KCNH7_RAT
ID KCNH7_RAT Reviewed; 1195 AA.
AC O54852;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 7;
DE AltName: Full=Ether-a-go-go-related gene potassium channel 3;
DE Short=ERG-3;
DE Short=Eag-related protein 3;
DE Short=Ether-a-go-go-related protein 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv11.3;
GN Name=Kcnh7; Synonyms=Erg3;
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].
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 KCNH6.
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174; SER-319; SER-891 AND
RP SER-894, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Channel properties may be modulated by cAMP and subunit
CC 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 KCNH6/ERG2.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in total brain, in superior cervical,
CC mesenteric and celiac ganglia, and at very low levels in retina. Found
CC in pituitary. {ECO:0000269|PubMed:10718922}.
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. Kv11.3/KCNH7 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF016191; AAB94741.1; -; mRNA.
DR RefSeq; NP_571987.1; NM_131912.1.
DR AlphaFoldDB; O54852; -.
DR BMRB; O54852; -.
DR SMR; O54852; -.
DR BioGRID; 250984; 1.
DR STRING; 10116.ENSRNOP00000009920; -.
DR GuidetoPHARMACOLOGY; 574; -.
DR TCDB; 1.A.1.20.3; the voltage-gated ion channel (vic) superfamily.
DR GlyGen; O54852; 1 site.
DR iPTMnet; O54852; -.
DR PhosphoSitePlus; O54852; -.
DR PaxDb; O54852; -.
DR PRIDE; O54852; -.
DR ABCD; O54852; 2 sequenced antibodies.
DR Ensembl; ENSRNOT00000112058; ENSRNOP00000078922; ENSRNOG00000007528.
DR GeneID; 170739; -.
DR KEGG; rno:170739; -.
DR UCSC; RGD:621112; rat.
DR CTD; 90134; -.
DR RGD; 621112; Kcnh7.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000155518; -.
DR InParanoid; O54852; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; O54852; -.
DR TreeFam; TF313130; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:O54852; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Genevisible; O54852; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; IDA:RGD.
DR GO; GO:0005267; F:potassium channel activity; IDA: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:0007623; P:circadian rhythm; IEP: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: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.
PE 1: Evidence at protein level;
KW Glycoprotein; Ion channel; Ion transport; Membrane; Phosphoprotein;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..1195
FT /note="Potassium voltage-gated channel subfamily H member
FT 7"
FT /id="PRO_0000054017"
FT TOPO_DOM 1..412
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 413..433
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 434..449
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 450..470
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 471..494
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 495..515
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 516..521
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 543..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..614
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 615..635
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 636..641
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 642..662
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 663..1195
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 41..70
FT /note="PAS"
FT DOMAIN 92..144
FT /note="PAC"
FT REGION 194..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 894..914
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 958..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1144..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..632
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT BINDING 745..862
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ER47"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 480
FT /note="E->S: Lower channel activity."
SQ SEQUENCE 1195 AA; 134901 MW; BA24C54BB86C59B7 CRC64;
MPVRRGHVAP QNTFLGTIIR KFEGQNKKFI IANARVQNCA IIYCNDGFCE MTGFSRPDVM
QKPCTCDFLH GPETKRHDIA QIAQALLGSE ERKVEVTYYH KNGSTFICNT HIIPVKNQEG
VAMMFIINFE YVTDEDNAAS PERVNPILPV KSVNRKLFGF KFPGLRVLTY RKQSLPQEDP
DVVVIDSSKH SDDSVAMKHF KSPTKESCSP SEADDTKALI QPSQCSPLVN ISGPLDHSSP
KRQWDRLYPD MLQSSSQLTH SRSRESLCSI RRASSVHDIE GFNVHPKNIF RDRHASEDNG
RNVKGPFNHI KSSLLGSTSD SNLNKYSTIN KIPQLTLNFS DVKTEKKNTS PPSSDKTIIA
PKVKERTHNV TEKVTQVLSL GADVLPEYKL QTPRINKFTI LHYSPFKAVW DWLILLLVIY
TAIFTPYSAA FLLNDREEQK RRECGYSCSP LNVVDLIVDI MFIIDILINF RTTYVNQNEE
VVSDPAKIAV HYFKGWFLID MVAAIPFDLL IFGSGSDETT TLIGLLKTAR LLRLVRVARK
LDRYSEYGAA VLMLLMCIFA LIAHWLACIW YAIGNVERPY LTDKIGWLDS LGTQIGKRYN
DSDSSSGPSI KDKYVTALYF TFSSLTSVGF GNVSPNTNSE KIFSICVMLI GSLMYASIFG
NVSAIIQRLY SGTARYHMQM LRVKEFIRFH QIPNPLRQRL EEYFQHAWTY TNGIDMNMVL
KGFPECLQAD ICLHLNQTLL QNCKAFRGAS KGCLRALAMK FKTTHAPPGD TLVHCGDVLT
ALYFLSRGSI EILKDDIVVA ILGKNDIFGE MVHLYAKPGK SNADVRALTY CDLHKIQRED
LLEVLDMYPE FSDHFLTNLE LTFNLRHESA KSQSINDSEG DTCKLRRRRL SFESEGDKDF
SKENSANDAD DSTDTIRRYQ SSKKHFEEKK SRSSSFISSI DDEQKPLFLG TVDSTPRMVK
ASRHHGEEAA PPSGRIHTDK RSHSCKDITD THSWEREHAR AQPEECSPSG LQRAAWGISE
TESDLTYGEV EQRLDLLQEQ LNRLESQMTT DIQAILQLLQ KQTTVVPPAY SMVTAGAEYQ
RPILRLLRTS HPRASIKTDR SFSPSSQCPE FLDLEKSKLK SKESLSSGKR LNTASEDNLT
SLLKQDSDAS SELDPRQRKS YLHPIRHPSL PDSSLSTVGI LGLHRHVSDP GLPGK
