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Potassium voltage-gated channel subfamily H member 2 (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (RERG) (r-ERG) (Voltage-gated potassium channel subunit Kv11.1)

 KCNH2_RAT               Reviewed;        1163 AA.
O08962; O08720;
28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
23-MAY-2018, entry version 150.
RecName: Full=Potassium voltage-gated channel subfamily H member 2;
AltName: Full=Ether-a-go-go-related gene potassium channel 1;
Short=ERG-1;
Short=Eag-related protein 1;
Short=Ether-a-go-go-related protein 1;
Short=RERG;
Short=r-ERG;
AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
Name=Kcnh2; Synonyms=Erg;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain cortex;
PubMed=9664620;
Bauer C.K., Engeland B., Wulfsen I., Ludwig J., Pongs O.,
Schwarz J.R.;
"RERG is a molecular correlate of the inward-rectifying K current in
clonal rat pituitary cells.";
Recept. Channels 6:19-29(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] OF 409-568.
PubMed=9012748; DOI=10.1161/01.RES.80.2.261;
Wymore R.S., Gintant G.A., Wymore R.T., Dixon J.E., McKinnon D.,
Cohen I.S.;
"Tissue and species distribution of mRNA for the IKr-like K+ channel,
erg.";
Circ. Res. 80:261-268(1997).
[3]
TISSUE SPECIFICITY.
PubMed=10718922; DOI=10.1046/j.1365-2826.2000.00447.x;
Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R.;
"Expression of mRNA for voltage-dependent and inward-rectifying K
channels in GH3/B6 cells and rat pituitary.";
J. Neuroendocrinol. 12:263-272(2000).
[4]
INTERACTION WITH KCNH6 AND KCNH7, AND MUTAGENESIS OF GLY-630.
PubMed=11212207; DOI=10.1007/s004240000467;
Wimmers S., Wulfsen I., Bauer C.K., Schwarz J.R.;
"Erg1, erg2 and erg3 K channel subunits are able to form
heteromultimers.";
Pflugers Arch. 441:450-455(2001).
[5]
INTERACTION WITH ALG10B.
PubMed=14525949; DOI=10.1096/fj.02-1057fje;
Kupershmidt S., Yang I.C.-H., Hayashi K., Wei J., Chanthaphaychith S.,
Petersen C.I., Johns D.C., George A.L. Jr., Roden D.M., Balser J.R.;
"The IKr drug response is modulated by KCR1 in transfected cardiac and
noncardiac cell lines.";
FASEB J. 17:2263-2265(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-285; SER-286 AND
SER-353, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated inwardly
rectifying potassium channel. Channel properties are modulated by
cAMP and subunit assembly. Mediates the rapidly activating
component of the delayed rectifying potassium current in heart
(IKr) (By similarity). {ECO:0000250|UniProtKB:Q12809}.
-!- SUBUNIT: The potassium channel is probably composed of a homo- or
heterotetrameric complex of pore-forming alpha subunits that can
associate with modulating beta subunits (By similarity). Interacts
with DNAJB12 and DNAJB14; chaperones DNAJB12 and DNAJB14 promote
tetramerization (By similarity). Heteromultimer with KCNH6/ERG2
and KCNH7/ERG3 (PubMed:11212207). Interacts with ALG10B
(PubMed:14525949). Heteromultimer with KCNE1 and KCNE2 (By
similarity). Interacts with CANX (By similarity). The core-
glycosylated, but not the fully glycosylated form interacts with
RNF207 (By similarity). Interacts with NDFIP1 and NDFIP2 (By
similarity). {ECO:0000250|UniProtKB:Q12809,
ECO:0000269|PubMed:11212207, ECO:0000269|PubMed:14525949}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q12809}; Multi-pass membrane protein
{ECO:0000255}.
-!- TISSUE SPECIFICITY: Highly expressed in brain and testis, slightly
less so in heart, adrenal, retina and thymus. Detected at lower
levels in lung, soleus, tibialis, and at very low levels in cornea
and lens. A shorter transcript is detected in skeletal muscle.
Found in pituitary. {ECO:0000269|PubMed:10718922}.
-!- DOMAIN: The segment S4 is probably the voltage-sensor and is
characterized by a series of positively charged amino acids at
every third position.
-!- PTM: Phosphorylated on serine and threonine residues.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
1.A.1.20) subfamily. Kv11.1/KCNH2 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Z96106; CAB09536.1; -; mRNA.
EMBL; U75210; AAC53160.1; -; mRNA.
RefSeq; NP_446401.1; NM_053949.1.
UniGene; Rn.10970; -.
ProteinModelPortal; O08962; -.
SMR; O08962; -.
BioGrid; 250619; 1.
IntAct; O08962; 1.
STRING; 10116.ENSRNOP00000013800; -.
GuidetoPHARMACOLOGY; 572; -.
iPTMnet; O08962; -.
PhosphoSitePlus; O08962; -.
PaxDb; O08962; -.
PRIDE; O08962; -.
GeneID; 117018; -.
KEGG; rno:117018; -.
CTD; 3757; -.
RGD; 621414; Kcnh2.
eggNOG; KOG0498; Eukaryota.
eggNOG; ENOG410XPSE; LUCA.
HOGENOM; HOG000230793; -.
HOVERGEN; HBG052232; -.
InParanoid; O08962; -.
KO; K04905; -.
PhylomeDB; O08962; -.
PRO; PR:O08962; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:RGD.
GO; GO:0005216; F:ion channel activity; IDA:RGD.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
GO; GO:0005267; F:potassium channel activity; IDA:RGD.
GO; GO:0097110; F:scaffold protein binding; IPI:BHF-UCL.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:RGD.
GO; GO:0007420; P:brain development; IEP:RGD.
GO; GO:0006813; P:potassium ion transport; IDA:RGD.
GO; GO:0051291; P:protein heterooligomerization; IDA:RGD.
GO; GO:0086091; P:regulation of heart rate by cardiac conduction; IBA:GO_Central.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0042391; P:regulation of membrane potential; IDA:RGD.
GO; GO:0021510; P:spinal cord development; IEP:RGD.
CDD; cd00038; CAP_ED; 1.
CDD; cd00130; PAS; 1.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR018490; cNMP-bd-like.
InterPro; IPR000595; cNMP-bd_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
InterPro; IPR003967; K_chnl_volt-dep_ERG.
InterPro; IPR001610; PAC.
InterPro; IPR000014; PAS.
InterPro; IPR000700; PAS-assoc_C.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR027359; Volt_channel_dom_sf.
Pfam; PF00027; cNMP_binding; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF13426; PAS_9; 1.
PRINTS; PR01463; EAGCHANLFMLY.
PRINTS; PR01470; ERGCHANNEL.
SMART; SM00100; cNMP; 1.
SMART; SM00086; PAC; 1.
SUPFAM; SSF51206; SSF51206; 1.
SUPFAM; SSF55785; SSF55785; 1.
TIGRFAMs; TIGR00229; sensory_box; 1.
PROSITE; PS50042; CNMP_BINDING_3; 1.
PROSITE; PS50113; PAC; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Glycoprotein; Ion channel;
Ion transport; Membrane; Methylation; Phosphoprotein; Potassium;
Potassium channel; Potassium transport; Reference proteome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 1163 Potassium voltage-gated channel subfamily
H member 2.
/FTId=PRO_0000054003.
TOPO_DOM 1 405 Cytoplasmic. {ECO:0000255}.
TRANSMEM 406 426 Helical; Name=Segment S1. {ECO:0000255}.
TOPO_DOM 427 452 Extracellular. {ECO:0000255}.
TRANSMEM 453 473 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 474 497 Cytoplasmic. {ECO:0000255}.
TRANSMEM 498 518 Helical; Name=Segment S3. {ECO:0000255}.
TOPO_DOM 519 522 Extracellular. {ECO:0000255}.
TRANSMEM 523 543 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 544 549 Cytoplasmic. {ECO:0000255}.
TRANSMEM 550 570 Helical; Name=Segment S5. {ECO:0000255}.
TOPO_DOM 571 613 Extracellular. {ECO:0000255}.
INTRAMEM 614 634 Pore-forming; Name=Segment H5.
{ECO:0000255}.
TOPO_DOM 635 640 Extracellular. {ECO:0000255}.
TRANSMEM 641 661 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 662 1163 Cytoplasmic. {ECO:0000255}.
DOMAIN 17 88 PAS. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 92 144 PAC. {ECO:0000255|PROSITE-
ProRule:PRU00141}.
NP_BIND 744 861 cNMP.
MOTIF 626 631 Selectivity filter. {ECO:0000250}.
MOD_RES 239 239 Phosphoserine.
{ECO:0000250|UniProtKB:Q12809}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000250|UniProtKB:O35219}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 286 286 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 322 322 Phosphoserine.
{ECO:0000250|UniProtKB:Q12809}.
MOD_RES 353 353 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000250|UniProtKB:Q12809}.
MOD_RES 876 876 Phosphoserine.
{ECO:0000250|UniProtKB:O35219}.
MOD_RES 1018 1018 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:O35219}.
MOD_RES 1141 1141 Phosphoserine.
{ECO:0000250|UniProtKB:Q12809}.
CARBOHYD 600 600 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
MUTAGEN 630 630 G->S: Dominant negative mutant; abolishes
ERG current.
{ECO:0000269|PubMed:11212207}.
CONFLICT 411 411 V -> A (in Ref. 2; AAC53160).
{ECO:0000305}.
SEQUENCE 1163 AA; 126952 MW; F0D75B0B532D9EA2 CRC64;
MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM
QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG
AVIMFILNFE VVMEKDMVGS PAHDTNHRGP STSWLASGRA KTFRLKLPAL LALTARESPM
RTGSTGSPGA PGAVVVDVDL TPAAPSSESL ALDEVSAMDN HVAGLGPAEE RRALVGPASA
SPVASIPGPH PSPRAQSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPL
PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI
IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV
IYTAVFTPYS AAFLLKETED GSQAPDCGYA CQPLAVVDLL VDIMFIVDIL INFRTTYVNA
NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK
LDRYSEYGAA VLFLLMCTFA LIAHWLACIW YAIGNMEQPH MDSHIGWLHN LGDQIGKPYN
SSGLGGPSIK DKYVTALYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN
VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK
GFPECLQADI CLHLNRSLLQ HCKPFRGATK GCLRALAMKF KTTHAPPGDT LVHAGDLLTA
LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL
LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPSSAELE SGFNRQRKRK LSFRRRTDKD
TEQPGEVSAL GQGPARVGPG PSCRGQPGGP WGESPSSGPS SPESSEDEGP GRSSSPLRLV
PFSSPRPPGD SPGGEPLTED GEKSSDTCNP LSGAFSGVSN IFSFWGDSRG RQYQELPRCP
APAPSLLNIP LSSPGRRSRG DVESRLDALQ RQLNRLETRL SADMATVLQL LQRQMTLVPP
AYSAVTTPGP GPTSTSPLLP VGPVPTLTLD SLSQVSQFVA FEELPAGAPE LPQDGPTRRL
SLPGQLGALT SQPLHRHGSD PGS


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