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 19-MAR-2014, entry version 107. 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; Sciurognathi; 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). 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 KCNQ1/KVLQT1 is proposed to CC 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) (By similarity). CC -!- SUBUNIT: Associates with KCNQ1/KVLQT1 and KCNH2/HERG (By CC similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane CC protein. CC -!- TISSUE SPECIFICITY: Restrictively localized in the apical membrane CC portion of epithelial cells. CC -!- PTM: Phosphorylation inhibits the potassium current (By CC similarity). CC -!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and CC requires prior cotranslational glycosylation at Asn-5 (By CC similarity). CC -!- SIMILARITY: Belongs to the potassium channel KCNE family. 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 PIR; S17307; S17307. DR RefSeq; NP_032450.1; NM_008424.3. DR RefSeq; XP_006523004.1; XM_006522941.1. DR UniGene; Mm.299425; -. DR ProteinModelPortal; P23299; -. DR SMR; P23299; 1-127. DR STRING; 10090.ENSMUSP00000052248; -. DR PhosphoSite; 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; NOG41824; -. DR HOGENOM; HOG000113207; -. DR HOVERGEN; HBG052226; -. DR InParanoid; P23299; -. DR KO; K04894; -. DR OMA; ALYILMV; -. DR OrthoDB; EOG7WMCMH; -. DR TreeFam; TF335976; -. DR NextBio; 289843; -. DR PRO; PR:P23299; -. DR ArrayExpress; P23299; -. DR Bgee; P23299; -. DR Genevestigator; P23299; -. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0009986; C:cell surface; IEA:Ensembl. DR GO; GO:0005783; C:endoplasmic reticulum; IEA:Ensembl. DR GO; GO:0005764; C:lysosome; IEA:Ensembl. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl. DR GO; GO:0030018; C:Z disc; IEA:Ensembl. DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IEA:Ensembl. DR GO; GO:0015459; F:potassium channel regulator activity; IEA:Ensembl. DR GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IEA:Ensembl. DR GO; GO:0071468; P:cellular response to acidity; IEA:Ensembl. DR GO; GO:0071320; P:cellular response to cAMP; 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:0090315; P:negative regulation of protein targeting to membrane; IEA:Ensembl. DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl. DR GO; GO:0071435; P:potassium ion export; IEA:Ensembl. DR GO; GO:0006487; P:protein N-linked glycosylation; ISS:UniProtKB. DR GO; GO:0006493; P:protein O-linked glycosylation; ISS:UniProtKB. DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IEA:Ensembl. 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; IEA:Ensembl. DR InterPro; IPR000369; K_chnl_volt-dep_bsu_KCNE. DR InterPro; IPR005424; K_chnl_volt-dep_bsu_KCNE1. DR PANTHER; PTHR17028; PTHR17028; 1. DR Pfam; PF02060; ISK_Channel; 1. DR PRINTS; PR01604; KCNE1CHANNEL. DR PRINTS; PR00168; KCNECHANNEL. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Glycoprotein; KW Ion channel; Ion transport; Membrane; Phosphoprotein; Potassium; KW 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; (Potential). FT TOPO_DOM 67 129 Cytoplasmic (Potential). FT MOD_RES 102 102 Phosphoserine; by PKC (By similarity). FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential). FT CARBOHYD 7 7 O-linked (GalNAc...) (By similarity). FT CARBOHYD 26 26 N-linked (GlcNAc...) (Potential). SQ SEQUENCE 129 AA; 14578 MW; E66DF4742300E839 CRC64; MSLPNSTTVL PFLARLWQET AEQGGNVSGL ARKSQLRDDS KLEALYILMV LGFFGFFTLG IMLSYIRSKK LEHSHDPFNV YIESDAWQEK GKAVFQARVL ESFRACYVIE NQAAVEQPAT HLPELKPLS //