KCNE1_MOUSE
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 03-AUG-2022, entry version 155.
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 GlyGen; P23299; 3 sites.
DR iPTMnet; P23299; -.
DR PhosphoSitePlus; P23299; -.
DR PaxDb; P23299; -.
DR PRIDE; P23299; -.
DR ProteomicsDB; 263594; -.
DR DNASU; 16509; -.
DR Ensembl; ENSMUST00000051705; ENSMUSP00000052248; ENSMUSG00000039639.
DR Ensembl; ENSMUST00000166707; ENSMUSP00000130866; ENSMUSG00000039639.
DR GeneID; 16509; -.
DR KEGG; mmu:16509; -.
DR UCSC; uc007zza.1; mouse.
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; 1452030at2759; -.
DR PhylomeDB; P23299; -.
DR TreeFam; TF335976; -.
DR BioGRID-ORCS; 16509; 2 hits in 74 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 42 other tissues.
DR ExpressionAtlas; P23299; baseline and differential.
DR Genevisible; P23299; MM.
DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; 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:0086008; F:voltage-gated potassium channel activity involved in cardiac muscle cell action potential repolarization; ISO:MGI.
DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; 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:1903817; P:negative regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; ISO:MGI.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; ISO:MGI.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; 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:1902259; P:regulation of delayed rectifier potassium channel activity; ISO: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; PTHR15282; 1.
DR Pfam; PF02060; ISK_Channel; 1.
DR PRINTS; PR01604; KCNE1CHANNEL.
DR PRINTS; PR00168; KCNECHANNEL.
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
