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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   25-OCT-2017, entry version 130.
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;
OC   Mammalia; Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae;
OC   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
RT   gene 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
RT   atrial 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
CC       cAMP and subunit assembly. Mediates the rapidly activating
CC       component of the delayed rectifying potassium current in heart
CC       (IKr) (By similarity). {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
CC       and DNAJB14; chaperones DNAJB12 and DNAJB14 promote
CC       tetramerization (By similarity). Heteromultimer with KCNH6/ERG2
CC       and KCNH7/ERG3 (By similarity). Interacts with ALG10B (By
CC       similarity). Heteromultimer with KCNE1 and KCNE2. Interacts with
CC       CANX. The core-glycosylated, but not the fully glycosylated form
CC       interacts with RNF207. Interacts with NDFIP1 and NDFIP2 (By
CC       similarity). {ECO:0000250|UniProtKB:O08962,
CC       ECO:0000250|UniProtKB:Q12809}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in left and right atria of
CC       the heart, in cortex and hippocampus; detected at intermediate
CC       levels in left and right ventricle, Purkinje fibers, cerebellum,
CC       thalamus and basal ganglia; detected at low levels in liver,
CC       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
CC       every third position.
CC   -!- PTM: Phosphorylated on serine and threonine residues.
CC       {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}.
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   UniGene; Cfa.3625; -.
DR   ProteinModelPortal; Q9TSZ3; -.
DR   SMR; Q9TSZ3; -.
DR   STRING; 9615.ENSCAFP00000035370; -.
DR   BindingDB; Q9TSZ3; -.
DR   ChEMBL; CHEMBL3085616; -.
DR   PaxDb; Q9TSZ3; -.
DR   GeneID; 403761; -.
DR   KEGG; cfa:403761; -.
DR   CTD; 3757; -.
DR   eggNOG; KOG0498; Eukaryota.
DR   eggNOG; ENOG410XPSE; LUCA.
DR   HOGENOM; HOG000230793; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; Q9TSZ3; -.
DR   KO; K04905; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; 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   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 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   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; Complete proteome; Glycoprotein; Ion channel;
KW   Ion transport; Membrane; Methylation; Phosphoprotein; Potassium;
KW   Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1158       Potassium voltage-gated channel subfamily
FT                                H member 2.
FT                                /FTId=PRO_0000053997.
FT   TOPO_DOM      1    402       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    403    423       Helical; Name=Segment S1. {ECO:0000255}.
FT   TOPO_DOM    424    449       Extracellular. {ECO:0000255}.
FT   TRANSMEM    450    470       Helical; Name=Segment S2. {ECO:0000255}.
FT   TOPO_DOM    471    494       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    495    515       Helical; Name=Segment S3. {ECO:0000255}.
FT   TOPO_DOM    516    519       Extracellular. {ECO:0000255}.
FT   TRANSMEM    520    540       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000255}.
FT   TOPO_DOM    541    546       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    547    567       Helical; Name=Segment S5. {ECO:0000255}.
FT   TOPO_DOM    568    610       Extracellular. {ECO:0000255}.
FT   INTRAMEM    611    631       Pore-forming; Name=Segment H5.
FT                                {ECO:0000255}.
FT   TOPO_DOM    632    637       Extracellular. {ECO:0000255}.
FT   TRANSMEM    638    658       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    659   1158       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       17     88       PAS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN       92    144       PAC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00141}.
FT   NP_BIND     741    858       cNMP.
FT   MOTIF       623    628       Selectivity filter. {ECO:0000250}.
FT   COMPBIAS    296    299       Poly-Pro.
FT   MOD_RES     239    239       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12809}.
FT   MOD_RES     283    283       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35219}.
FT   MOD_RES     284    284       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35219}.
FT   MOD_RES     319    319       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12809}.
FT   MOD_RES     350    350       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O08962}.
FT   MOD_RES     870    870       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12809}.
FT   MOD_RES     873    873       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:O35219}.
FT   MOD_RES    1013   1013       Omega-N-methylarginine.
FT                                {ECO:0000250|UniProtKB:O35219}.
FT   MOD_RES    1136   1136       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:Q12809}.
FT   CARBOHYD    597    597       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CONFLICT    442    442       P -> T (in Ref. 2; AAC48722).
FT                                {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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