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Database: UniProt
Entry: KCNH2_CANLF
LinkDB: KCNH2_CANLF
Original site: KCNH2_CANLF 
ID   KCNH2_CANLF             Reviewed;        1158 AA.
AC   Q9TSZ3; O02719; O18820;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   02-DEC-2020, entry version 146.
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=DERG;
DE            Short=ERG-1;
DE            Short=Eag-related protein 1;
DE            Short=Ether-a-go-go-related protein 1;
DE            Short=c-ERG;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
GN   Name=KCNH2; Synonyms=CERG, ERG;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Heart;
RX   PubMed=11417212; DOI=10.1007/s004240100524;
RA   Zehelein J., Zhang W., Koenen M., Graf M., Heinemann S.H., Katus H.A.;
RT   "Molecular cloning and expression of cERG, the ether a go-go-related gene
RT   from canine myocardium.";
RL   Pflugers Arch. 442:188-191(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 407-566.
RC   TISSUE=Heart;
RX   PubMed=9012748; DOI=10.1161/01.res.80.2.261;
RA   Wymore R.S., Gintant G.A., Wymore R.T., Dixon J.E., McKinnon D.,
RA   Cohen I.S.;
RT   "Tissue and species distribution of mRNA for the IKr-like K+ channel,
RT   erg.";
RL   Circ. Res. 80:261-268(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 616-714.
RC   TISSUE=Heart atrium;
RX   PubMed=10205145; DOI=10.1161/01.res.84.7.776;
RA   Yue L., Melnyk P., Gaspo R., Wang Z., Nattel S.;
RT   "Molecular mechanisms underlying ionic remodeling in a dog model of atrial
RT   fibrillation.";
RL   Circ. Res. 84:776-784(1999).
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   -!- TISSUE SPECIFICITY: Highly expressed in left and right atria of the
CC       heart, in cortex and hippocampus; detected at intermediate levels in
CC       left and right ventricle, Purkinje fibers, cerebellum, thalamus and
CC       basal ganglia; detected at low levels in liver, spleen and kidney.
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   -!- PTM: Phosphorylated on serine and threonine residues. {ECO:0000250}.
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; AJ243344; CAB64868.1; -; mRNA.
DR   EMBL; U75213; AAC48722.1; -; mRNA.
DR   EMBL; AF017429; AAB70524.1; -; mRNA.
DR   RefSeq; NP_001003145.1; NM_001003145.1.
DR   BMRB; Q9TSZ3; -.
DR   SMR; Q9TSZ3; -.
DR   STRING; 9612.ENSCAFP00000035370; -.
DR   BindingDB; Q9TSZ3; -.
DR   ChEMBL; CHEMBL3085616; -.
DR   PaxDb; Q9TSZ3; -.
DR   Ensembl; ENSCAFT00030045812; ENSCAFP00030040025; ENSCAFG00030024832.
DR   Ensembl; ENSCAFT00040008538; ENSCAFP00040007416; ENSCAFG00040004496.
DR   GeneID; 403761; -.
DR   KEGG; cfa:403761; -.
DR   CTD; 3757; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   InParanoid; Q9TSZ3; -.
DR   OrthoDB; 247304at2759; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:1902937; C:inward rectifier potassium channel complex; IEA:Ensembl.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
DR   GO; GO:0055131; F:C3HC4-type RING finger domain binding; IEA:Ensembl.
DR   GO; GO:0005251; F:delayed rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0005242; F:inward rectifier potassium channel activity; IEA:Ensembl.
DR   GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR   GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR   GO; GO:1902282; F:voltage-gated potassium channel activity involved in ventricular cardiac muscle cell action potential repolarization; IEA:Ensembl.
DR   GO; GO:0035690; P:cellular response to drug; IEA:Ensembl.
DR   GO; GO:0086010; P:membrane depolarization during action potential; IEA:Ensembl.
DR   GO; GO:1903765; P:negative regulation of potassium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IEA:Ensembl.
DR   GO; GO:0097623; P:potassium ion export across plasma membrane; IEA:Ensembl.
DR   GO; GO:0055075; P:potassium ion homeostasis; IEA:Ensembl.
DR   GO; GO:1990573; P:potassium ion import across plasma membrane; IEA:Ensembl.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   GO; GO:0060307; P:regulation of ventricular cardiac muscle cell membrane repolarization; IEA:Ensembl.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.20.120.350; -; 1.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR018490; cNMP-bd-like.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
DR   InterPro; IPR003967; K_chnl_volt-dep_ERG.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR027359; Volt_channel_dom_sf.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01470; ERGCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF51206; SSF51206; 1.
DR   SUPFAM; SSF55785; SSF55785; 1.
DR   TIGRFAMs; TIGR00229; sensory_box; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Methylation; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN           1..1158
FT                   /note="Potassium voltage-gated channel subfamily H member
FT                   2"
FT                   /id="PRO_0000053997"
FT   TOPO_DOM        1..402
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        403..423
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..449
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        450..470
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        471..494
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        495..515
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        516..519
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        520..540
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        541..546
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        547..567
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        568..610
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   INTRAMEM        611..631
FT                   /note="Pore-forming; Name=Segment H5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        632..637
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        638..658
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        659..1158
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..88
FT                   /note="PAS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT   DOMAIN          92..144
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   NP_BIND         741..858
FT                   /note="cNMP"
FT   MOTIF           623..628
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        296..299
FT                   /note="Poly-Pro"
FT   MOD_RES         239
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12809"
FT   MOD_RES         283
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35219"
FT   MOD_RES         284
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35219"
FT   MOD_RES         319
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12809"
FT   MOD_RES         350
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O08962"
FT   MOD_RES         870
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12809"
FT   MOD_RES         873
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O35219"
FT   MOD_RES         1013
FT                   /note="Omega-N-methylarginine"
FT                   /evidence="ECO:0000250|UniProtKB:O35219"
FT   MOD_RES         1136
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q12809"
FT   CARBOHYD        597
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        442
FT                   /note="P -> T (in Ref. 2; AAC48722)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1158 AA;  126645 MW;  53C849032B4AA3D0 CRC64;
     MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM
     QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG
     AVIMFILNFE VVMEKDMVGS PTHDTNHRGP PTSWLAPGRA KTFRLKLPAL LALTTRESSA
     RPGGVGSAGA PGAVVVDVDL SPAVPSRESL ALDEVTAMDN HVAGLGPMEE QRALVGSSSP
     PAGAPEPLPS PRAHSLNPDA SGSSCSLART RSRESCASVR RASSADDIEA MRAGLPPPPR
     HASTGAMHPL RGGLLNSTSD SDLVRYRTIS KIPQITLNFV DLKGDPFLAS PTSDREIIAP
     KIKERTHNVT EKVTQVLSLG ADVLPEYKLQ APRIHRWTIL HYSPFKAVWD WLILLLVIYT
     AVFTPYSAAF LLKETEEGPP APDCGYACQP LAVVDFIVDI MFIVDILINF RTTYVNANEE
     VVSHPGRIAV HYFKGWFLID MVAAIPFDLL IFGSGSEELI GLLKTARLLR LVRVARKLDR
     YSEYGAAVLF LLMCTFALIA HWLACIWYAI GNMEQPHMDS RIGWLHNLGD QIGKPYNSSG
     LGGPSIKDKY VTALYFTFSS LTSVGFGNVS PNTNSEKIFS ICVMLIGSLM YASIFGNVSA
     IIQRLYSGTA RYHTQMLRVR EFIRFHQIPN PLRQRLEEYF QHAWSYTNGI DMNAVLKGFP
     ECLQADICLH LNRSLLQHCK PFRGATKGCL RALAMKFKTT HAPPGDTLVH AGDLLTALYF
     ISRGSIEILR GDVVVAILGK NDIFGEPLNL YARPGKSNGD VRALTYCDLH KIHRDDLLEV
     LDMYPEFSDH FWSSLEITFN LRDTNMIPGS PGSAELEGGF NRQRKRKLSF RRRTDRDPEQ
     PGEVSALGPG RAGAGPSGRG RPGGPWGESP SSGPSSPESS EDEGPGRSSS PLRLVPFSSP
     RPPGEPPGGE PLTEDGEKSS DTCNPLSGAF SGVSNIFSFW GDSRGHQYQE LPRCPAPTPS
     LLNIPLSSPC RRPRGDVEGR LDALQRQLNR LETRLSADMA TVLQLLQRQM TLIPPAYSAV
     TTPGPGPTST SSLLPVSPIP TLTLDSLSQV SQFMAFEELP PGAPELPQDG PPRRLSLPGQ
     LGALTSQPLH RHGSDPGS
//
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