KCNH6_CHICK
ID KCNH6_CHICK Reviewed; 1202 AA.
AC Q9PT84; F1NBY6;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 6 {ECO:0000305};
DE AltName: Full=Ether-a-go-go-related gene potassium channel {ECO:0000303|PubMed:10906470};
DE Short=ERG {ECO:0000303|PubMed:10906470};
DE Short=Eag-related protein {ECO:0000303|PubMed:10906470};
DE Short=Ether-a-go-go-related protein {ECO:0000303|PubMed:10906470};
DE AltName: Full=Voltage-gated potassium channel subunit Kv11.2 {ECO:0000250|UniProtKB:Q9H252};
GN Name=KCNH6 {ECO:0000305}; Synonyms=ERG {ECO:0000303|PubMed:10906470};
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red jungle fowl;
RX PubMed=15592404; DOI=10.1038/nature03154;
RA Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P.,
RA Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B.,
RA Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C.,
RA Fulton R.S., Graves T.A., Kremitzki C., Layman D., Magrini V.,
RA McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O.,
RA Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W.,
RA Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D.,
RA Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K.,
RA Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L.,
RA Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B.,
RA Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M.,
RA Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K.,
RA Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E.,
RA Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M.,
RA Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M.,
RA Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S.,
RA Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M.,
RA Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M.,
RA Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A.,
RA Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S.,
RA Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J.,
RA Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J.,
RA Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E.,
RA Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M.,
RA Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A.,
RA Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M.,
RA Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O.,
RA Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E.,
RA Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S.,
RA Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E.,
RA Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R.,
RA Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R.,
RA Wilson R.K.;
RT "Sequence and comparative analysis of the chicken genome provide unique
RT perspectives on vertebrate evolution.";
RL Nature 432:695-716(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 294-819.
RC TISSUE=Embryo;
RX PubMed=10906470; DOI=10.1016/s0925-4773(00)00335-x;
RA Crociani O., Cherubini A., Piccini E., Polvani S., Costa L., Fontana L.,
RA Hofmann G., Rosati B., Wanke E., Olivotto M., Arcangeli A.;
RT "erg gene(s) expression during development of the nervous and muscular
RT system of quail embryos.";
RL Mech. Dev. 95:239-243(2000).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits a slowly activating, rectifying current (By
CC similarity). Channel properties may be modulated by cAMP and subunit
CC assembly (By similarity). {ECO:0000250}.
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
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; AADN03008798; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ271210; CAB66135.1; -; mRNA.
DR AlphaFoldDB; Q9PT84; -.
DR SMR; Q9PT84; -.
DR STRING; 9031.ENSGALP00000030828; -.
DR PaxDb; Q9PT84; -.
DR VEuPathDB; HostDB:geneid_414871; -.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q9PT84; -.
DR OrthoDB; 247304at2759; -.
DR TreeFam; TF313130; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
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:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR000014; PAS.
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 SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS50112; PAS; 1.
PE 2: Evidence at transcript level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1202
FT /note="Potassium voltage-gated channel subfamily H member
FT 6"
FT /id="PRO_0000054004"
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..443
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..485
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 486..506
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 507..515
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 516..536
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 537..543
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 544..564
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 565..608
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 609..629
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 630..635
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 636..656
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 657..1202
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 36..84
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 87..139
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 203..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 285..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 912..948
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1092..1112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1140..1202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 621..626
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 209..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..943
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 739..839
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00060"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 594
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CONFLICT 294..299
FT /note="MGLSGK -> QSWRAE (in Ref. 2; CAB66135)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1202 AA; 135501 MW; 72E0BA6044999682 CRC64;
MGSAALPHAR QRWVSHALDS NRKFLIANAQ MENCAIIYCN DGFCEMFGYS RVEVMQRPCT
CDFLTGPDTT KSSIAQLTQA LLGSEECKLE ILYYRKDTSC FRCLVDVVPV KNEDGVVIMF
ILNFEDLAQL IAKSSGRSLH HRLSQSWRAG EGRRLKFSLP SLRRLKAQRN SLPTSEFDGV
AIDYGKPGGD SLILRDLKTS PKENCVQSET ESLLEKERRP SLEADPTLQH PIPKQEPPSL
GPRGSYSAWG FIRSRPGGSF HSLRRVSSLD NFEAARSEFQ RKFRERRANS EGGMGLSGKA
SHVKPNPPNS TSDSDLMKYR TISQIPQFTL NFVEFNLEKH RSGSTTEIEI IAPHKVTERT
QNVTEKVTQV LSLGADVLPE YKLQAPRIHR WTILHYSPFK AVWDWLILLL VIYTAVFTPY
SAAFLLNEEQ GEEKHWNCSY SCDPLNIIDL IVDIMFIVDI VINFRTTYVN INDEVVSHPG
KIAIHYFKGW FLIDMVAAIP FDLLIFRSGS DETTTLIGLL KTARLLRLVR VARKLDRYSE
YGAAVLFLLM CTFALIAHWL ACIWYAIGNV ERPYMEHKIG WLDNLGDQIG KRYNDSDLSS
GPSIKDKYVT ALYFTFSSLT SVGFGNVSPN TNSEKIFSIC VMLIGSLMYA SIFGNVSAII
QRLYSGTARY HTQMLRVKEF IRFHQIPNPL RQRLEEYFQH AWSYTNGIDM NAVLKGFPDC
LQADICLHLN RTLLQNCKAF RGASKGCLRA LAMKFKTTHA PPGDTLVHYG DVLTTLYFIS
RGSIEILKED IVVAILGKND IFGEPISLYA RPGKSNADVR ALTYCDLHKI QREDLLEVLD
MYPAFSDNFW SNLEITFNLR DADSVPRTPL SEEYDCTYRR VRRRKHSLCQ PNKPDPDTGT
SDAEQYHTYS ELTNPQDPLS KDQWDDVGSS TTPCSQTSDD EAKPGSPTKA LSLVTASASG
TEVSKQAAES SQSYAGTHIC TTPLDIPNMF TFWEDQRPNH HPEPLQHVSL VHSSRDIPLH
SDYRPGQIES RLELLQAQLS RLESRMSSDI NIILQLLQRQ LSQVPPAYSP ISPSSHNLAM
YGIVPRSLEP LTPCAPLEDE QQTAPGQSPS YAEVEKFHLK SRHSLSSGMH LTVASDETMT
VYSEQEHHSP PLLNPEPPHQ RAPNTQGLLR GSRFPSLPEH LEASSEHQDI QRHLSDPVLP
GS
