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 20-JAN-2016, entry version 123.
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).
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 KNCQ1-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 KNCQ1 (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}.
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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_006522941.2.
DR UniGene; Mm.299425; -.
DR ProteinModelPortal; P23299; -.
DR SMR; P23299; 1-127.
DR STRING; 10090.ENSMUSP00000052248; -.
DR iPTMnet; P23299; -.
DR PhosphoSite; 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 HOGENOM; HOG000113207; -.
DR HOVERGEN; HBG052226; -.
DR InParanoid; P23299; -.
DR KO; K04894; -.
DR OMA; ALYILMV; -.
DR OrthoDB; EOG7WMCMH; -.
DR PhylomeDB; P23299; -.
DR TreeFam; TF335976; -.
DR NextBio; 289843; -.
DR PRO; PR:P23299; -.
DR Proteomes; UP000000589; Chromosome 16.
DR Bgee; P23299; -.
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; IEA:Ensembl.
DR GO; GO:0005794; C:Golgi apparatus; 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:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
DR GO; GO:0071468; P:cellular response to acidic pH; 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:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
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:1901387; P:positive regulation of voltage-gated calcium channel activity; 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:0086091; P:regulation of heart rate by cardiac conduction; IMP:MGI.
DR InterPro; IPR000369; K_chnl_KCNE.
DR InterPro; IPR005424; K_chnl_volt-dep_bsu_KCNE1.
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...). {ECO:0000255}.
FT CARBOHYD 7 7 O-linked (GalNAc...). {ECO:0000250}.
FT CARBOHYD 26 26 N-linked (GlcNAc...). {ECO:0000255}.
SQ SEQUENCE 129 AA; 14578 MW; E66DF4742300E839 CRC64;
MSLPNSTTVL PFLARLWQET AEQGGNVSGL ARKSQLRDDS KLEALYILMV LGFFGFFTLG
IMLSYIRSKK LEHSHDPFNV YIESDAWQEK GKAVFQARVL ESFRACYVIE NQAAVEQPAT
HLPELKPLS
//