KCNE1_CAVPO
ID KCNE1_CAVPO Reviewed; 125 AA.
AC Q60409; Q9QVZ5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RX PubMed=8265583; DOI=10.1073/pnas.90.24.11528;
RA Varnum M.D., Busch A.E., Bond C.T., Maylie J., Adelman J.P.;
RT "The min K channel underlies the cardiac potassium current IKs and mediates
RT species-specific responses to protein kinase C.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11528-11532(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart muscle;
RX PubMed=7510407; DOI=10.1073/pnas.91.5.1766;
RA Zhang J., Jurkiewicz N.K., Folander K., Lazarides E., Salata J.J.,
RA Swanson R.;
RT "K+ currents expressed from the guinea pig cardiac IsK protein are enhanced
RT by activators of protein kinase C.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:1766-1770(1994).
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) (By similarity).
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).
CC {ECO:0000250|UniProtKB:P15382, ECO:0000250|UniProtKB:P15383,
CC ECO:0000250|UniProtKB:P23299}.
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 -!- 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; L20462; AAA72394.1; -; mRNA.
DR PIR; A49392; A49392.
DR PIR; I48146; I48146.
DR RefSeq; NP_001166443.1; NM_001172972.1.
DR AlphaFoldDB; Q60409; -.
DR SMR; Q60409; -.
DR STRING; 10141.ENSCPOP00000010090; -.
DR ChEMBL; CHEMBL5241; -.
DR Ensembl; ENSCPOT00000038529; ENSCPOP00000023836; ENSCPOG00000037389.
DR GeneID; 100135562; -.
DR KEGG; cpoc:100135562; -.
DR CTD; 3753; -.
DR eggNOG; ENOG502SG7D; Eukaryota.
DR GeneTree; ENSGT00940000154497; -.
DR HOGENOM; CLU_159026_0_0_1; -.
DR InParanoid; Q60409; -.
DR OMA; ESCRACY; -.
DR OrthoDB; 1452030at2759; -.
DR TreeFam; TF335976; -.
DR PRO; PR:Q60409; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000037389; Expressed in heart left ventricle and 8 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:Ensembl.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0031433; F:telethonin binding; IEA:Ensembl.
DR GO; GO:0071320; P:cellular response to cAMP; IEA:Ensembl.
DR GO; GO:0002070; P:epithelial cell maturation; IEA:Ensembl.
DR GO; GO:0098915; P:membrane repolarization during ventricular cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR GO; GO:0097623; P:potassium ion export across plasma membrane; IEA:Ensembl.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IEA:Ensembl.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR GO; GO:0033363; P:secretory granule organization; IEA:Ensembl.
DR GO; GO:0021750; P:vestibular nucleus development; IEA:Ensembl.
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 2: Evidence at transcript 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..125
FT /note="Potassium voltage-gated channel subfamily E member
FT 1"
FT /id="PRO_0000144276"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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 CONFLICT 15..17
FT /note="TVW -> SVM (in Ref. 1; no nucleotide entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 125 AA; 14266 MW; E5CB6843D9AB5E76 CRC64;
MILPNSTAVM PFLTTVWQGT VQPSSNASGL ARRSPLRDDG KLEALYILMV LGFFGFFTLG
IMLSYIRSKK LEHSHDPFNV YIESDTWQEK DKAFFQARVL ENCRSCCVIE NQLTVEQPNT
YLPEL
