ID   KCNS2_MOUSE             Reviewed;         477 AA.
AC   O35174; Q543P3;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   24-JAN-2024, entry version 169.
DE   RecName: Full=Potassium voltage-gated channel subfamily S member 2;
DE   AltName: Full=Delayed-rectifier K(+) channel alpha subunit 2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv9.2;
GN   Name=Kcns2;
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.
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 MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Cerebellum, and Eye;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; 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 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. Expression was highest in the olfactory bulb, cerebral cortex,
CC       hippocampus, habenula, basolateral amygdaloid nuclei and cerebellum
CC       (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. Kv9.2/KCNS2 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; AF008574; AAB72051.1; -; mRNA.
DR   EMBL; AK048819; BAC33468.1; -; mRNA.
DR   EMBL; AK087481; BAC39892.1; -; mRNA.
DR   EMBL; BC059833; AAH59833.1; -; mRNA.
DR   CCDS; CCDS27421.1; -.
DR   RefSeq; NP_001258633.1; NM_001271704.1.
DR   RefSeq; NP_851834.1; NM_181317.4.
DR   AlphaFoldDB; O35174; -.
DR   SMR; O35174; -.
DR   BioGRID; 200920; 4.
DR   STRING; 10090.ENSMUSP00000072645; -.
DR   iPTMnet; O35174; -.
DR   PhosphoSitePlus; O35174; -.
DR   PaxDb; 10090-ENSMUSP00000072645; -.
DR   ProteomicsDB; 263420; -.
DR   ABCD; O35174; 1 sequenced antibody.
DR   Antibodypedia; 26073; 214 antibodies from 26 providers.
DR   DNASU; 16539; -.
DR   Ensembl; ENSMUST00000072868.5; ENSMUSP00000072645.4; ENSMUSG00000050963.8.
DR   Ensembl; ENSMUST00000228725.2; ENSMUSP00000153984.2; ENSMUSG00000050963.8.
DR   GeneID; 16539; -.
DR   KEGG; mmu:16539; -.
DR   UCSC; uc007vly.2; mouse.
DR   AGR; MGI:1197011; -.
DR   CTD; 3788; -.
DR   MGI; MGI:1197011; Kcns2.
DR   VEuPathDB; HostDB:ENSMUSG00000050963; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000160344; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; O35174; -.
DR   OMA; ETIPACW; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; O35174; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16539; 1 hit in 77 CRISPR screens.
DR   ChiTaRS; Kcns2; mouse.
DR   PRO; PR:O35174; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   RNAct; O35174; Protein.
DR   Bgee; ENSMUSG00000050963; Expressed in medial dorsal nucleus of thalamus and 91 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; 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: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   CDD; cd18427; BTB_POZ_KCNS2; 1.
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:SF60; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY S MEMBER 2; 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; O35174; 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..477
FT                   /note="Potassium voltage-gated channel subfamily S member
FT                   2"
FT                   /id="PRO_0000054085"
FT   TOPO_DOM        1..184
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        185..206
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        207..225
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        226..248
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        249..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        260..280
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        281..290
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        291..311
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        312..326
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        327..348
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        349..361
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        362..373
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        374..381
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        382..388
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        389..417
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        418..477
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   MOTIF           374..379
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
SQ   SEQUENCE   477 AA;  54289 MW;  C7AD7AA3AE312B2C CRC64;
     MTRQSLWDVS DTDVEDGEIR INVGGFKRRL RSHTLLRFPE TRLGRLLLCH SREAILELCD
     DYDDVQREFY FDRNPELFPY VLHFYHTGKL HVMAELCVFS FSQEIEYWGI NEFFIDSCCS
     YSYHGRKVEP EQEKWDEQSD QESTTSSFDE ILAFYNDASK FDGQPLGNFR RQLWLALDNP
     GYSVLSRVFS VLSILVVLGS IITMCLNSLP DFQIPDSQGN PGEDPRFEIV EHFGIAWFTF
     ELVARFAVAP DFLKFFKNAL NLIDLMSIVP FYITLVVNLV VESSPTLANL GRVAQVLRLM
     RIFRILKLAR HSTGLRSLGA TLKYSYKEVG LLLLYLSVGI SIFSVVAYTI EKEENEGLAT
     IPACWWWATV SMTTVGYGDV VPGTTAGKLT ASACILAGIL VVVLPITLIF NKFSHFYRRQ
     KQLESAMRSC DFGDGMKEVP SVNLRDYYAH KVKSLMASLT NMSRSSPSEL SLDDSLH
//