KCNS1_RAT
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 03-AUG-2022, entry version 141.
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 voltage-sensor and is
CC 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; 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; O88758; -.
DR PRIDE; O88758; -.
DR ABCD; O88758; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000018364; ENSRNOP00000018364; ENSRNOG00000013681.
DR GeneID; 117023; -.
DR KEGG; rno:117023; -.
DR UCSC; RGD:621524; rat.
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; FGQEAEY; -.
DR OrthoDB; 818306at2759; -.
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 tissues.
DR Genevisible; O88758; RN.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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: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: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; 1.20.120.350; -; 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 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
