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 08-MAY-2019, entry version 142. 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; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RC TISSUE=Heart; RX PubMed=1655403; 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 RT rectifier K+ 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. RT Characterization of multiple cDNAs and gene organization in the RT 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., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA 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., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA 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., RA 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 CC a voltage-gated potassium channel complex of pore-forming alpha CC subunits. Modulates the gating kinetics and enhances stability of CC the channel complex. Assembled with KCNB1 modulates the gating CC characteristics of the delayed rectifier voltage-dependent CC potassium channel KCNB1. Assembled with KCNQ1/KVLQT1 is proposed CC to form the slowly activating delayed rectifier cardiac potassium CC (IKs) channel. The outward current reaches its steady state only CC after 50 seconds. Assembled with KCNH2/HERG may modulate the CC rapidly activating component of the delayed rectifying potassium CC current in heart (IKr). {ECO:0000250|UniProtKB:P15382, CC ECO:0000250|UniProtKB:P15383}. CC -!- SUBUNIT: Interacts with KCNB1. Interacts with KCNC2 (By CC similarity). Associates with KCNH2/HERG. Interacts with KCNQ1; CC targets the complex KCNQ1-KCNE1 to the membrane raft (By CC similarity) (PubMed:8900282). {ECO:0000250|UniProtKB:P15382, CC ECO:0000250|UniProtKB:P15383, 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). CC {ECO:0000250|UniProtKB:P15382, 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. CC {ECO:0000250}. CC -!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and CC requires prior cotranslational glycosylation at Asn-5. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the potassium channel KCNE family. CC {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; 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 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 iPTMnet; P23299; -. DR PhosphoSitePlus; P23299; -. DR PaxDb; P23299; -. DR PRIDE; P23299; -. 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 eggNOG; ENOG410IY71; Eukaryota. DR eggNOG; ENOG410Y1SF; LUCA. DR GeneTree; ENSGT00940000154497; -. DR HOGENOM; HOG000113207; -. DR InParanoid; P23299; -. DR KO; K04894; -. DR OMA; ALYILMV; -. DR OrthoDB; 1452030at2759; -. DR PhylomeDB; P23299; -. DR TreeFam; TF335976; -. DR PRO; PR:P23299; -. DR Proteomes; UP000000589; Chromosome 16. DR Bgee; ENSMUSG00000039639; Expressed in 64 organ(s), highest expression level in stria vascularis of cochlear duct. DR ExpressionAtlas; P23299; baseline and differential. DR Genevisible; P23299; MM. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI. DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl. 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:0044325; F:ion channel binding; ISO:MGI. DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB. DR GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI. DR GO; GO:0071468; P:cellular response to acidic pH; 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:0086011; P:membrane repolarization during action potential; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI. DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IBA:GO_Central. DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; IBA:GO_Central. DR InterPro; IPR000369; K_chnl_KCNE. DR InterPro; IPR005424; K_chnl_volt-dep_bsu_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; Complete proteome; Direct protein sequencing; KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein; KW Potassium; Potassium channel; Potassium transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1 129 Potassium voltage-gated channel subfamily FT E member 1. FT /FTId=PRO_0000144279. FT TRANSMEM 44 66 Helical. {ECO:0000255}. FT TOPO_DOM 67 129 Cytoplasmic. {ECO:0000255}. FT MOD_RES 102 102 Phosphoserine; by PKC. {ECO:0000250}. FT CARBOHYD 5 5 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. FT CARBOHYD 7 7 O-linked (GalNAc...) threonine. FT {ECO:0000250}. FT CARBOHYD 26 26 N-linked (GlcNAc...) asparagine. FT {ECO:0000255}. SQ SEQUENCE 129 AA; 14578 MW; E66DF4742300E839 CRC64; MSLPNSTTVL PFLARLWQET AEQGGNVSGL ARKSQLRDDS KLEALYILMV LGFFGFFTLG IMLSYIRSKK LEHSHDPFNV YIESDAWQEK GKAVFQARVL ESFRACYVIE NQAAVEQPAT HLPELKPLS //