Swiss-Prot entry

ID   KCNE1_FELCA    STANDARD;      PRT;   129 AA.
AC   Q9XSP1;
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   Felis silvestris catus (Cat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; 
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Fissipedia; Felidae; 
OC   Felis. 
OX   NCBI_TaxID=9685;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Heart;
RA   Chen L.-S.K., Cuddy M.;
RT   "Cloning and expression of the cat delayed rectifier minK potassium
RT   channel.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
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; U62404; AAD41532.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
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; Q9XSP1.
DR   ProtoNet; Q9XSP1.
DR   ProtoMap; Q9XSP1.
DR   PRESAGE; Q9XSP1.
DR   DIP; Q9XSP1.
DR   ModBase; Q9XSP1.
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    129       Cytoplasmic (Potential).
FT   MOD_RES     102    102       Phosphoserine (by PKC) (By similarity).
FT   CARBOHYD      5      5       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     26     26       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   129 AA;  14505 MW;  F696A686CFF8DB95 CRC64;
     MILPNTTATT PFLNALWQGT AHQGGNTSGL ARRSPGGDDS QLEALYILMV LGFFGFFTLG
     IMLSYIRSKK LEHSHDPFNV YIESDTWQEK DKAYLQARVL ESYKACYVIE NQLAVERPNA
     HLPEIKPLS
//