KCNE1_RAT
ID KCNE1_RAT Reviewed; 130 AA.
AC P15383;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Potassium voltage-gated channel subfamily E member 1;
DE AltName: Full=Delayed rectifier potassium channel subunit IsK;
DE AltName: Full=IKs producing slow voltage-gated potassium channel subunit beta Mink;
DE AltName: Full=Minimal potassium channel;
GN Name=Kcne1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RX PubMed=3194754; DOI=10.1126/science.3194754;
RA Takumi T., Ohkubo H., Nakanishi S.;
RT "Cloning of a membrane protein that induces a slow voltage-gated potassium
RT current.";
RL Science 242:1042-1045(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=2183220; DOI=10.1073/pnas.87.8.2975;
RA Folander K., Smith J.S., Antanavage J., Bennett C., Stein R.B., Swanson R.;
RT "Cloning and expression of the delayed-rectifier IsK channel from neonatal
RT rat heart and diethylstilbestrol-primed rat uterus.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2975-2979(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE, INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Uterus;
RX PubMed=2344412; DOI=10.1016/0896-6273(90)90207-v;
RA Pragnell M., Snay K.J., Trimmer J.S., Maclusky N.J., Naftolin F.,
RA Kaczmarek L.K., Boyle M.B.;
RT "Estrogen induction of a small, putative K+ channel mRNA in rat uterus.";
RL Neuron 4:807-812(1990).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RX PubMed=2229022; DOI=10.1093/oxfordjournals.jbchem.a123181;
RA Iwai M., Masu M., Tsuchida K., Mori T., Ohkubo H., Nakanishi S.;
RT "Characterization of gene organization and generation of heterogeneous mRNA
RT species of rat ISK protein.";
RL J. Biochem. 108:200-206(1990).
RN [5]
RP MUTAGENESIS OF SER-103.
RX PubMed=1553557; DOI=10.1126/science.1553557;
RA Busch A.E., Varnum M.D., North R.A., Adelman J.P.;
RT "An amino acid mutation in a potassium channel that prevents inhibition by
RT protein kinase C.";
RL Science 255:1705-1707(1992).
RN [6]
RP MUTAGENESIS OF ASP-77.
RX PubMed=7605639; DOI=10.1016/0896-6273(95)90277-5;
RA Wang K.-W., Goldstein S.A.N.;
RT "Subunit composition of minK potassium channels.";
RL Neuron 14:1303-1309(1995).
RN [7]
RP SUBUNIT, INTERACTION WITH KCNC2, AND SUBCELLULAR LOCATION.
RX PubMed=14679187; DOI=10.1074/jbc.m310501200;
RA Lewis A., McCrossan Z.A., Abbott G.W.;
RT "MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
RT gating.";
RL J. Biol. Chem. 279:7884-7892(2004).
RN [8]
RP FUNCTION, INTERACTION WITH KCNB1, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=19219384; DOI=10.1007/s00232-009-9154-8;
RA McCrossan Z.A., Roepke T.K., Lewis A., Panaghie G., Abbott G.W.;
RT "Regulation of the Kv2.1 potassium channel by MinK and MiRP1.";
RL J. Membr. Biol. 228:1-14(2009).
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 (PubMed:19219384). Assembled with KCNQ1/KVLQT1 is proposed to form the
CC slowly activating delayed rectifier cardiac potassium (IKs) channel.
CC The outward current reaches its steady state only after 50 seconds.
CC Assembled with KCNH2/HERG may modulate the rapidly activating component
CC of the delayed rectifying potassium current in heart (IKr) (By
CC similarity). {ECO:0000250|UniProtKB:P15382,
CC ECO:0000269|PubMed:19219384}.
CC -!- SUBUNIT: Interacts with KCNB1 (PubMed:19219384). Interacts with KCNC2
CC (PubMed:14679187). Associates with KCNH2/HERG (By similarity).
CC Interacts with KCNQ1; targets the complex KCNQ1-KCNE1 to the membrane
CC raft (By similarity). {ECO:0000250|UniProtKB:P15382,
CC ECO:0000250|UniProtKB:P23299, ECO:0000269|PubMed:14679187,
CC ECO:0000269|PubMed:19219384}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14679187,
CC ECO:0000269|PubMed:19219384}; Single-pass type I membrane protein
CC {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:19219384}.
CC Membrane raft {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with
CC KCNB1 at the plasma membrane. Restrictively localized in the apical
CC membrane portion of epithelial cells. Targets to the membrane raft when
CC associated with KCNQ1 (By similarity). {ECO:0000250|UniProtKB:P15382,
CC ECO:0000269|PubMed:19219384}.
CC -!- TISSUE SPECIFICITY: Expressed in the heart (PubMed:2183220,
CC PubMed:19219384). Expressed in kidney (PubMed:2344412). Expressed in
CC estrogen-induced uterus (PubMed:2344412). {ECO:0000269|PubMed:19219384,
CC ECO:0000269|PubMed:2183220, ECO:0000269|PubMed:2344412}.
CC -!- INDUCTION: By estrogen. {ECO:0000269|PubMed:2344412}.
CC -!- PTM: Phosphorylation inhibits the potassium current.
CC -!- PTM: N-glycosylation at Asn-26 occurs post-translationally, and
CC requires prior cotranslational glycosylation at Asn-5. {ECO:0000250}.
CC -!- MISCELLANEOUS: Mutagenesis experiments were carried out by expressing
CC in Xenopus oocytes the mutant Asn-77 either individually
CC (homomultimers) or in combination with wild-type KCNE1
CC (heteromultimers) in a 1:1 ratio (PubMed:7605639).
CC {ECO:0000269|PubMed:7605639}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC {ECO:0000305}.
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DR EMBL; M22412; AAA41822.1; -; mRNA.
DR EMBL; M36461; AAA41098.1; -; mRNA.
DR EMBL; D10709; BAA01553.1; ALT_SEQ; Genomic_DNA.
DR PIR; A35633; A35633.
DR RefSeq; NP_037105.1; NM_012973.1.
DR RefSeq; XP_006248096.1; XM_006248034.3.
DR RefSeq; XP_006248097.1; XM_006248035.2.
DR RefSeq; XP_008766788.1; XM_008768566.2.
DR RefSeq; XP_017453375.1; XM_017597886.1.
DR RefSeq; XP_017453376.1; XM_017597887.1.
DR AlphaFoldDB; P15383; -.
DR SMR; P15383; -.
DR CORUM; P15383; -.
DR STRING; 10116.ENSRNOP00000002717; -.
DR TCDB; 8.A.10.1.1; the slow voltage-gated k+) channel accessory protein (mink) family.
DR GlyGen; P15383; 2 sites.
DR iPTMnet; P15383; -.
DR PhosphoSitePlus; P15383; -.
DR PaxDb; P15383; -.
DR Ensembl; ENSRNOT00000002717; ENSRNOP00000002717; ENSRNOG00000001984.
DR Ensembl; ENSRNOT00000096553; ENSRNOP00000086617; ENSRNOG00000001984.
DR Ensembl; ENSRNOT00000098014; ENSRNOP00000087251; ENSRNOG00000001984.
DR Ensembl; ENSRNOT00000114695; ENSRNOP00000092414; ENSRNOG00000001984.
DR GeneID; 25471; -.
DR KEGG; rno:25471; -.
DR UCSC; RGD:2956; rat.
DR CTD; 3753; -.
DR RGD; 2956; Kcne1.
DR eggNOG; ENOG502SG7D; Eukaryota.
DR GeneTree; ENSGT00940000154497; -.
DR HOGENOM; CLU_159026_0_0_1; -.
DR InParanoid; P15383; -.
DR OMA; ESCRACY; -.
DR OrthoDB; 1452030at2759; -.
DR PhylomeDB; P15383; -.
DR TreeFam; TF335976; -.
DR PRO; PR:P15383; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001984; Expressed in pancreas and 5 other tissues.
DR Genevisible; P15383; RN.
DR GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:RGD.
DR GO; GO:0030018; C:Z disc; IDA:BHF-UCL.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IMP:RGD.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0031433; F:telethonin binding; ISO:RGD.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:RGD.
DR GO; GO:0086002; P:cardiac muscle cell action potential involved in contraction; ISO:RGD.
DR GO; GO:0071468; P:cellular response to acidic pH; IDA:RGD.
DR GO; GO:0071320; P:cellular response to cAMP; ISO:RGD.
DR GO; GO:0071482; P:cellular response to light stimulus; IEP:RGD.
DR GO; GO:0002070; P:epithelial cell maturation; ISO:RGD.
DR GO; GO:0060047; P:heart contraction; ISO:RGD.
DR GO; GO:0008584; P:male gonad development; IEP:RGD.
DR GO; GO:0086009; P:membrane repolarization; ISO:RGD.
DR GO; GO:0086011; P:membrane repolarization during action potential; ISO:RGD.
DR GO; GO:0086013; P:membrane repolarization during cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0090315; P:negative regulation of protein targeting to membrane; IDA:RGD.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IDA:RGD.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
DR GO; GO:1901387; P:positive regulation of voltage-gated calcium channel activity; IDA:RGD.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IMP:RGD.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; ISO:RGD.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISO:RGD.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; ISO:RGD.
DR GO; GO:0033363; P:secretory granule organization; ISO:RGD.
DR GO; GO:0086005; P:ventricular cardiac muscle cell action potential; ISO:RGD.
DR GO; GO:0021750; P:vestibular nucleus development; ISO:RGD.
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; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..130
FT /note="Potassium voltage-gated channel subfamily E member
FT 1"
FT /id="PRO_0000144283"
FT TRANSMEM 45..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..130
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 103
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000305"
FT CARBOHYD 5
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 26
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 77
FT /note="D->N: No current (homomultimers); one fourth of the
FT WT current (heteromultimers)."
FT /evidence="ECO:0000269|PubMed:7605639"
FT MUTAGEN 103
FT /note="S->A: Abolishes inhibition by phosphorylation."
FT /evidence="ECO:0000269|PubMed:1553557"
SQ SEQUENCE 130 AA; 14699 MW; 76717E7ED73C5E4D CRC64;
MALSNSTTVL PFLASLWQET DEPGGNMSAD LARRSQLRDD SKLEALYILM VLGFFGFFTL
GIMLSYIRSK KLEHSHDPFN VYIESDAWQE KGKALFQARV LESFRACYVI ENQAAVEQPA
THLPELKPLS
