KCNH6_RAT
ID KCNH6_RAT Reviewed; 950 AA.
AC O54853;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 6;
DE AltName: Full=Ether-a-go-go-related gene potassium channel 2;
DE Short=ERG-2;
DE Short=Eag-related protein 2;
DE Short=Ether-a-go-go-related protein 2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv11.2;
GN Name=Kcnh6; Synonyms=Erg2;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Cervical ganglion;
RX PubMed=9390998; DOI=10.1523/jneurosci.17-24-09423.1997;
RA Shi W., Wymore R.S., Wang H.-S., Pan Z., Cohen I.S., McKinnon D.,
RA Dixon J.E.;
RT "Identification of two nervous system-specific members of the erg potassium
RT channel gene family.";
RL J. Neurosci. 17:9423-9432(1997).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=10718922; DOI=10.1046/j.1365-2826.2000.00447.x;
RA Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R.;
RT "Expression of mRNA for voltage-dependent and inward-rectifying K channels
RT in GH3/B6 cells and rat pituitary.";
RL J. Neuroendocrinol. 12:263-272(2000).
RN [3]
RP INTERACTION WITH KCNH2 AND KCNH7, AND MUTAGENESIS OF GLY-480.
RX PubMed=11212207; DOI=10.1007/s004240000467;
RA Wimmers S., Wulfsen I., Bauer C.K., Schwarz J.R.;
RT "Erg1, erg2 and erg3 K channel subunits are able to form heteromultimers.";
RL Pflugers Arch. 441:450-455(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11425889; DOI=10.1523/jneurosci.21-13-04609.2001;
RA Saganich M.J., Machado E., Rudy B.;
RT "Differential expression of genes encoding subthreshold-operating voltage-
RT gated K+ channels in brain.";
RL J. Neurosci. 21:4609-4624(2001).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits a slowly activating, rectifying current. Channel
CC properties may be modulated by cAMP and subunit assembly.
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. Heteromultimer with KCNH2/ERG1
CC and KCNH7/ERG3.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Highly expressed in celiac and superior mesenteric
CC ganglia, but not detected in brain or in heart. Detected at low levels
CC in retina. Also found in pituitary. Also found in the olfactory bulb
CC (granular and mitral cell layers) (PubMed:11425889).
CC {ECO:0000269|PubMed:10718922, ECO:0000269|PubMed:11425889}.
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. Kv11.2/KCNH6 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF016192; AAB94742.1; -; mRNA.
DR RefSeq; NP_446389.1; NM_053937.1.
DR AlphaFoldDB; O54853; -.
DR BMRB; O54853; -.
DR SMR; O54853; -.
DR STRING; 10116.ENSRNOP00000010816; -.
DR GuidetoPHARMACOLOGY; 573; -.
DR TCDB; 1.A.1.20.2; the voltage-gated ion channel (vic) superfamily.
DR PhosphoSitePlus; O54853; -.
DR PaxDb; O54853; -.
DR PRIDE; O54853; -.
DR GeneID; 116745; -.
DR KEGG; rno:116745; -.
DR UCSC; RGD:620304; rat.
DR CTD; 81033; -.
DR RGD; 620304; Kcnh6.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; O54853; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; O54853; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:O54853; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:RGD.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0005267; F:potassium channel activity; TAS:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:RGD.
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:0006813; P:potassium ion transport; IDA:RGD.
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 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; IPR030172; KCNH6.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR10217:SF468; PTHR10217:SF468; 1.
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 SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
PE 1: Evidence at protein level;
KW Ion channel; Ion transport; Membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..950
FT /note="Potassium voltage-gated channel subfamily H member
FT 6"
FT /id="PRO_0000054014"
FT TOPO_DOM 1..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..298
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..340
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..370
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 392..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..463
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 464..484
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 485..490
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 491..511
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 512..950
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..70
FT /note="PAS"
FT DOMAIN 92..144
FT /note="PAC"
FT REGION 154..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 719..750
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 890..950
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 476..481
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT BINDING 594..711
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MUTAGEN 480
FT /note="G->S: Dominant negative mutant; abolishes ERG
FT current."
FT /evidence="ECO:0000269|PubMed:11212207"
SQ SEQUENCE 950 AA; 105706 MW; AB5AE674B08776F0 CRC64;
MPVRRGHVAP QNTYLDTIIR KFEGQSRKFL IANAQMENCA IIYCNDGFCE LFGYSRVEVM
QRPCTCDFLT GPNTPSSAVS RLAQALLGAE ECKVDILYYR KDASSFRCLV DVVPVKNEDG
AVIMFILNFE DLAQLLAKSS SRSLTQRLLS HSFLGSEGSH SRPSGQGPGP GRGKYRTVSQ
IPQFTLNFVE FNLEKHRSGS TTEIEIIAPH KVVERTQNVT EKVTQVLSLG ADVLPEYKLQ
APRIHRGTIL HYSPFKAVWD WLILLLVIYT AVFTPYSAAF LLSDQDESQR GTCGYTCSPL
TVVDLIVDIM FVVDIVINFR TTYVNTNDEV VSHPRRIAVH YFKGWFLIDM VAAIPFDLLI
FRTGSDETTT LIGLLKTARL LRLVRVARKL DRYSEYGAAV LFLLMCTFAL IAHWLACIWY
AIGNVERPYL EPKIGWLDSL GAQLGKQYNG SDPASGPSVQ DKYVTALYFT FSSLTSVGFG
NVSPNTNSEK VFSICVMLIG SLMYASIFGN VSAIIQRLYS GTARYHTQML RVKEFIRFHQ
IPNPLRQRLE EYFQHAWSYT NGIDMNAVLK GFPECLQADI CLHLHRALLQ HCPAFRGASK
GCLRALAVKF KTTHAPPGDT LVHLGDVLST LYFISRGSIE ILRDDVVVAI LGKNDIFGEP
ASLHARPGKS SADVRALTYC DLHKIHRADL LEVLDMYPAF ADTFWNKLEV TFNLRDADGG
LQSTPRQAPG HQDPQGFFLN DSQSGAAPSL SISDTSALWP ELLQQMPPSP PNPRQDLDCW
HRELGFKLEQ LQAQMNRLES RVSSDLSRIL QLLQHPQGRP SYILGASASS DLASFPETSV
TRSSESTLLV GHVPSAQTLS YGDLDDHIQT PRNFSPRTPH VAMAMDKTLV PSSEQEQPGG
LLSPLASPLR PLEVPGLGGS RFPSLPEHLS SVPKQLEFQR HGSDPGFTRS
