Swiss-Prot entry
ID KCNE1_CAVPO STANDARD; PRT; 125 AA.
AC Q60409; Q9QVZ5;
DT 30-MAY-2000 (Rel. 39, Created)
DT 30-MAY-2000 (Rel. 39, Last sequence update)
DT 10-MAY-2005 (Rel. 47, Last annotation update)
DE Potassium voltage-gated channel subfamily E member 1 (IKs producing
DE slow voltage-gated potassium channel beta subunit Mink) (Minimal
DE potassium channel) (Delayed rectifier potassium channel subunit IsK).
GN Name=KCNE1;
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia;
OC Hystricognathi; Caviidae; Cavia.
OX NCBI_TaxID=10141;
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart;
RX MEDLINE=94089666; PubMed=8265583 [NCBI, ExPASy, EBI, Israel, Japan];
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
RT mediates species-specific responses to protein kinase C.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:11528-11532(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Heart muscle;
RX MEDLINE=94173910; PubMed=7510407 [NCBI, ExPASy, EBI, Israel, Japan];
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
RT enhanced 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
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: Type I membrane protein.
CC -!- PTM: Phosphorylation inhibits the potassium current (By
CC similarity).
CC -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC --------------------------------------------------------------------------
CC This Swiss-Prot entry is copyright. It is produced through a collaboration
CC between the Swiss Institute of Bioinformatics and the EMBL outstation -
CC the European Bioinformatics Institute. There are no restrictions on its
CC use as long as its content is in no way modified and this statement is not
CC removed.
CC --------------------------------------------------------------------------
DR EMBL; L20462; AAA72394.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR PIR; A49392; A49392.
DR PIR; I48146; I48146.
DR InterPro; IPR000369; ISK_Channel.
DR InterPro; IPR005424; KCNE_beta1.
DR InterPro; Graphical view of domain structure.
DR Pfam; PF02060; ISK_Channel; 1.
DR Pfam; Graphical view of domain structure.
DR PRINTS; PR01604; KCNE1CHANNEL.
DR PRINTS; PR00168; KCNECHANNEL.
DR ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR HOVERGEN [Family / Alignment / Tree]
DR BLOCKS; Q60409.
DR ProtoNet; Q60409.
DR ProtoMap; Q60409.
DR PRESAGE; Q60409.
DR DIP; Q60409.
DR ModBase; Q60409.
DR SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW Glycoprotein; Ion transport; Ionic channel; Phosphorylation;
KW Potassium; Potassium channel; Potassium transport; Transmembrane;
KW Transport; Voltage-gated channel.
FT TRANSMEM 44 66 Potential.
FT TOPO_DOM 67 125 Cytoplasmic (Potential).
FT CARBOHYD 5 5 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 26 26 N-linked (GlcNAc...) (Potential).
FT CONFLICT 15 17 TVW -> SVM (in Ref. 1).
SQ SEQUENCE 125 AA; 14266 MW; E5CB6843D9AB5E76 CRC64;
MILPNSTAVM PFLTTVWQGT VQPSSNASGL ARRSPLRDDG KLEALYILMV LGFFGFFTLG
IMLSYIRSKK LEHSHDPFNV YIESDTWQEK DKAFFQARVL ENCRSCCVIE NQLTVEQPNT
YLPEL
//