KCNN_DROME
ID KCNN_DROME Reviewed; 927 AA.
AC Q7KVW5; A4V3Z5; A8WHR7; Q058W0; Q7KVW6; Q8IRR8; Q8IS28; Q8IS29; Q8MRM1;
AC Q8MRR6; Q9W4C6; Q9W4C7;
DT 03-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-OCT-2011, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Small conductance calcium-activated potassium channel protein;
DE AltName: Full=Protein SK;
DE AltName: Full=dSK;
GN Name=SK {ECO:0000312|FlyBase:FBgn0029761}; ORFNames=CG10706;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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 [2] {ECO:0000305}
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 [3] {ECO:0000305, ECO:0000312|EMBL:AAM50183.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS I AND J), AND RNA EDITING
RP OF POSITION 782.
RC STRAIN=Berkeley {ECO:0000312|EMBL:AAM50183.1};
RC TISSUE=Head {ECO:0000269|PubMed:12537569};
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 [4] {ECO:0000305, ECO:0000312|EMBL:ABJ17041.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM H).
RC STRAIN=Berkeley {ECO:0000312|EMBL:ABJ17041.1};
RA Stapleton M., Carlson J.W., Frise E., Kapadia B., Park S., Wan K.H., Yu C.,
RA Celniker S.E.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000305, ECO:0000312|EMBL:ABJ17041.1}
RP NUCLEOTIDE SEQUENCE [MRNA] OF 483-767 (ISOFORMS I/J/K/L AND M/H).
RA Nolazco G.M., Nguyen P., Theisen H., Ono J.K., McCaman R.E.;
RT "Gene structure and developmental regulation of the small conductance
RT calcium-activated potassium channel gene (dSK) in Drosophila.";
RL Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305}
RP RNA EDITING OF POSITION 785.
RX PubMed=17018572; DOI=10.1261/rna.254306;
RA Stapleton M., Carlson J.W., Celniker S.E.;
RT "RNA editing in Drosophila melanogaster: new targets and functional
RT consequences.";
RL RNA 12:1922-1932(2006).
CC -!- FUNCTION: Forms a voltage-independent potassium channel activated by
CC intracellular calcium. Activation is followed by membrane
CC hyperpolarization. Thought to regulate neuronal excitability by
CC contributing to the slow component of synaptic afterhyperpolarization.
CC The channel is blocked by apamin (By similarity).
CC {ECO:0000250|UniProtKB:P70604}.
CC -!- SUBUNIT: Heterooligomer. The complex is composed of 4 channel subunits
CC each of which binds to a calmodulin subunit which regulates the channel
CC activity through calcium-binding (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=K;
CC IsoId=Q7KVW5-1; Sequence=Displayed;
CC Name=J;
CC IsoId=Q7KVW5-2; Sequence=VSP_052364;
CC Name=L;
CC IsoId=Q7KVW5-4; Sequence=VSP_052358, VSP_052365;
CC Name=M;
CC IsoId=Q7KVW5-5; Sequence=VSP_052363;
CC Name=N;
CC IsoId=Q7KVW5-6; Sequence=VSP_038238, VSP_038239;
CC Name=I;
CC IsoId=Q7KVW5-7; Sequence=VSP_052358;
CC Name=H;
CC IsoId=Q7KVW5-8; Sequence=VSP_052358, VSP_052362, VSP_052363;
CC -!- RNA EDITING: Modified_positions=782 {ECO:0000269|PubMed:12537569};
CC Note=Partially edited. Target of Adar. {ECO:0000269|PubMed:17018572};
CC -!- SIMILARITY: Belongs to the potassium channel KCNN family. SK subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM50111.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
CC Sequence=ABJ17041.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF46029.4; -; Genomic_DNA.
DR EMBL; AE014298; AAF46030.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09136.3; -; Genomic_DNA.
DR EMBL; AE014298; AAN09137.2; -; Genomic_DNA.
DR EMBL; AE014298; AAS65264.2; -; Genomic_DNA.
DR EMBL; AE014298; AAF46027.4; -; Genomic_DNA.
DR EMBL; AE014298; ABX11900.2; -; Genomic_DNA.
DR EMBL; AY119457; AAM50111.1; ALT_SEQ; mRNA.
DR EMBL; AY119529; AAM50183.1; -; mRNA.
DR EMBL; BT029108; ABJ17041.1; ALT_FRAME; mRNA.
DR EMBL; AY157147; AAN71717.1; -; mRNA.
DR EMBL; AY157148; AAN71718.1; -; mRNA.
DR RefSeq; NP_001096885.2; NM_001103415.2. [Q7KVW5-6]
DR RefSeq; NP_525078.3; NM_080339.3. [Q7KVW5-4]
DR RefSeq; NP_726986.3; NM_167029.3. [Q7KVW5-1]
DR RefSeq; NP_726987.2; NM_167030.2. [Q7KVW5-7]
DR RefSeq; NP_726988.3; NM_167031.3. [Q7KVW5-2]
DR RefSeq; NP_726989.3; NM_167032.2. [Q7KVW5-8]
DR RefSeq; NP_996354.2; NM_206631.4. [Q7KVW5-5]
DR AlphaFoldDB; Q7KVW5; -.
DR SMR; Q7KVW5; -.
DR IntAct; Q7KVW5; 1.
DR STRING; 7227.FBpp0303993; -.
DR TCDB; 1.A.1.16.3; the voltage-gated ion channel (vic) superfamily.
DR PaxDb; Q7KVW5; -.
DR EnsemblMetazoa; FBtr0300467; FBpp0289694; FBgn0029761. [Q7KVW5-8]
DR EnsemblMetazoa; FBtr0301949; FBpp0291161; FBgn0029761. [Q7KVW5-7]
DR EnsemblMetazoa; FBtr0301950; FBpp0291162; FBgn0029761. [Q7KVW5-2]
DR EnsemblMetazoa; FBtr0301951; FBpp0291163; FBgn0029761. [Q7KVW5-1]
DR EnsemblMetazoa; FBtr0301952; FBpp0291164; FBgn0029761. [Q7KVW5-4]
DR EnsemblMetazoa; FBtr0301953; FBpp0291165; FBgn0029761. [Q7KVW5-5]
DR EnsemblMetazoa; FBtr0301954; FBpp0291166; FBgn0029761. [Q7KVW5-6]
DR GeneID; 31456; -.
DR KEGG; dme:Dmel_CG10706; -.
DR UCSC; CG10706-RG; d. melanogaster.
DR CTD; 31456; -.
DR FlyBase; FBgn0029761; SK.
DR VEuPathDB; VectorBase:FBgn0029761; -.
DR eggNOG; KOG3684; Eukaryota.
DR GeneTree; ENSGT00950000182904; -.
DR HOGENOM; CLU_011943_0_0_1; -.
DR InParanoid; Q7KVW5; -.
DR OMA; PPCQWPP; -.
DR Reactome; R-DME-1296052; Ca2+ activated K+ channels.
DR BioGRID-ORCS; 31456; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 31456; -.
DR PRO; PR:Q7KVW5; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0029761; Expressed in brain and 16 other tissues.
DR ExpressionAtlas; Q7KVW5; baseline and differential.
DR Genevisible; Q7KVW5; DM.
DR GO; GO:0016021; C:integral component of membrane; IDA:FlyBase.
DR GO; GO:0043005; C:neuron projection; IBA:GO_Central.
DR GO; GO:0043025; C:neuronal cell body; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IBA:GO_Central.
DR GO; GO:0009881; F:photoreceptor activity; IDA:FlyBase.
DR GO; GO:0016286; F:small conductance calcium-activated potassium channel activity; IDA:FlyBase.
DR GO; GO:0006811; P:ion transport; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IMP:FlyBase.
DR GO; GO:0016057; P:regulation of membrane potential in photoreceptor cell; IDA:FlyBase.
DR InterPro; IPR004178; CaM-bd_dom.
DR InterPro; IPR036122; CaM-bd_dom_sf.
DR InterPro; IPR015449; K_chnl_Ca-activ_SK.
DR InterPro; IPR013099; K_chnl_dom.
DR PANTHER; PTHR10153; PTHR10153; 1.
DR Pfam; PF02888; CaMBD; 1.
DR Pfam; PF07885; Ion_trans_2; 1.
DR Pfam; PF03530; SK_channel; 1.
DR PRINTS; PR01451; SKCHANNEL.
DR SMART; SM01053; CaMBD; 1.
DR SUPFAM; SSF81327; SSF81327; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calmodulin-binding; Ion channel; Ion transport;
KW Membrane; Reference proteome; RNA editing; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..927
FT /note="Small conductance calcium-activated potassium
FT channel protein"
FT /id="PRO_0000282954"
FT TRANSMEM 489..509
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TRANSMEM 530..550
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TRANSMEM 569..589
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TRANSMEM 609..629
FT /note="Helical; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TRANSMEM 658..678
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT INTRAMEM 696..716
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TRANSMEM 724..744
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT REGION 1..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 763..839
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..215
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..251
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..405
FT /note="Missing (in isoform H, isoform I and isoform L)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.4"
FT /id="VSP_052358"
FT VAR_SEQ 2..150
FT /note="SIQKLNDTTNSGYVSSEETDSLLVSSSNPSKGGGRTALLRQVKSNSTNGPTT
FT GASTSSSGSVSGGGGGSGSGGGSASGSAAGASKPTLMRQDRTSTYLTSPQQSQHARMGS
FT EESMRGGASGAAGHDEDVEQGLVRSSIVPDIEVHEEDQ -> SPAFCMDNDCNQSALYQ
FT KCHATPPPPPMPPMPVIPPLPPMPVIPPIPPLPPMVVSTSSTPSATPSMTPSPTPSRSP
FT SLTVMMTSPQALQSLQPQVPQTQMSQPVNTAAALMTRTGSVGGATSAARRNSLWLETLR
FT STRKLSYANERPIL (in isoform N)"
FT /evidence="ECO:0000305"
FT /id="VSP_038238"
FT VAR_SEQ 151..392
FT /note="Missing (in isoform N)"
FT /evidence="ECO:0000305"
FT /id="VSP_038239"
FT VAR_SEQ 546
FT /note="Q -> QVR (in isoform H)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_052362"
FT VAR_SEQ 699..732
FT /note="SMWLTAITFLCVGYGDIVPNTYCGRGITLTCGMV -> AMWLIAITFLSVGF
FT GDIVPNTYCGRGIAVSTGIM (in isoform H and isoform M)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_052363"
FT VAR_SEQ 813..927
FT /note="Missing (in isoform J)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_052364"
FT VAR_SEQ 926
FT /note="S -> SRSVPSSNNAAATYHWPTSPILPPISSRTPHLVPDTHMPSNGSAVNS
FT YASSNKYG (in isoform L)"
FT /evidence="ECO:0000305"
FT /id="VSP_052365"
FT VARIANT 785
FT /note="Y -> C (in RNA edited version)"
FT CONFLICT 781
FT /note="T -> A (in Ref. 3; AAM50111)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 927 AA; 101868 MW; A2342819C33C08B1 CRC64;
MSIQKLNDTT NSGYVSSEET DSLLVSSSNP SKGGGRTALL RQVKSNSTNG PTTGASTSSS
GSVSGGGGGS GSGGGSASGS AAGASKPTLM RQDRTSTYLT SPQQSQHARM GSEESMRGGA
SGAAGHDEDV EQGLVRSSIV PDIEVHEEDQ EQHSQQLNAT TMATMTNNQQ QQQPTISIMN
LSLKPGDSHS HSSSPGSHPN LGTSSYQNLA SSIPPSVPSR CRACRNCSRR ASTTPTTLID
RSASRDSVKS AFQQGNLSGS MAICISNSAL PQQQQLQQQY HLQQQQQQHY QLQQHHLHQQ
QLQQSQQQVP PVLITSSPTN GSRIIRQSSQ PESSSTAICC GPHSACVGHA HSHSHTVPNV
SLKQLRESSG DGIAGIAADS LRINGGMRPF KQLRKPASTL SIPGSMKTPS IANREQISSG
CNEEAAEALV GIHSDYPRYE MYMEERALTG GNTSRKPSTN SAKHKPNVGY RLGKRKALFE
KRKRISDYAL VMGMFGIIVM VIENELSSAG VYTKASFYST ALKTLISVST VILLGLIVAY
HALEVQLFMI DNCADDWRIA MTWQRISQIG LELFICAIHP IPGEYYFQWT TKLANKNKTI
GTEMVPYDVA LSLPMFLRLY LICRVMLLHS KLFTDASSRS IGALNRINFN TRFVLKTLMT
ICPGTVLLVF MVSLWIIASW TLRQCERFHD EEHANLLNSM WLTAITFLCV GYGDIVPNTY
CGRGITLTCG MVGAGCTALL VAVVSRKLEL TRAEKHVHNF MMDTQLTKRL KNAAANVLRE
TWLIYKHTRL VKRVNPGRVR THQRKFLLAI YALRKVKMDQ RKLMDNANTI TDMAKTQNTV
YEIISDMSSR QDAIEERLTN LEDKMQSIQE HMESLPDLLS RCLTQHQERI EQRRNFLHPD
TAAVAPIQAP TPQSMFNAAP MLFPHSS
