KCNH2_RABIT
ID KCNH2_RABIT Reviewed; 1161 AA.
AC Q8WNY2; O02731; O19119; O97586; Q9TV06;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2002, sequence version 3.
DT 03-AUG-2022, entry version 133.
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 Short=RERG;
DE Short=ra-erg;
DE AltName: Full=Voltage-gated potassium channel subunit Kv11.1;
GN Name=KCNH2; Synonyms=ERG;
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE (ISOFORMS 1 AND 2).
RA Witchel H.J., Hancox J.C., Levi A.J., Meech R.W.;
RT "RERG -- rabbit ventricular ERG K+ channel subunit.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 411-571 (ISOFORMS 1/2).
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).
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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WNY2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WNY2-2; Sequence=VSP_000971;
CC -!- TISSUE SPECIFICITY: Detected in heart, both in atrium and in left
CC ventricle.
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; U87513; AAB68612.1; -; mRNA.
DR EMBL; AF068736; AAC99425.1; -; mRNA.
DR EMBL; AF105061; AAD39357.1; -; Genomic_DNA.
DR EMBL; U75212; AAC48723.1; -; mRNA.
DR RefSeq; NP_001075853.1; NM_001082384.1. [Q8WNY2-2]
DR AlphaFoldDB; Q8WNY2; -.
DR BMRB; Q8WNY2; -.
DR SMR; Q8WNY2; -.
DR STRING; 9986.ENSOCUP00000017172; -.
DR ChEMBL; CHEMBL2216746; -.
DR GeneID; 100009242; -.
DR KEGG; ocu:100009242; -.
DR CTD; 3757; -.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q8WNY2; -.
DR OrthoDB; 247304at2759; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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 Alternative splicing; Cell membrane; Glycoprotein; Ion channel;
KW Ion transport; Membrane; Methylation; Phosphoprotein; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1161
FT /note="Potassium voltage-gated channel subfamily H member
FT 2"
FT /id="PRO_0000054002"
FT TOPO_DOM 1..405
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 406..426
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 427..452
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 453..473
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 474..497
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 498..518
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 519..522
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 523..543
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 544..549
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 550..570
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 571..613
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 614..634
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 635..640
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 641..661
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 662..1161
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 REGION 233..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..985
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1121..1161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 626..631
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 258..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..949
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 744..861
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12809"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35219"
FT MOD_RES 285
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35219"
FT MOD_RES 286
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35219"
FT MOD_RES 322
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12809"
FT MOD_RES 353
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O08962"
FT MOD_RES 873
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12809"
FT MOD_RES 876
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O35219"
FT MOD_RES 1016
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:O35219"
FT MOD_RES 1139
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12809"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 69..85
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_000971"
FT CONFLICT 411
FT /note="V -> A (in Ref. 2; AAC48723)"
FT /evidence="ECO:0000305"
FT CONFLICT 445..446
FT /note="PE -> TD (in Ref. 2; AAC48723)"
FT /evidence="ECO:0000305"
FT CONFLICT 553
FT /note="L -> F (in Ref. 2; AAC48723)"
FT /evidence="ECO:0000305"
FT CONFLICT 561
FT /note="L -> C (in Ref. 2; AAC48723)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1161 AA; 126962 MW; 79B532B2FFBD9AEB CRC64;
MPVRRGHVAP QNTFLDTIIR KFEGQSRKFI IANARVENCA VIYCNDGFCE LCGYSRAEVM
QRPCTCDFLH GPRTQRRAAA QIAQALLGAE ERKVEIAFYR KDGSCFLCLV DVVPVKNEDG
AVIMFILNFE VVMEKDMVGS PARDTNHRGP PTSWLAPGRA KTFRLKLPAL LALTARESSV
RPGGAGGAGA PGAVVVDVDL TPAAPSSESL ALDEVPAMDN HVAGLGPAEE RRALVGSCSP
PPPVSAPGPH PSLRAHSLNP DASGSSCSLA RTRSRESCAS VRRASSADDI EAMRAGALPP
PPRHASTGAM HPLRSGLLNS TSDSDLVRYR TISKIPQITL NFVDLKGDPF LASPTSDREI
IAPKIKERTH NVTEKVTQVL SLGADVLPEY KLQAPRIHRW TILHYSPFKA VWDWLILLLV
IYTAVFTPYS AAFLLKETEE GPPAPECGYA CQPLAVVDLI VDIMFIVDIL INFRTTYVNA
NEEVVSHPGR IAVHYFKGWF LIDMVAAIPF DLLIFGSGSE ELIGLLKTAR LLRLVRVARK
LDRYSEYGAA VLLLLMCTFA LIAHWLACIW YAIGNMEQPH MDSRIGWLHN LGDQMGKPYN
SSGLGGPSIK DKYVTGLYFT FSSLTSVGFG NVSPNTNSEK IFSICVMLIG SLMYASIFGN
VSAIIQRLYS GTARYHTQML RVREFIRFHQ IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK
GFPECLQADI CLHLNRSLLQ HCKPFRGATK DCLRALAMKF KTTHAPPGDT LVHAGDLLTA
LYFISRGSIE ILRGDVVVAI LGKNDIFGEP LNLYARPGKS NGDVRALTYC DLHKIHRDDL
LEVLDMYPEF SDHFWSSLEI TFNLRDTNMI PGSPGSTEWE GGFNRQRKRK LSFRRRTDKD
TEQPGEVSAL GPGRAGAGPS SRGRPGGPWG ESPSSGPSSP ESSEDEGPGR SSSPLRLVPF
SSPRPPGEPP GGEPLTEDCE KSSDTCNPLS GAFSGVSNIF SFWGDSRGRQ YQELPRCPAP
APSLLNIPLS SPSRRPRGDV ESRLDALQRQ LNRLETRLSA DMATVLQLLQ RQMTLVPPAY
SAVTTPGPGP TSTSPLLPVS PFPTLTLDSL SQVSQFMACE ELPPGAPELP QEGPTRRLSL
PGQLGALTSQ PLHRHGSDPG S
