KCNAW_DROME
ID KCNAW_DROME Reviewed; 498 AA.
AC P17972; Q9VQU5;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Potassium voltage-gated channel protein Shaw;
DE AltName: Full=Shaw2;
GN Name=Shaw; Synonyms=SHAW2; ORFNames=CG2822;
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].
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].
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.
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 -!- 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 -!- MISCELLANEOUS: This channel protein belongs to the delayed rectifier
CC class.
CC -!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
CC 1.A.1.2) subfamily. Shaw sub-subfamily. {ECO:0000305}.
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DR EMBL; M32661; AAA28897.1; -; mRNA.
DR EMBL; AE014134; AAF51069.1; -; Genomic_DNA.
DR PIR; A41359; A41359.
DR RefSeq; NP_476721.1; NM_057373.3.
DR AlphaFoldDB; P17972; -.
DR SMR; P17972; -.
DR BioGRID; 59803; 2.
DR STRING; 7227.FBpp0288427; -.
DR TCDB; 1.A.1.2.2; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; P17972; 3 sites.
DR PaxDb; P17972; -.
DR DNASU; 33599; -.
DR EnsemblMetazoa; FBtr0089274; FBpp0088331; FBgn0003386.
DR GeneID; 33599; -.
DR KEGG; dme:Dmel_CG2822; -.
DR CTD; 33599; -.
DR FlyBase; FBgn0003386; Shaw.
DR VEuPathDB; VectorBase:FBgn0003386; -.
DR eggNOG; KOG3713; Eukaryota.
DR HOGENOM; CLU_011722_4_3_1; -.
DR InParanoid; P17972; -.
DR OMA; KQIEACC; -.
DR PhylomeDB; P17972; -.
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; 33599; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 33599; -.
DR PRO; PR:P17972; -.
DR Proteomes; UP000000803; Chromosome 2L.
DR Bgee; FBgn0003386; Expressed in brain and 16 other tissues.
DR ExpressionAtlas; P17972; baseline and differential.
DR Genevisible; P17972; DM.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0032590; C:dendrite membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0032809; C:neuronal cell body membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:FlyBase.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:FlyBase.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022843; F:voltage-gated cation channel activity; ISS:FlyBase.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISS:FlyBase.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0030431; P:sleep; 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; IPR003974; K_chnl_volt-dep_Kv3.
DR InterPro; IPR015572; Shaw_inv.
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 PANTHER; PTHR11537:SF257; PTHR11537:SF257; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01498; SHAWCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..498
FT /note="Potassium voltage-gated channel protein Shaw"
FT /id="PRO_0000053967"
FT TRANSMEM 175..193
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 230..252
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..284
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 292..313
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 329..350
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TRANSMEM 392..413
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 431..498
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..382
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 498 AA; 56509 MW; 977E3B7F22F098E2 CRC64;
MNLINMDSEN RVVLNVGGIR HETYKATLKK IPATRLSRLT EALANYDPIL NEYFFDRHPG
VFAQVLNYYR TGKLHYPTDV CGPLFEEELE FWGLDSNQVE PCCWMTYTQH RDTQETLAVL
DRLDLDTEKP SEEELARKFG FEEDYYKGTI SWWQEMKPRI WSLFDEPYSS NAAKTIGVVS
VFFICISILS FCLKTHPDMR VPIVRNITVK TANGSNGWFL DKTQTNAHIA FFYIECVCNA
WFTFEILVRF ISSPNKWEFI KSSVNIIDYI ATLSFYIDLV LQRFASHLEN ADILEFFSII
RIMRLFKLTR HSSGLKILIQ TFRASAKELT LLVFFLVLGI VIFASLVYYA ERIQPNPHND
FNSIPLGLWW ALVTMTTVGY GDMAPKTYIG MFVGALCALA GVLTIALPVP VIVSNFAMYY
SHTQARAKLP KKRRRVLPVE QPRQPRLPGA PGGVSGCGTP GSGPHSGPMG SGGTGPRRMN
NKTKDLVSPK SDMAFSFD
