ID   KCNE1_MOUSE             Reviewed;         129 AA.
AC   P23299;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   24-JAN-2024, entry version 161.
DE   RecName: Full=Potassium voltage-gated channel subfamily E member 1;
DE   AltName: Full=Delayed rectifier potassium channel subunit IsK;
DE            Short=mISK;
DE   AltName: Full=IKs producing slow voltage-gated potassium channel subunit beta Mink;
DE   AltName: Full=Minimal potassium channel;
GN   Name=Kcne1;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   TISSUE=Heart;
RX   PubMed=1655403; DOI=10.1002/j.1460-2075.1991.tb07829.x;
RA   Honore E., Attali B., Romey G., Heurteaux C., Ricard P., Lesage F.,
RA   Lazdunski M., Barhanin J.;
RT   "Cloning, expression, pharmacology and regulation of a delayed rectifier K+
RT   channel in mouse heart.";
RL   EMBO J. 10:2805-2811(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=1568475; DOI=10.1016/0014-5793(92)81240-m;
RA   Lesage F., Attali B., Lazdunski M., Barhanin J.;
RT   "ISK, a slowly activating voltage-sensitive K+ channel. Characterization of
RT   multiple cDNAs and gene organization in the mouse.";
RL   FEBS Lett. 301:168-172(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Skin;
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   [4]
RP   INTERACTION WITH KCNQ1.
RC   TISSUE=Heart;
RX   PubMed=8900282; DOI=10.1038/384078a0;
RA   Barhanin J., Lesage F., Guillemare E., Fink M., Lazdunski M., Romey G.;
RT   "K(V)LQT1 and IsK (minK) proteins associate to form the I(Ks) cardiac
RT   potassium current.";
RL   Nature 384:78-80(1996).
CC   -!- FUNCTION: Ancillary protein that assembles as a beta subunit with a
CC       voltage-gated potassium channel complex of pore-forming alpha subunits.
CC       Modulates the gating kinetics and enhances stability of the channel
CC       complex. Assembled with KCNB1 modulates the gating characteristics of
CC       the delayed rectifier voltage-dependent potassium channel KCNB1.
CC       Assembled with KCNQ1/KVLQT1 is proposed to form the slowly activating
CC       delayed rectifier cardiac potassium (IKs) channel. The outward current
CC       reaches its steady state only after 50 seconds. Assembled with
CC       KCNH2/HERG may modulate the rapidly activating component of the delayed
CC       rectifying potassium current in heart (IKr).
CC       {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383}.
CC   -!- SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By similarity).
CC       Associates with KCNH2/HERG. Interacts with KCNQ1; targets the complex
CC       KCNQ1-KCNE1 to the membrane raft (By similarity) (PubMed:8900282).
CC       {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383,
CC       ECO:0000269|PubMed:8900282}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15382,
CC       ECO:0000250|UniProtKB:P15383}; Single-pass type I membrane protein
CC       {ECO:0000250|UniProtKB:P15382}. Apical cell membrane
CC       {ECO:0000250|UniProtKB:P15383}. Membrane raft
CC       {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with KCNB1 at the
CC       plasma membrane (By similarity). Targets to the membrane raft when
CC       associated with KCNQ1 (By similarity). {ECO:0000250|UniProtKB:P15382,
CC       ECO:0000250|UniProtKB:P15383}.
CC   -!- TISSUE SPECIFICITY: Restrictively localized in the apical membrane
CC       portion of epithelial cells.
CC   -!- PTM: Phosphorylation inhibits the potassium current. {ECO:0000250}.
CC   -!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and
CC       requires prior cotranslational glycosylation at Asn-5. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC       {ECO:0000305}.
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DR   EMBL; X60457; CAA42990.1; -; mRNA.
DR   EMBL; AK028907; BAC26189.1; -; mRNA.
DR   CCDS; CCDS28336.1; -.
DR   PIR; S17307; S17307.
DR   RefSeq; NP_032450.1; NM_008424.3.
DR   RefSeq; XP_006523004.1; XM_006522941.3.
DR   AlphaFoldDB; P23299; -.
DR   SMR; P23299; -.
DR   ComplexPortal; CPX-3198; Voltage-gated potassium channel complex variant 1.
DR   ComplexPortal; CPX-3274; KCNQ1-KCNE1 I(Ks) channel complex.
DR   STRING; 10090.ENSMUSP00000052248; -.
DR   GlyCosmos; P23299; 3 sites, No reported glycans.
DR   GlyGen; P23299; 3 sites.
DR   PhosphoSitePlus; P23299; -.
DR   PaxDb; 10090-ENSMUSP00000052248; -.
DR   ProteomicsDB; 263594; -.
DR   DNASU; 16509; -.
DR   Ensembl; ENSMUST00000051705.7; ENSMUSP00000052248.6; ENSMUSG00000039639.8.
DR   Ensembl; ENSMUST00000166707.3; ENSMUSP00000130866.2; ENSMUSG00000039639.8.
DR   GeneID; 16509; -.
DR   KEGG; mmu:16509; -.
DR   UCSC; uc007zza.1; mouse.
DR   AGR; MGI:96673; -.
DR   CTD; 3753; -.
DR   MGI; MGI:96673; Kcne1.
DR   VEuPathDB; HostDB:ENSMUSG00000039639; -.
DR   eggNOG; ENOG502SG7D; Eukaryota.
DR   GeneTree; ENSGT00940000154497; -.
DR   HOGENOM; CLU_159026_0_0_1; -.
DR   InParanoid; P23299; -.
DR   OMA; ESCRACY; -.
DR   OrthoDB; 5320042at2759; -.
DR   PhylomeDB; P23299; -.
DR   TreeFam; TF335976; -.
DR   BioGRID-ORCS; 16509; 2 hits in 79 CRISPR screens.
DR   PRO; PR:P23299; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; P23299; Protein.
DR   Bgee; ENSMUSG00000039639; Expressed in stria vascularis of cochlear duct and 44 other cell types or tissues.
DR   ExpressionAtlas; P23299; baseline and differential.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR   GO; GO:0009986; C:cell surface; ISO:MGI.
DR   GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISO:MGI.
DR   GO; GO:0030018; C:Z disc; ISO:MGI.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0031433; F:telethonin binding; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:MGI.
DR   GO; GO:0071468; P:cellular response to acidic pH; ISO:MGI.
DR   GO; GO:0071320; P:cellular response to cAMP; ISO:MGI.
DR   GO; GO:0071482; P:cellular response to light stimulus; IEA:Ensembl.
DR   GO; GO:0002070; P:epithelial cell maturation; IMP:MGI.
DR   GO; GO:0060047; P:heart contraction; IMP:MGI.
DR   GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR   GO; GO:0086009; P:membrane repolarization; ISO:MGI.
DR   GO; GO:0086011; P:membrane repolarization during action potential; ISO:MGI.
DR   GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR   GO; GO:0090315; P:negative regulation of protein targeting to membrane; ISO:MGI.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IMP:MGI.
DR   GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:MGI.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:MGI.
DR   GO; GO:0033363; P:secretory granule organization; IMP:MGI.
DR   GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:MGI.
DR   GO; GO:0021750; P:vestibular nucleus development; IMP:MGI.
DR   InterPro; IPR000369; K_chnl_KCNE.
DR   InterPro; IPR005424; KCNE1.
DR   PANTHER; PTHR15282:SF11; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY E MEMBER 1; 1.
DR   PANTHER; PTHR15282; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY E MEMBER 1, 3; 1.
DR   Pfam; PF02060; ISK_Channel; 1.
DR   PRINTS; PR01604; KCNE1CHANNEL.
DR   PRINTS; PR00168; KCNECHANNEL.
DR   Genevisible; P23299; MM.
PE   1: Evidence at protein level;
KW   Cell membrane; Direct protein sequencing; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..129
FT                   /note="Potassium voltage-gated channel subfamily E member
FT                   1"
FT                   /id="PRO_0000144279"
FT   TRANSMEM        44..66
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        67..129
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         102
FT                   /note="Phosphoserine; by PKC"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        5
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        7
FT                   /note="O-linked (GalNAc...) threonine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   129 AA;  14578 MW;  E66DF4742300E839 CRC64;
     MSLPNSTTVL PFLARLWQET AEQGGNVSGL ARKSQLRDDS KLEALYILMV LGFFGFFTLG
     IMLSYIRSKK LEHSHDPFNV YIESDAWQEK GKAVFQARVL ESFRACYVIE NQAAVEQPAT
     HLPELKPLS
//