KCNH7_MOUSE
ID KCNH7_MOUSE Reviewed; 1195 AA.
AC Q9ER47; A2AUY8;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 165.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RA Arcangeli A.;
RT "Erg genes expression during development of mouse embryos.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-174 AND SER-238, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel (By similarity). Channel properties may be modulated by cAMP
CC and subunit assembly. {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. Heteromultimer with KCNH2/ERG1
CC and KCNH6/ERG2 (By similarity). {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. Kv11.3/KCNH7 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ291608; CAC14797.1; -; mRNA.
DR EMBL; AL928663; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL928689; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL929246; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS38128.1; -.
DR RefSeq; NP_573470.2; NM_133207.2.
DR AlphaFoldDB; Q9ER47; -.
DR SMR; Q9ER47; -.
DR STRING; 10090.ENSMUSP00000074563; -.
DR GlyGen; Q9ER47; 1 site.
DR iPTMnet; Q9ER47; -.
DR PhosphoSitePlus; Q9ER47; -.
DR PaxDb; Q9ER47; -.
DR PRIDE; Q9ER47; -.
DR ProteomicsDB; 301773; -.
DR ABCD; Q9ER47; 2 sequenced antibodies.
DR Antibodypedia; 19119; 176 antibodies from 25 providers.
DR DNASU; 170738; -.
DR Ensembl; ENSMUST00000075052; ENSMUSP00000074563; ENSMUSG00000059742.
DR GeneID; 170738; -.
DR KEGG; mmu:170738; -.
DR UCSC; uc008jvq.1; mouse.
DR CTD; 90134; -.
DR MGI; MGI:2159566; Kcnh7.
DR VEuPathDB; HostDB:ENSMUSG00000059742; -.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000155518; -.
DR HOGENOM; CLU_005746_2_0_1; -.
DR InParanoid; Q9ER47; -.
DR OMA; RLMRTSH; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; Q9ER47; -.
DR TreeFam; TF313130; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 170738; 1 hit in 73 CRISPR screens.
DR ChiTaRS; Kcnh7; mouse.
DR PRO; PR:Q9ER47; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9ER47; protein.
DR Bgee; ENSMUSG00000059742; Expressed in primary visual cortex and 53 other tissues.
DR ExpressionAtlas; Q9ER47; baseline and differential.
DR Genevisible; Q9ER47; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005242; F:inward rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0005267; F:potassium channel activity; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0007623; P:circadian rhythm; IEA:Ensembl.
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; ISO:MGI.
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_0000054016"
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 870..915
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 627..632
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 880..915
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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:21183079"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54852"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54852"
FT MOD_RES 894
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O54852"
FT CARBOHYD 600
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 48
FT /note="F -> L (in Ref. 1; CAC14797)"
FT /evidence="ECO:0000305"
FT CONFLICT 511
FT /note="I -> V (in Ref. 1; CAC14797)"
FT /evidence="ECO:0000305"
FT CONFLICT 750
FT /note="S -> N (in Ref. 1; CAC14797)"
FT /evidence="ECO:0000305"
FT CONFLICT 972..974
FT /note="HSG -> PSP (in Ref. 1; CAC14797)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="E -> D (in Ref. 1; CAC14797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1195 AA; 135062 MW; EC9A541243FED06D CRC64;
MPVRRGHVAP QNTFLGTIIR KFEGQNKKFI IANARVQNCA IIYCNDGFCE MTGFSRPDVM
QKPCTCDFLH GPETKRHDIA QIAQALLGSE ERKVEVTYYH KNGSTFICNT HIIPVKNQEG
VAMMFIINFE YVTDEENAAT PERVNPILPV KTVNRKLFGF KFPGLRVLTY RKQSLPQEDP
DVVVIDSSKH SDDSVAMKHF KSPTKESCSP SEADDTKALI QPSQCSPLVN ISGPLDHSSP
KRQWDRLYPD MLQSSSQLTH SRSRESLCSI RRASSVHDIE GFSVHPKNIF RDRHASEDNG
RNVKGPFNHI KSSLLGSTSD SNLNKYSTIN KIPQLTLNFS DVKTEKKNTS PPSSDKTIIA
PKVKERTHNV TEKVTQVLSL GADVLPEYKL QTPRINKFTI LHYSPFKAVW DWLILLLVIY
TAIFTPYSAA FLLNDREEQK RRECGYSCSP LNVVDLIVDI MFIIDILINF RTTYVNQNEE
VVSDPAKIAI 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 KSQSVNDSEG DTGKLRRRRL SFESEGEKDF
SKENSANDAD DSTDTIRRYQ SSKKHFEERK SRSSSFISSI DDEQKPLFLG TVDSTPRMVK
ATRLHGEETM PHSGRIHTEK RSHSCRDITD THSWEREPAR AQPEECSPSG LQRAAWGVSE
TESDLTYGEV EQRLDLLQEQ LNRLESQMTT DIQAILQLLQ KQTTVVPPAY SMVTAGAEYQ
RPILRLLRTS HPRASIKTDR SFSPSSQCPE FLDLEKSKLQ SKESLSSGRR LNTASEDNLT
SLLKQDSDAS SELDPRQRKT YLHPIRHPSL PDSSLSTVGI LGLHRHVSDP GLPGK
