KCNAB_DROME
ID KCNAB_DROME Reviewed; 985 AA.
AC P17970; O76805; Q9I7T9; Q9I7U0;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Potassium voltage-gated channel protein Shab;
GN Name=Shab; ORFNames=CG43128;
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 (ISOFORMS A AND B).
RC STRAIN=Oregon-R;
RX PubMed=2493160; DOI=10.1126/science.2493160;
RA Butler A., Wei A.G., Baker K., Salkoff L.;
RT "A family of putative potassium channel genes in Drosophila.";
RL Science 243:943-947(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), AND MUTAGENESIS.
RC STRAIN=Canton-S;
RX PubMed=10419540; DOI=10.1074/jbc.274.31.22109;
RA Hegde P., Gu G.G., Chen D., Free S.J., Singh S.;
RT "Mutational analysis of the Shab-encoded delayed rectifier K(+) channels in
RT Drosophila.";
RL J. Biol. Chem. 274:22109-22113(1999).
RN [5]
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 [6]
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).
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.
CC -!- SUBUNIT: Heterotetramer of potassium channel proteins. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=B;
CC IsoId=P17970-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P17970-2; Sequence=VSP_000960;
CC -!- DEVELOPMENTAL STAGE: Expressed in late embryos and pupae.
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. B (Shab) (TC
CC 1.A.1.2) subfamily. Shab sub-subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG22232.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAG22233.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; M32659; AAA28896.1; -; mRNA.
DR EMBL; AF084525; AAC33365.1; -; mRNA.
DR EMBL; AE014296; AAG22232.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014296; AAG22233.1; ALT_INIT; Genomic_DNA.
DR PIR; S12746; S12746.
DR RefSeq; NP_523894.2; NM_079170.6.
DR RefSeq; NP_728783.1; NM_167967.4.
DR AlphaFoldDB; P17970; -.
DR SMR; P17970; -.
DR BioGRID; 63854; 4.
DR STRING; 7227.FBpp0306030; -.
DR TCDB; 1.A.1.2.1; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P17970; 8 sites.
DR PaxDb; P17970; -.
DR GeneID; 38352; -.
DR KEGG; dme:Dmel_CG43128; -.
DR CTD; 38352; -.
DR FlyBase; FBgn0262593; Shab.
DR VEuPathDB; VectorBase:FBgn0262593; -.
DR eggNOG; KOG3713; Eukaryota.
DR HOGENOM; CLU_009690_0_0_1; -.
DR InParanoid; P17970; -.
DR PhylomeDB; P17970; -.
DR Reactome; R-DME-1296072; Voltage gated Potassium channels.
DR Reactome; R-DME-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR BioGRID-ORCS; 38352; 1 hit in 3 CRISPR screens.
DR ChiTaRS; Shab; fly.
DR GenomeRNAi; 38352; -.
DR PRO; PR:P17970; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR ExpressionAtlas; P17970; baseline and differential.
DR Genevisible; P17970; DM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0005251; F:delayed rectifier potassium 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:0007268; P:chemical synaptic transmission; IMP:FlyBase.
DR GO; GO:0008345; P:larval locomotory behavior; IMP:FlyBase.
DR GO; GO:0045938; P:positive regulation of circadian sleep/wake cycle, sleep; 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:0008016; P:regulation of heart contraction; 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 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; IPR003971; K_chnl_volt-dep_Kv9.
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; PR01494; KV9CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..985
FT /note="Potassium voltage-gated channel protein Shab"
FT /id="PRO_0000053965"
FT TRANSMEM 436..454
FT /note="Helical; Name=Segment S1"
FT TRANSMEM 474..495
FT /note="Helical; Name=Segment S2"
FT TRANSMEM 506..527
FT /note="Helical; Name=Segment S3"
FT TRANSMEM 536..561
FT /note="Helical; Name=Segment S4"
FT TRANSMEM 577..598
FT /note="Helical; Name=Segment S5"
FT TRANSMEM 638..659
FT /note="Helical; Name=Segment S6"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 160..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 721..775
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 789..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..916
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 623..628
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 170..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..774
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 690
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 731
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT MOD_RES 796
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 530
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 885
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 888
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 914
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 717..746
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:10419540"
FT /id="VSP_000960"
FT MUTAGEN 435
FT /note="R->Q: In allele Shab-1; temperature-sensitive
FT paralytic."
FT /evidence="ECO:0000269|PubMed:10419540"
FT MUTAGEN 608
FT /note="V->D: In allele Shab-1; temperature-sensitive
FT paralytic."
FT /evidence="ECO:0000269|PubMed:10419540"
FT CONFLICT 31
FT /note="Q -> L (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 220
FT /note="S -> G (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 307
FT /note="R -> G (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="S -> G (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 414..415
FT /note="FS -> CA (in Ref. 5; AAG22232/AAG22233)"
FT /evidence="ECO:0000305"
FT CONFLICT 495
FT /note="A -> S (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="V -> I (in Ref. 5; AAG22232/AAG22233)"
FT /evidence="ECO:0000305"
FT CONFLICT 613
FT /note="A -> T (in Ref. 5; AAG22232/AAG22233)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="C -> Y (in Ref. 5; AAG22232/AAG22233)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="V -> I (in Ref. 5; AAG22232/AAG22233)"
FT /evidence="ECO:0000305"
FT CONFLICT 827..828
FT /note="EQ -> DE (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 877
FT /note="A -> G (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 903..985
FT /note="GDGDGGGVDDDNLSQAKGLPIQMMITPGEVAELRRQVALENLQNQRMDNLEQ
FT DVPVEFECCFCTTKGLPGCHGECIPLRANSV -> VMEMGAVSMTTTFPRPRDCPSR
FT (in Ref. 1, 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 911..913
FT /note="DDD -> NDN (in Ref. 4; AAC33365)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 985 AA; 106359 MW; 59E38AD35F064AC8 CRC64;
MVGQLQGGQA AGQQQQQQQA TQQQQHSKQQ QQQQQQQQQQ LQLKQHQQQQ QDILYQQHNE
AIAIARGLQA ATPADIGDNQ PYYDTSGNVD WERAMGAGGA GAYGGIGIGS LPAAGGAAYH
LGPANPAGLV SRHLDYGDGG HLAGPSAGLP AGAVGSGAGA GAGAGASVTG SGSGAGTGTG
TGAGSGSGSG AAGKEVRYAP FPVASPTHSI PTTSQQIVGS VGGVGVGGAS SQSISGGVPT
HSQSNTTGAL QRTHSRSMSS IPPPEPFMIA QSKAVNSRVS INVGGVRHEV LWRTLERLPH
TRLGRLRECT THEAIVELCD DYSLADNEYF FDRHPKSFSS ILNFYRTGKL HIVDEMCVLA
FSDDLEYWGV DELYLESCCQ HKYHQRKENV HEEMRKEAES LRQRDEEEFG EGKFSEYQKY
LWELLEKPNT SFAARVIAVI SILFIVLSTI ALTLNTLPQL QHIDNGTPQD NPQLAMVEAV
CITWFTLEYI LRFSASPDKW KFFKGGLNII DLLAILPYFV SLFLLETNKN ATDQFQDVRR
VVQVFRIMRI LRVLKLARHS TGLQSLGFTL RNSYKELGLL MLFLAMGVLI FSSLAYFAEK
DEKDTKFVSI PEAFWWAGIT MTTVGYGDIC PTTALGKVIG TVCCICGVLV VALPIPIIVN
NFAEFYKNQM RREKALKRRE ALDRAKREGS IVSFHHINLK DAFAKSMDLI DVIVDTGKQT
NVVHPKGKRQ STPNIGRQTL DVQSAPGHNL SQTDGNSTEG ESTSGRNPAT TGTGCYKNYD
HVANLRNSNL HNRRGSSSEQ DAVPPYSFDN PNARQTSMMA MESYRREQQA LLQQQQQQQQ
QMLQMQQIQQ KAPNGNGGAT GGGVANNLAM VAASSAATAV ATATNASNAS NTAPGSEGAE
GGGDGDGGGV DDDNLSQAKG LPIQMMITPG EVAELRRQVA LENLQNQRMD NLEQDVPVEF
ECCFCTTKGL PGCHGECIPL RANSV
