KCNE1_PONAB
ID KCNE1_PONAB Reviewed; 129 AA.
AC Q5R8Q2;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=Potassium voltage-gated channel subfamily E member 1;
GN Name=KCNE1;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Heart;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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).
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; CR859699; CAH91858.1; -; mRNA.
DR RefSeq; NP_001126076.1; NM_001132604.1.
DR AlphaFoldDB; Q5R8Q2; -.
DR SMR; Q5R8Q2; -.
DR STRING; 9601.ENSPPYP00000012714; -.
DR PRIDE; Q5R8Q2; -.
DR GeneID; 100173028; -.
DR KEGG; pon:100173028; -.
DR CTD; 3753; -.
DR eggNOG; ENOG502SG7D; Eukaryota.
DR InParanoid; Q5R8Q2; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
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:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
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..129
FT /note="Potassium voltage-gated channel subfamily E member
FT 1"
FT /id="PRO_0000144281"
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 67..129
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 102
FT /note="Phosphoserine; by PKC"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 129 AA; 14568 MW; 32F043C431E61ABB CRC64;
MILSNTTAVT PFLTKLWQET VQQGGNVSGL ARRSPRSDDG KLEALYVLMV LGFFGFFTLG
IMLSYIRSKK LEHSNDPFNV YIESDAWQEK DKAYVQARVL KSYRACYVVE NHLAVEQPNT
HLPGTKPSP