KCNH2_PIG
ID KCNH2_PIG Reviewed; 97 AA.
AC Q9TUI4;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 2;
DE AltName: Full=Ether-a-go-go-related gene potassium channel 1;
DE Short=ERG-1;
DE Short=Eag-related protein 1;
DE Short=Ether-a-go-go-related protein 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
DE Flags: Fragment;
GN Name=KCNH2; Synonyms=ERG;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Heart;
RA Ohya S., Imaizumi Y.;
RT "Porcine eag-related gene (erg).";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly
CC rectifying potassium channel. Channel properties are modulated by cAMP
CC and subunit assembly. Mediates the rapidly activating component of the
CC delayed rectifying potassium current in heart (IKr) (By similarity).
CC {ECO:0000250|UniProtKB:Q12809}.
CC -!- SUBUNIT: The potassium channel is probably composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits. Interacts with DNAJB12 and
CC DNAJB14; chaperones DNAJB12 and DNAJB14 promote tetramerization (By
CC similarity). Heteromultimer with KCNH6/ERG2 and KCNH7/ERG3 (By
CC similarity). Interacts with ALG10B (By similarity). Heteromultimer with
CC KCNE1 and KCNE2. Interacts with CANX. The core-glycosylated, but not
CC the fully glycosylated form interacts with RNF207. Interacts with
CC NDFIP1 and NDFIP2 (By similarity). {ECO:0000250|UniProtKB:O08962,
CC ECO:0000250|UniProtKB:Q12809}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12809};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is
CC characterized by a series of positively charged amino acids at every
CC third position.
CC -!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
CC 1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB030030; BAA85106.1; -; mRNA.
DR AlphaFoldDB; Q9TUI4; -.
DR InParanoid; Q9TUI4; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0086011; P:membrane repolarization during action potential; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IBA:GO_Central.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
DR GO; GO:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IBA:GO_Central.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01463; EAGCHANLFMLY.
PE 2: Evidence at transcript level;
KW Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN <1..>97
FT /note="Potassium voltage-gated channel subfamily H member
FT 2"
FT /id="PRO_0000054001"
FT TRANSMEM 19..39
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..64
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 65..85
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT NON_TER 1
FT NON_TER 97
SQ SEQUENCE 97 AA; 10743 MW; 7F516B35B065AA8C CRC64;
LLKETEEGSQ APDCGYACQP LAVVDLIVDI MFIVDILINF RTTYVNANEE VVSHPGRIAV
HYFKGWFLID MVAAIPFDLL IFGSGSEELI GLLKTAR
