KCNAL_DROME
ID KCNAL_DROME Reviewed; 571 AA.
AC P17971; A8JNV8; Q29R37; Q9VW11;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Potassium voltage-gated channel protein Shal;
DE AltName: Full=Shaker cognate l;
DE AltName: Full=Shal2;
GN Name=Shal; Synonyms=SHAL2; ORFNames=CG9262;
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 A).
RX PubMed=2333511; DOI=10.1126/science.2333511;
RA Wei A.G., Covarrubias M., Butler A., Baker K., Pak M., Salkoff L.;
RT "K+ current diversity is produced by an extended gene family conserved in
RT Drosophila and mouse.";
RL Science 248:599-603(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A).
RX PubMed=2336395; DOI=10.1093/nar/18.8.2173;
RA Butler A., Wei A., Baker K., Salkoff L.;
RT "Shal, Shab, and Shaw: three genes encoding potassium channels in
RT Drosophila.";
RL Nucleic Acids Res. 18:2173-2174(1990).
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 A).
RC STRAIN=Berkeley; TISSUE=Embryo;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH SIDL, TISSUE SPECIFICITY, AND MUTAGENESIS OF
RP 481-LEU-LEU-482.
RX PubMed=20550966; DOI=10.1016/j.mcn.2010.06.001;
RA Diao F., Chaufty J., Waro G., Tsunoda S.;
RT "SIDL interacts with the dendritic targeting motif of Shal (K(v)4) K+
RT channels in Drosophila.";
RL Mol. Cell. Neurosci. 45:75-83(2010).
CC -!- FUNCTION: Mediates the voltage-dependent potassium ion permeability of
CC excitable membranes. Assuming opened or closed conformations in
CC response to the voltage difference across the membrane, the protein
CC forms a potassium-selective channel through which potassium ions may
CC pass in accordance with their electrochemical gradient. May play a role
CC in the nervous system and in the regulation of beating frequency in
CC pacemaker cells.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins (By similarity).
CC Interacts (via C-terminal dendritic targeting motif) with SIDL.
CC {ECO:0000250, ECO:0000269|PubMed:20550966}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. Cell
CC projection, dendrite. Perikaryon.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B; Synonyms=Shal1;
CC IsoId=P17971-2; Sequence=Displayed;
CC Name=A;
CC IsoId=P17971-1; Sequence=VSP_042874, VSP_042875;
CC -!- TISSUE SPECIFICITY: Co-expressed with SIDL in the nervous system.
CC {ECO:0000269|PubMed:20550966}.
CC -!- DOMAIN: The N-terminus may be important in determining the rate of
CC inactivation of the channel while the tail may play a role in
CC modulation of channel activity and/or targeting of the channel to
CC specific subcellular compartments.
CC -!- MISCELLANEOUS: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
CC 1.A.1.2) subfamily. Shal sub-subfamily. {ECO:0000305}.
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DR EMBL; M32660; AAA28895.1; -; mRNA.
DR EMBL; AE014296; AAF49144.2; -; Genomic_DNA.
DR EMBL; AE014296; ABW08570.1; -; Genomic_DNA.
DR EMBL; BT024203; ABC86265.1; -; mRNA.
DR PIR; A35312; A35312.
DR RefSeq; NP_001097646.1; NM_001104176.2. [P17971-2]
DR RefSeq; NP_524159.1; NM_079435.4. [P17971-1]
DR AlphaFoldDB; P17971; -.
DR SMR; P17971; -.
DR BioGRID; 65399; 4.
DR DIP; DIP-19398N; -.
DR IntAct; P17971; 2.
DR STRING; 7227.FBpp0111766; -.
DR TCDB; 1.A.1.2.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P17971; 4 sites.
DR PaxDb; P17971; -.
DR PRIDE; P17971; -.
DR DNASU; 40129; -.
DR EnsemblMetazoa; FBtr0074973; FBpp0074741; FBgn0005564. [P17971-1]
DR EnsemblMetazoa; FBtr0112853; FBpp0111766; FBgn0005564. [P17971-2]
DR GeneID; 40129; -.
DR KEGG; dme:Dmel_CG9262; -.
DR UCSC; CG9262-RB; d. melanogaster.
DR CTD; 40129; -.
DR FlyBase; FBgn0005564; Shal.
DR VEuPathDB; VectorBase:FBgn0005564; -.
DR eggNOG; KOG4390; Eukaryota.
DR GeneTree; ENSGT00940000155343; -.
DR InParanoid; P17971; -.
DR OMA; RTTVEKY; -.
DR PhylomeDB; P17971; -.
DR Reactome; R-DME-1296072; Voltage gated Potassium channels.
DR Reactome; R-DME-5576894; Phase 1 - inactivation of fast Na+ channels.
DR SignaLink; P17971; -.
DR BioGRID-ORCS; 40129; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 40129; -.
DR PRO; PR:P17971; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0005564; Expressed in crop (Drosophila) and 26 other tissues.
DR ExpressionAtlas; P17971; baseline and differential.
DR GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
DR GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IDA:FlyBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0008306; P:associative learning; IMP:FlyBase.
DR GO; GO:0007268; P:chemical synaptic transmission; 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:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR003975; K_chnl_volt-dep_Kv4.
DR InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
DR InterPro; IPR021645; Shal-type_N.
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; PF11879; DUF3399; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF11601; Shal-type; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01497; SHALCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..571
FT /note="Potassium voltage-gated channel protein Shal"
FT /id="PRO_0000053966"
FT TRANSMEM 186..204
FT /note="Helical; Name=Segment S1"
FT TRANSMEM 229..250
FT /note="Helical; Name=Segment S2"
FT TRANSMEM 261..282
FT /note="Helical; Name=Segment S3"
FT TRANSMEM 290..308
FT /note="Helical; Name=Segment S4"
FT TRANSMEM 324..345
FT /note="Helical; Name=Segment S5"
FT TRANSMEM 385..406
FT /note="Helical; Name=Segment S6"
FT REGION 474..489
FT /note="Mediates dendritic targeting"
FT /evidence="ECO:0000250"
FT REGION 500..520
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 370..375
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT CARBOHYD 46
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 353
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 408
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 490
FT /note="D -> M (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2333511,
FT ECO:0000303|PubMed:2336395, ECO:0000303|Ref.5"
FT /id="VSP_042874"
FT VAR_SEQ 491..571
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2333511,
FT ECO:0000303|PubMed:2336395, ECO:0000303|Ref.5"
FT /id="VSP_042875"
FT MUTAGEN 481..482
FT /note="LL->AA: Reduced binding to SIDL."
FT /evidence="ECO:0000269|PubMed:20550966"
SQ SEQUENCE 571 AA; 64570 MW; E69D483ADD1D0BDC CRC64;
MASVAAWLPF ARAAAIGWVP IATHPLPPPP MPKDRRKTDD EKLLINVSGR RFETWRNTLE
KYPDTLLGSN EREFFYDEDC KEYFFDRDPD IFRHILNYYR TGKLHYPKHE CLTSYDEELA
FFGIMPDVIG DCCYEDYRDR KRENAERLMD DKLSENGDQN LQQLTNMRQK MWRAFENPHT
STSALVFYYV TGFFIAVSVM ANVVETVPCG HRPGRAGTLP CGERYKIVFF CLDTACVMIF
TAEYLLRLFA APDRCKFVRS VMSIIDVVAI MPYYIGLGIT DNDDVSGAFV TLRVFRVFRI
FKFSRHSQGL RILGYTLKSC ASELGFLVFS LAMAIIIFAT VMFYAEKNVN GTNFTSIPAA
FWYTIVTMTT LGYGDMVPET IAGKIVGGVC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
KRKAQRKARL ARIRIAKASS GAAFVSKKKA AEARWAAQES GIELDDNYRD EDIFELQHHH
LLRCLEKTTD REFVELEIPF NGQPKRPGSP SPMASPAHST NSAAGLLQSC CGRCCSQRYQ
ACGKYMPAAS NAQNSQNNQP MDGTYLVEAS F
