
CC contains the signature sequence of potassium channels that displays
CC selectivity to potassium (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The RCK N-terminal domain mediates the homotetramerization,
CC thereby promoting the assembly of monomers into functional potassium
CC channel. It includes binding sites for Ca(2+) and Mg(2+) (By
CC similarity). {ECO:0000250}.
CC -!- DOMAIN: The calcium bowl constitutes one of the Ca(2+) sensors and
CC probably acts as a Ca(2+)-binding site. {ECO:0000269|PubMed:11274367}.
CC -!- PTM: Phosphorylated. Phosphorylation may be mediated by both PKA and
CC SRC kinases, which activate the channel activity. Phosphorylation by
CC PKA is however unclear. Indeed, although modulation of channel activity
CC requires Pka-C1, it does not interacts with the whole PKA holoenzyme.
CC Moreover, modulation of activity does not depend upon phosphorylation
CC of Ser-978. {ECO:0000269|PubMed:10234050, ECO:0000269|PubMed:12019304}.
CC -!- SIMILARITY: Belongs to the potassium channel family. Calcium-activated
CC (TC 1.A.1.3) subfamily. Slo sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA28902.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO45232.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M69053; AAA28902.1; ALT_INIT; mRNA.
DR EMBL; M96840; AAA28651.1; -; mRNA.
DR EMBL; AE014297; AAF56324.1; -; Genomic_DNA.
DR EMBL; AE014297; AAN14013.1; -; Genomic_DNA.
DR EMBL; AE014297; AAS65211.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52977.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52978.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52979.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52980.2; -; Genomic_DNA.
DR EMBL; AE014297; AAX52981.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52982.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52983.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52984.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52985.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52986.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52987.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52988.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52989.1; -; Genomic_DNA.
DR EMBL; AE014297; AAX52990.1; -; Genomic_DNA.
DR EMBL; BT004876; AAO45232.1; ALT_FRAME; mRNA.
DR EMBL; U40315; AAC47020.1; -; Genomic_DNA.
DR EMBL; U40315; AAC47021.1; -; Genomic_DNA.
DR PIR; A39800; A39800.
DR PIR; C39800; C39800.
DR PIR; JH0697; JH0697.
DR PIR; PS0438; PS0438.
DR PIR; PS0439; PS0439.
DR PIR; PS0440; PS0440.
DR PIR; PS0441; PS0441.
DR PIR; PS0446; PS0446.
DR RefSeq; NP_001014651.1; NM_001014651.3. [Q03720-20]
DR RefSeq; NP_001014652.1; NM_001014652.3. [Q03720-19]
DR RefSeq; NP_001014653.1; NM_001014653.3. [Q03720-18]
DR RefSeq; NP_001014654.1; NM_001014654.3. [Q03720-1]
DR RefSeq; NP_001014655.1; NM_001014655.3. [Q03720-17]
DR RefSeq; NP_001014656.1; NM_001014656.3. [Q03720-16]
DR RefSeq; NP_001014657.1; NM_001014657.3. [Q03720-15]
DR RefSeq; NP_001014658.1; NM_001014658.3. [Q03720-14]
DR RefSeq; NP_001014659.1; NM_001014659.3. [Q03720-13]
DR RefSeq; NP_001014660.1; NM_001014660.3. [Q03720-12]
DR RefSeq; NP_001014661.2; NM_001014661.4. [Q03720-3]
DR RefSeq; NP_001014662.1; NM_001014662.3. [Q03720-11]
DR RefSeq; NP_001014663.1; NM_001014663.3. [Q03720-10]
DR RefSeq; NP_001014664.1; NM_001014664.3. [Q03720-9]
DR RefSeq; NP_524486.2; NM_079762.4. [Q03720-5]
DR RefSeq; NP_733029.1; NM_170164.4. [Q03720-7]
DR RefSeq; NP_996289.1; NM_206566.4. [Q03720-8]
DR PDB; 7PXE; EM; 2.38 A; A/B/C/D=1-1200.
DR PDB; 7PXF; EM; 2.68 A; A/B/C/D=1-1200.
DR PDB; 7PXG; EM; 2.73 A; A/B/C/D=1-1200.
DR PDB; 7PXH; EM; 2.59 A; A/B/C/D=1-1200.
DR PDBsum; 7PXE; -.
DR PDBsum; 7PXF; -.
DR PDBsum; 7PXG; -.
DR PDBsum; 7PXH; -.
DR AlphaFoldDB; Q03720; -.
DR SMR; Q03720; -.
DR BioGRID; 67865; 12.
DR IntAct; Q03720; 9.
DR STRING; 7227.FBpp0303318; -.
DR TCDB; 1.A.1.3.1; the voltage-gated ion channel (vic) superfamily.
DR iPTMnet; Q03720; -.
DR PRIDE; Q03720; -.
DR EnsemblMetazoa; FBtr0084683; FBpp0084063; FBgn0003429. [Q03720-7]
DR EnsemblMetazoa; FBtr0084684; FBpp0084064; FBgn0003429. [Q03720-5]
DR EnsemblMetazoa; FBtr0084685; FBpp0089227; FBgn0003429. [Q03720-8]
DR EnsemblMetazoa; FBtr0100622; FBpp0100082; FBgn0003429. [Q03720-9]
DR EnsemblMetazoa; FBtr0100623; FBpp0100083; FBgn0003429. [Q03720-10]
DR EnsemblMetazoa; FBtr0100624; FBpp0100084; FBgn0003429. [Q03720-11]
DR EnsemblMetazoa; FBtr0100627; FBpp0100086; FBgn0003429. [Q03720-12]
DR EnsemblMetazoa; FBtr0100629; FBpp0100089; FBgn0003429. [Q03720-13]
DR EnsemblMetazoa; FBtr0100631; FBpp0100091; FBgn0003429. [Q03720-14]
DR EnsemblMetazoa; FBtr0100632; FBpp0100092; FBgn0003429. [Q03720-15]
DR EnsemblMetazoa; FBtr0100633; FBpp0100093; FBgn0003429. [Q03720-16]
DR EnsemblMetazoa; FBtr0100634; FBpp0100094; FBgn0003429. [Q03720-17]
DR EnsemblMetazoa; FBtr0100635; FBpp0100095; FBgn0003429. [Q03720-1]
DR EnsemblMetazoa; FBtr0100636; FBpp0100096; FBgn0003429. [Q03720-18]
DR EnsemblMetazoa; FBtr0100637; FBpp0100097; FBgn0003429. [Q03720-19]
DR EnsemblMetazoa; FBtr0100638; FBpp0100098; FBgn0003429. [Q03720-20]
DR EnsemblMetazoa; FBtr0301581; FBpp0290796; FBgn0003429. [Q03720-3]
DR GeneID; 42940; -.
DR KEGG; dme:Dmel_CG10693; -.
DR UCSC; CG10693-RA; d. melanogaster.
DR UCSC; CG10693-RG; d. melanogaster.
DR CTD; 42940; -.
DR FlyBase; FBgn0003429; slo.
DR VEuPathDB; VectorBase:FBgn0003429; -.
DR eggNOG; KOG1420; Eukaryota.
DR GeneTree; ENSGT00940000168407; -.
DR InParanoid; Q03720; -.
DR PhylomeDB; Q03720; -.
DR Reactome; R-DME-1300642; Sperm Motility And Taxes.
DR SignaLink; Q03720; -.
DR BioGRID-ORCS; 42940; 0 hits in 3 CRISPR screens.
DR ChiTaRS; slo; fly.
DR GenomeRNAi; 42940; -.
DR PRO; PR:Q03720; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0003429; Expressed in brain and 13 other tissues.
DR ExpressionAtlas; Q03720; baseline and differential.
DR Genevisible; Q03720; DM.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IDA:FlyBase.
DR GO; GO:0043025; C:neuronal cell body; IDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; NAS:FlyBase.
DR GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; IDA:UniProtKB.
DR GO; GO:0060072; F:large conductance calcium-activated potassium channel activity; IBA:GO_Central.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0048512; P:circadian behavior; IMP:FlyBase.
DR GO; GO:0007623; P:circadian rhythm; IMP:FlyBase.
DR GO; GO:0045433; P:male courtship behavior, veined wing generated song production; IMP:FlyBase.
DR GO; GO:1900074; P:negative regulation of neuromuscular synaptic transmission; IMP:FlyBase.
DR GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0008582; P:regulation of synaptic assembly at neuromuscular junction; IMP:FlyBase.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IMP:FlyBase.
DR InterPro; IPR024939; Ca-act_K_channel_Slo-1.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003929; K_chnl_BK_asu.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10027:SF28; PTHR10027:SF28; 2.
DR Pfam; PF03493; BK_channel_a; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR SUPFAM; SSF51735; SSF51735; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Ion channel; Ion transport;
KW Membrane; Phosphoprotein; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1200
FT /note="Calcium-activated potassium channel slowpoke"
FT /id="PRO_0000054141"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=Segment S0"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..127
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 128..149
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 150..164
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 165..185
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 186..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 211..214
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 215..235
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 236..250
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 285..307
FT /note="Pore-forming; Name=P region"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..316
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 317..337
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 338..1200
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 364..507
FT /note="RCK N-terminal"
FT REGION 505..525
FT /note="Segment S7"
FT REGION 563..583
FT /note="Segment S8"
FT REGION 681..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 746..785
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 828..848
FT /note="Segment S9"
FT REGION 1017..1037
FT /note="Segment S10"
FT REGION 1170..1200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 301..304
FT /note="Selectivity for potassium"
FT MOTIF 988..1010
FT /note="Calcium bowl"
FT COMPBIAS 683..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 746..778
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1180..1200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:10234050"
FT VAR_SEQ 1..17
FT /note="Missing (in isoform 6, isoform B and isoform C)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1857984"
FT /id="VSP_009999"
FT VAR_SEQ 328..356
FT /note="MFASSIPEIIELVGSGNKYGGELKREHGK -> IFASCIPEIIDLIGTRAKY
FT GGTLKNEKGR (in isoform 6, isoform E, isoform P and isoform
FT Q)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1497890"
FT /id="VSP_010000"
FT VAR_SEQ 328..355
FT /note="MFASSIPEIIELVGSGNKYGGELKREHG -> VFASWIPEITELAAQRSKYG
FT GTYSKDPR (in isoform D)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_020625"
FT VAR_SEQ 396..426
FT /note="PPDLELEGLFKRHFTTVEFFQGTIMNPIDLQ -> EPDLELEGLLKRHYTTV
FT AFFQGTMMNAVDLE (in isoform 5, isoform 6 and isoform F)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1497890"
FT /id="VSP_010001"
FT VAR_SEQ 536..569
FT /note="MQSWTNDYLRGTGMEMYTETLSPTFIGIPFAQAT -> TQAWQNDYLQGTGC
FT EMYTETLSPSFTGMTFPQAS (in isoform 5, isoform C, isoform H,
FT isoform O, isoform P and isoform Q)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_010002"
FT VAR_SEQ 649..685
FT /note="LTVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVS -> YVGMIMMQTGM
FT VNQGITSVMNTME (in isoform L)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_020626"
FT VAR_SEQ 650..686
FT /note="TVQPRSKFDDLDEHHPAPTFTPPELPKRVHVRGSVSG -> ATFRKGVRAVQ
FT MVGRAS (in isoform J)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_020627"
FT VAR_SEQ 650..661
FT /note="TVQPRSKFDDLD -> ATFRKGVRAVQMVGRAKDDEYSLSN (in
FT isoform 2, isoform 5 and isoform I)"
FT /evidence="ECO:0000303|PubMed:1497890,
FT ECO:0000303|PubMed:1857984"
FT /id="VSP_050267"
FT VAR_SEQ 650..661
FT /note="TVQPRSKFDDLD -> ATFRKGVRAVQMVGRAN (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_010003"
FT VAR_SEQ 661..697
FT /note="DEHHPAPTFTPPELPKRVHVRGSVSGDITRDREDTNL -> V (in
FT isoform K, isoform O and isoform P)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_020628"
FT VAR_SEQ 661..685
FT /note="Missing (in isoform A, isoform D, isoform E, isoform
FT F, isoform H, isoform M and isoform Q)"
FT /evidence="ECO:0000303|PubMed:1497890"
FT /id="VSP_010004"
FT VAR_SEQ 761
FT /note="P -> PPENDANPYAGYQLAYEVKKLMP (in isoform 2, isoform
FT 3, isoform 5, isoform 6 and isoform M)"
FT /evidence="ECO:0000303|PubMed:12537569,
FT ECO:0000303|PubMed:1497890, ECO:0000303|PubMed:1857984"
FT /id="VSP_050268"
FT MUTAGEN 552
FT /note="Y->F: Affects the interaction with SRC."
FT /evidence="ECO:0000269|PubMed:10234050"
FT MUTAGEN 978
FT /note="S->A: Does not affect activation of channel."
FT /evidence="ECO:0000269|PubMed:10234050"
FT MUTAGEN 1002..1006
FT /note="DDDDD->NNNNN: Alters calcium binding."
FT /evidence="ECO:0000269|PubMed:11274367"
FT MUTAGEN 1012
FT /note="Y->F: Affects the interaction with SRC."
FT /evidence="ECO:0000269|PubMed:10234050"
FT CONFLICT 81
FT /note="E -> R (in Ref. 6; AAC47020/AAC47021)"
FT /evidence="ECO:0000305"
FT CONFLICT 281
FT /note="N -> D (in Ref. 1; AAA28902, 2; AAA28651 and 5;
FT AAO45232)"
FT /evidence="ECO:0000305"
FT CONFLICT 994
FT /note="S -> G (in Ref. 1; AAA28902, 2; AAA28651 and 5;
FT AAO45232)"
FT /evidence="ECO:0000305"
FT HELIX 49..76
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 107..119
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 124..148
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 149..151
FT /evidence="ECO:0007829|PDB:7PXF"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 163..185
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 189..193
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 196..202
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 222..231
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 232..238
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 245..274
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 277..279
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 288..299
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:7PXH"
FT HELIX 312..340
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 367..377
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 380..382
FT /evidence="ECO:0007829|PDB:7PXH"
FT STRAND 387..395
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 412..416
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 422..427
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 430..432
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 434..439
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 447..464
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 469..475
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 477..479
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 480..484
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 491..494
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 496..499
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 500..513
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 517..524
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 534..536
FT /evidence="ECO:0007829|PDB:7PXH"
FT HELIX 538..547
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 550..555
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 558..560
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 565..574
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 579..585
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 595..599
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 610..617
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 618..625
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 800..807
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 815..817
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 821..825
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 833..838
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 849..852
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 853..856
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 862..864
FT /evidence="ECO:0007829|PDB:7PXF"
FT STRAND 868..872
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 874..880
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 881..883
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 884..886
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 888..895
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 900..905
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 908..910
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 912..918
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 927..929
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 932..942
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 981..983
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 986..989
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 993..998
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1001..1003
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1011..1013
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1015..1018
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1022..1024
FT /evidence="ECO:0007829|PDB:7PXH"
FT HELIX 1025..1030
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1031..1037
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1039..1049
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1055..1063
FT /evidence="ECO:0007829|PDB:7PXE"
FT TURN 1074..1077
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1078..1080
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1084..1093
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1096..1101
FT /evidence="ECO:0007829|PDB:7PXE"
FT HELIX 1104..1115
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1118..1126
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1138..1143
FT /evidence="ECO:0007829|PDB:7PXE"
FT STRAND 1155..1160
FT /evidence="ECO:0007829|PDB:7PXE"
SQ SEQUENCE 1200 AA; 133102 MW; 306A12234C63AD0D CRC64;
MASGLIDTNF SSTLANGMSG CDQSTVESLA DDPTDSPFDA DDCLKVRKYW CFLLSSIFTF
LAGLLVVLLW RAFAFVCCRK EPDLGPNDPK QKEQKASRNK QEFEGTFMTE AKDWAGELIS
GQTTTGRILV VLVFILSIAS LIIYFVDASS EEVERCQKWS NNITQQIDLA FNIFFMVYFF
IRFIAASDKL WFMLEMYSFV DYFTIPPSFV SIYLDRTWIG LRFLRALRLM TVPDILQYLN
VLKTSSSIRL AQLVSIFISV WLTAAGIIHL LENSGDPLDF NNAHRLSYWT CVYFLIVTMS
TVGYGDVYCE TVLGRTFLVF FLLVGLAMFA SSIPEIIELV GSGNKYGGEL KREHGKRHIV
VCGHITYESV SHFLKDFLHE DREDVDVEVV FLHRKPPDLE LEGLFKRHFT TVEFFQGTIM
NPIDLQRVKV HEADACLVLA NKYCQDPDAE DAANIMRVIS IKNYSDDIRV IIQLMQYHNK
AYLLNIPSWD WKQGDDVICL AELKLGFIAQ SCLAPGFSTM MANLFAMRSF KTSPDMQSWT
NDYLRGTGME MYTETLSPTF IGIPFAQATE LCFSKLKLLL LAIEIKGAEE GADSKISINP
RGAKIQANTQ GFFIAQSADE VKRAWFYCKA CHEDIKDETL IKKCKCKNLT VQPRSKFDDL
DEHHPAPTFT PPELPKRVHV RGSVSGDITR DREDTNLLNR NVRRPNGTGN GTGGMHHMNN
TAAAAAAAAA AGKQVNKVKP TVNVSRQVEG QVISPSQYNR PTSRSSGTGT QNQNGGVSLP
AGIADDQSKD FDFEKTEMKY DSTGMFHWSP AKSLEDCILD RNQAAMTVLN GHVVVCLFAD
PDSPLIGLRN LVMPLRASNF HYHELKHVVI VGSVDYIRRE WKMLQNLPKI SVLNGSPLSR
ADLRAVNVNL CDMCCILSAK VPSNDDPTLA DKEAILASLN IKAMTFDDTI GVLSQRGPEF
DNLSATAGSP IVLQRRGSVY GANVPMITEL VNDSNVQFLD QDDDDDPDTE LYLTQPFACG
TAFAVSVLDS LMSTTYFNQN ALTLIRSLIT GGATPELELI LAEGAGLRGG YSTVESLSNR
DRCRVGQISL YDGPLAQFGE CGKYGDLFVA ALKSYGMLCI GLYRFRDTSS SCDASSKRYV
ITNPPDDFSL LPTDQVFVLM QFDPGLEYKP PAVRAPAGGR GTNTQGSGVG GGGSNKDDNS
