ID   KCNS1_RAT               Reviewed;         497 AA.
AC   O88758;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   27-MAR-2024, entry version 148.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Brain;
RX   PubMed=9704029; DOI=10.1006/bbrc.1998.9072;
RA   Stocker M., Kerschensteiner D.;
RT   "Cloning and tissue distribution of two new potassium channel alpha-
RT   subunits from rat brain.";
RL   Biochem. Biophys. Res. Commun. 248:927-934(1998).
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       {ECO:0000250|UniProtKB:O35173}.
CC   -!- SUBUNIT: Heteromultimer with KCNB1 and KCNB2. Does not form
CC       homomultimers. {ECO:0000250|UniProtKB:O35173}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O35173};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:O35173}. Note=May
CC       not reach the plasma membrane but remain in an intracellular
CC       compartment in the absence of KCNB1 or KCNB2.
CC       {ECO:0000250|UniProtKB:O35173}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in brain, but not in the other
CC       tissues tested (PubMed:9704029). {ECO:0000269|PubMed:9704029}.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; Y17606; CAA76804.1; -; mRNA.
DR   PIR; JE0275; JE0275.
DR   RefSeq; NP_446406.1; NM_053954.1.
DR   RefSeq; XP_006235571.1; XM_006235509.3.
DR   RefSeq; XP_017446922.1; XM_017591433.1.
DR   AlphaFoldDB; O88758; -.
DR   SMR; O88758; -.
DR   STRING; 10116.ENSRNOP00000018364; -.
DR   PhosphoSitePlus; O88758; -.
DR   PaxDb; 10116-ENSRNOP00000018364; -.
DR   ABCD; O88758; 1 sequenced antibody.
DR   Ensembl; ENSRNOT00000018364.4; ENSRNOP00000018364.2; ENSRNOG00000013681.4.
DR   Ensembl; ENSRNOT00055006467; ENSRNOP00055004958; ENSRNOG00055004048.
DR   Ensembl; ENSRNOT00060001679; ENSRNOP00060000894; ENSRNOG00060001185.
DR   GeneID; 117023; -.
DR   KEGG; rno:117023; -.
DR   UCSC; RGD:621524; rat.
DR   AGR; RGD:621524; -.
DR   CTD; 3787; -.
DR   RGD; 621524; Kcns1.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000160096; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; O88758; -.
DR   OMA; CSGRYHE; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; O88758; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR   PRO; PR:O88758; -.
DR   Proteomes; UP000002494; Chromosome 3.
DR   Bgee; ENSRNOG00000013681; Expressed in frontal cortex and 7 other cell types or tissues.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; ISS: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; ISS:UniProtKB.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS: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; O88758; RN.
PE   2: Evidence at transcript 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_0000054083"
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"
SQ   SEQUENCE   497 AA;  54915 MW;  268AE4D56051F7A0 CRC64;
     MVSEFPGPGS RVPWRPRDEA LRVNVGGVRR LLSARALARF PGTRLGRLQA AVSEEQARRL
     CDDYDAAARE FYFDRHPGFF LGLLHFYRTG HLHVLDELCV FAFGQEADYW GLGENALATC
     CRARYLERRV TRPRAWDEDS DAPSSVDPCP DEISDVQREL ARYGAARCGR LRRRLWLTME
     NPGYSLPSKL FSCVSIGVVL ASIAAMCIHS LPEYQAREAA AAVAAVAAGR SAEDVRDDPV
     LRRLEYFCIA WFSFEVSSRL LLAPSTRNFF CHPLNLIDIV SVLPFYLTLL AGAALGDRRG
     ASGEELGDLG KVVQVFRLMR IFRVLKLARH STGLRSLGAT LKHSYREVGI LLLYLAVGVS
     VFSGVAYTAE EKNVGFDTIP ACWWWGTVSM TTVGYGDVVP ETVAGKLAAS GCILGGILVV
     ALPITIIFNK FSHFYRRQKA LEAAVRSSGQ REFEDLLSSV DGVSDVSLET SRETSQEGRS
     TDLETQAPSE PAKSHSY
//