Swiss-Prot entry

ID   KCNE2_CAVPO    STANDARD;      PRT;   123 AA.
AC   P63160; Q9WTW0;
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 2 (Minimum
DE   potassium ion channel-related peptide 1) (Potassium channel beta
DE   subunit MiRP1) (MinK-related peptide 1).
GN   Name=Kcne2;
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;
RA   Jiang M., Zhang M., Liu J., Tseng G.-N.;
RL   Submitted (AUG-2001) 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. Associated with KCNH2/HERG is proposed to
CC       form the rapidly activating component of the delayed rectifying
CC       potassium current in heart (IKr). May associate with KCNQ2 and/or
CC       KCNQ3 and modulate the native M-type current. May associate with
CC       KCNQ1/KCLQT1 and elicit a voltage-independent current (By
CC       similarity).
CC   -!- SUBUNIT: Associates with KCNH2/ERG1 (By similarity). May associate
CC       with KCNQ1/KVLQT1, KCNQ2 and KCNQ3. Associates with HCN1 and
CC       probably HCN2 (By similarity).
CC   -!- SUBCELLULAR LOCATION: Type I membrane protein.
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; AY050513; AAL13163.1; -; mRNA. [EMBL / GenBank / DDBJ] [CoDingSequence]
DR   InterPro; IPR000369; ISK_Channel.
DR   InterPro; IPR005425; KCNE_beta2.
DR   InterPro; Graphical view of domain structure.
DR   Pfam; PF02060; ISK_Channel; 1.
DR   Pfam; Graphical view of domain structure.
DR   PRINTS; PR01605; KCNE2CHANNEL.
DR   PRINTS; PR00168; KCNECHANNEL.
DR   ProDom [Domain structure / List of seq. sharing at least 1 domain]
DR   HOVERGEN [Family / Alignment / Tree]
DR   BLOCKS; P63160.
DR   ProtoNet; P63160.
DR   ProtoMap; P63160.
DR   PRESAGE; P63160.
DR   DIP; P63160.
DR   ModBase; P63160.
DR   SWISS-2DPAGE; GET REGION ON 2D PAGE.
KW   Glycoprotein; Ion transport; Ionic channel; Potassium;
KW   Potassium channel; Potassium transport; Transmembrane; Transport;
KW   Voltage-gated channel.
FT   TRANSMEM     49     69       Potential.
FT   TOPO_DOM     70    123       Cytoplasmic (Potential).
FT   CARBOHYD      6      6       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     29     29       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   123 AA;  14356 MW;  CB91870E7B1EB82A CRC64;
     MTTLANLTQT LEDAFKKVFI TYMDSWRRNT TAEQQALQAR VDAENFYYVI LYLMVMIGMF
     AFIVVAILVS TVKSKRREHS QDPYHQYIVE DWQQKYRSQI LHLEDSKATI HENLGATGFT
     VSP
//