KCNS1_MOUSE
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 03-AUG-2022, entry version 157.
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 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; 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 PhosphoSitePlus; O35173; -.
DR PaxDb; O35173; -.
DR PRIDE; O35173; -.
DR ProteomicsDB; 263504; -.
DR ABCD; O35173; 1 sequenced antibody.
DR Antibodypedia; 27521; 60 antibodies from 20 providers.
DR DNASU; 16538; -.
DR Ensembl; ENSMUST00000045196; ENSMUSP00000038901; ENSMUSG00000040164.
DR GeneID; 16538; -.
DR KEGG; mmu:16538; -.
DR UCSC; uc008ntv.1; mouse.
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; FGQEAEY; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; O35173; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16538; 2 hits in 72 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 32 other tissues.
DR Genevisible; O35173; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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: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; 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; 1.20.120.350; -; 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 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
