KCNE2_CAVPO
ID KCNE2_CAVPO Reviewed; 123 AA.
AC P63160; Q9WTW0;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2004, sequence version 1.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=Potassium voltage-gated channel subfamily E member 2;
DE AltName: Full=MinK-related peptide 1;
DE AltName: Full=Minimum potassium ion channel-related peptide 1;
DE AltName: Full=Potassium channel subunit beta MiRP1;
GN Name=Kcne2;
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;
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 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 Associated with KCNH2/HERG is proposed to form the rapidly activating
CC component of the delayed rectifying potassium current in heart (IKr).
CC May associate with KCNQ2 and/or KCNQ3 and modulate the native M-type
CC current. May associate with HCN1 and HCN2 and increase potassium
CC current (By similarity). Interacts with KCNQ1; forms a heterooligomer
CC complex leading to currents with an apparently instantaneous
CC activation, a rapid deactivation process and a linear current-voltage
CC relationship and decreases the amplitude of the outward current (By
CC similarity). {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}.
CC -!- SUBUNIT: Interacts with KCNB1 (By similarity). Associates with
CC KCNH2/ERG1 (By similarity). May associate with KCNQ2 and KCNQ3 (By
CC similarity). Associates with HCN1 and probably HCN2 (By similarity).
CC Heteromultimer with KCNC2. Interacts with KCNC2 (By similarity).
CC Interacts with KCNQ1; forms a heterooligomer complex that targets to
CC the membrane raft and leading to currents with an apparently
CC instantaneous activation, a rapid deactivation process and a linear
CC current-voltage relationship and decreases the amplitude of the outward
CC current (By similarity). {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P63161,
CC ECO:0000250|UniProtKB:Q9Y6J6}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:P63161}. Note=Colocalizes with KCNB1 at the
CC plasma membrane. {ECO:0000250|UniProtKB:P63161}.
CC -!- SIMILARITY: Belongs to the potassium channel KCNE family.
CC {ECO:0000305}.
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DR EMBL; AY050513; AAL13163.1; -; mRNA.
DR AlphaFoldDB; P63160; -.
DR SMR; P63160; -.
DR InParanoid; P63160; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR InterPro; IPR000369; K_chnl_KCNE.
DR InterPro; IPR005425; K_chnl_volt-dep_bsu_KCNE2.
DR PANTHER; PTHR15282; PTHR15282; 1.
DR Pfam; PF02060; ISK_Channel; 1.
DR PRINTS; PR01605; KCNE2CHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..123
FT /note="Potassium voltage-gated channel subfamily E member
FT 2"
FT /id="PRO_0000144284"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 6
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 29
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 123 AA; 14356 MW; CB91870E7B1EB82A CRC64;
MTTLANLTQT LEDAFKKVFI TYMDSWRRNT TAEQQALQAR VDAENFYYVI LYLMVMIGMF
AFIVVAILVS TVKSKRREHS QDPYHQYIVE DWQQKYRSQI LHLEDSKATI HENLGATGFT
VSP