ID   KCNS1_MOUSE             Reviewed;         497 AA.
AC   O35173; A2A5M1;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   27-MAR-2024, entry version 166.
DE   RecName: Full=Potassium voltage-gated channel subfamily S member 1;
DE   AltName: Full=Delayed-rectifier K(+) channel alpha subunit 1;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv9.1;
GN   Name=Kcns1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND
RP   TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9305895; DOI=10.1074/jbc.272.39.24371;
RA   Salinas M., Duprat F., Heurteaux C., Hugnot J.-P., Lazdunski M.;
RT   "New modulatory alpha subunits for mammalian Shab K+ channels.";
RL   J. Biol. Chem. 272:24371-24379(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potassium channel subunit that does not form functional
CC       channels by itself. Can form functional heterotetrameric channels with
CC       KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated
CC       potassium channel activation and deactivation rates of KCNB1 and KCNB2
CC       (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
CC   -!- SUBUNIT: Heterotetramer with KCNB1 and KCNB2 (PubMed:9305895). Does not
CC       form homomultimers (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9305895};
CC       Multi-pass membrane protein {ECO:0000305}. Note=May not reach the
CC       plasma membrane but remain in an intracellular compartment in the
CC       absence of KCNB1 or KCNB2 (PubMed:9305895).
CC       {ECO:0000269|PubMed:9305895}.
CC   -!- TISSUE SPECIFICITY: Detected in brain, but not in the other tissues
CC       tested. The highest levels of expression are in olfactory bulb,
CC       cerebral cortex, hippocampus, habenula, basolateral amygdaloid nuclei
CC       and cerebellum (PubMed:9305895). {ECO:0000269|PubMed:9305895}.
CC   -!- DOMAIN: The transmembrane segment S4 functions as a voltage-sensor and
CC       is characterized by a series of positively charged amino acids at every
CC       third position. Channel opening and closing is effected by a
CC       conformation change that affects the position and orientation of the
CC       voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC       transmembrane electric field that is positive inside would push the
CC       positively charged S4 segment outwards, thereby opening the pore, while
CC       a field that is negative inside would pull the S4 segment inwards and
CC       close the pore. Changes in the position and orientation of S4 are then
CC       transmitted to the activation gate formed by the inner helix bundle via
CC       the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
CC   -!- SIMILARITY: Belongs to the potassium channel family. S (TC 1.A.1.2)
CC       subfamily. Kv9.1/KCNS1 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF008573; AAB72050.1; -; mRNA.
DR   EMBL; AL591512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH466551; EDL06364.1; -; Genomic_DNA.
DR   CCDS; CCDS17022.1; -.
DR   RefSeq; NP_032461.2; NM_008435.2.
DR   AlphaFoldDB; O35173; -.
DR   SMR; O35173; -.
DR   BioGRID; 200919; 7.
DR   STRING; 10090.ENSMUSP00000038901; -.
DR   iPTMnet; O35173; -.
DR   PhosphoSitePlus; O35173; -.
DR   PaxDb; 10090-ENSMUSP00000038901; -.
DR   ProteomicsDB; 263504; -.
DR   ABCD; O35173; 1 sequenced antibody.
DR   Antibodypedia; 27521; 75 antibodies from 20 providers.
DR   DNASU; 16538; -.
DR   Ensembl; ENSMUST00000045196.4; ENSMUSP00000038901.4; ENSMUSG00000040164.4.
DR   GeneID; 16538; -.
DR   KEGG; mmu:16538; -.
DR   UCSC; uc008ntv.1; mouse.
DR   AGR; MGI:1197019; -.
DR   CTD; 3787; -.
DR   MGI; MGI:1197019; Kcns1.
DR   VEuPathDB; HostDB:ENSMUSG00000040164; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000160096; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; O35173; -.
DR   OMA; CSGRYHE; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; O35173; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16538; 2 hits in 77 CRISPR screens.
DR   ChiTaRS; Kcns1; mouse.
DR   PRO; PR:O35173; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; O35173; Protein.
DR   Bgee; ENSMUSG00000040164; Expressed in lumbar dorsal root ganglion and 34 other cell types or tissues.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0006813; P:potassium ion transport; IDA:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF61; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY S MEMBER 1; 1.
DR   PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF02214; BTB_2; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   PRINTS; PR00169; KCHANNEL.
DR   PRINTS; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   Genevisible; O35173; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..497
FT                   /note="Potassium voltage-gated channel subfamily S member
FT                   1"
FT                   /id="PRO_0000054082"
FT   TOPO_DOM        1..186
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        187..208
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        209..239
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        240..262
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        263..273
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        274..291
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        292..309
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        310..330
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        331..345
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        346..367
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        368..379
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        380..391
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        392..399
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        400..406
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        407..435
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        436..497
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   REGION          464..497
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           392..397
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   COMPBIAS        475..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        440
FT                   /note="A -> G (in Ref. 1; AAB72050)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   497 AA;  54918 MW;  F734A3D4B093BEBE CRC64;
     MVSEFPGPGS RVPWRPRDEA LRVNVGGVRR LLSARALARF PGTRLGRLQA AASEEQARRL
     CDDYDAAAHE FYFDRHPGFF LGLLHFYRTG HLHVLDELCV FAFGQEADYW GLGENALATC
     CRARYLERRV ARPRAWDEDS DAPSSVDPCP DEISDVQREL ARYGAARCGR LRRRLWLTME
     NPGYSLPSKL FSCVSIGVVL ASIAAMCIHS LPEYQAREAA AAVAAVAAGR SAEEVRDDPV
     LRRLEYFCIA WFSFEVSSRL LLAPSTRNFF CHPLNLIDIV SVLPFYLTLL AGAALGDQRG
     ASGEELGDLG KVVQVFRLMR IFRVLKLARH STGLRSLGAT LKHSYREVGI LLLYLAVGVS
     VFSGVAYTAE EENEGFHTIP ACWWWGTVSM TTVGYGDVVP ETVGGKLAAS GCILGGILVV
     ALPITIIFNK FSHFYRRQKA LEAAVRSSGQ REFEDLLSSV DGVSDVSLET SRDTSQEGRS
     TDLETQAPRE PAKSHSY
//