KCNS3_MOUSE
ID KCNS3_MOUSE Reviewed; 491 AA.
AC Q8BQZ8;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Potassium voltage-gated channel subfamily S member 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv9.3;
GN Name=Kcns3;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Potassium channel subunit that does not form functional
CC channels by itself. Can form functional heterotetrameric channels with
CC KCNB1; modulates the delayed rectifier voltage-gated potassium channel
CC activation and deactivation rates of KCNB1. Heterotetrameric channel
CC activity formed with KCNB1 show increased current amplitude with the
CC threshold for action potential activation shifted towards more negative
CC values in hypoxic-treated pulmonary artery smooth muscle cells.
CC {ECO:0000250|UniProtKB:O88759, ECO:0000250|UniProtKB:Q9BQ31}.
CC -!- SUBUNIT: Heterotetramer with KCNB1. Does not form homomultimers.
CC {ECO:0000250|UniProtKB:Q9BQ31}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9BQ31};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BQ31}. Note=May
CC not reach the plasma membrane but remain in an intracellular
CC compartment in the absence of KCNB1. {ECO:0000250|UniProtKB:Q9BQ31}.
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. Kv9.3/KCNS3 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; AK046054; BAC32583.1; -; mRNA.
DR EMBL; AK162957; BAE37134.1; -; mRNA.
DR EMBL; BC132164; AAI32165.1; -; mRNA.
DR EMBL; BC132464; AAI32465.1; -; mRNA.
DR CCDS; CCDS25813.1; -.
DR RefSeq; NP_001162036.1; NM_001168564.1.
DR RefSeq; NP_775593.1; NM_173417.3.
DR RefSeq; XP_006515143.1; XM_006515080.3.
DR RefSeq; XP_011242164.1; XM_011243862.1.
DR RefSeq; XP_011242165.1; XM_011243863.2.
DR RefSeq; XP_011242166.1; XM_011243864.1.
DR RefSeq; XP_011242167.1; XM_011243865.2.
DR RefSeq; XP_011242168.1; XM_011243866.2.
DR AlphaFoldDB; Q8BQZ8; -.
DR SMR; Q8BQZ8; -.
DR STRING; 10090.ENSMUSP00000060706; -.
DR PaxDb; Q8BQZ8; -.
DR PRIDE; Q8BQZ8; -.
DR Antibodypedia; 3102; 122 antibodies from 23 providers.
DR DNASU; 238076; -.
DR Ensembl; ENSMUST00000055673; ENSMUSP00000060706; ENSMUSG00000043673.
DR Ensembl; ENSMUST00000164495; ENSMUSP00000129412; ENSMUSG00000043673.
DR Ensembl; ENSMUST00000217974; ENSMUSP00000152026; ENSMUSG00000043673.
DR GeneID; 238076; -.
DR KEGG; mmu:238076; -.
DR UCSC; uc007nas.1; mouse.
DR CTD; 3790; -.
DR MGI; MGI:1098804; Kcns3.
DR VEuPathDB; HostDB:ENSMUSG00000043673; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000155979; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; Q8BQZ8; -.
DR OMA; EYICIGW; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q8BQZ8; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR Reactome; R-MMU-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
DR BioGRID-ORCS; 238076; 2 hits in 72 CRISPR screens.
DR PRO; PR:Q8BQZ8; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q8BQZ8; protein.
DR Bgee; ENSMUSG00000043673; Expressed in lumbar dorsal root ganglion and 58 other tissues.
DR Genevisible; Q8BQZ8; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central.
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:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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..491
FT /note="Potassium voltage-gated channel subfamily S member
FT 3"
FT /id="PRO_0000320143"
FT TOPO_DOM 1..182
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 183..204
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 205..220
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 221..243
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 244..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 255..275
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 276..285
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 286..306
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 307..321
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 322..343
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 344..357
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 358..369
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 370..377
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 378..384
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 385..413
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 414..491
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 370..375
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 491 AA; 55993 MW; B36B818126D439C5 CRC64;
MVFGEFFHRP GQDEELVNLN VGGFKQSVDQ STLLRFPHTR LGKLLTCHSE EAILELCDDY
SVADKEYYFD RNPFLFRYVL NFYYTGKLHV MEELCVFSFC QEIEYWGINE LFIDSCCSSR
YQERKEESHD KDWDQKSNDV STDSSFEESS LFEKELEKFD ELRFGQLRKK IWIRMENPAY
CLSAKLIAIS SLSVVLASIV AMCVHSMSEF QNEDGEVDDP VLEGVEIACI AWFTGELAIR
LVAAPSQKKF WKNPLNIIDF VSIIPFYATL AVDTKEEESE DIENMGKVVQ ILRLMRIFRI
LKLARHSVGL RSLGATLRHS YHEVGLLLLF LSVGISIFSV LIYSVEKDEH KSSLTSIPIC
WWWATISMTT VGYGDTHPVT LAGKIIASTC IICGILVVAL PITIIFNKFS KYYQKQKDME
VDQCSEDPPE KCHELPYFNI RDVYAQQVHA FITSLSSIGI VVSDPDSTDA SSVEDNEDAY
NTASLENCTG K
