KCNH3_MOUSE
ID KCNH3_MOUSE Reviewed; 1095 AA.
AC Q9WVJ0; B2RU85; E9QMZ8; Q6U1M1;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2017, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 3;
DE AltName: Full=Ether-a-go-go-like potassium channel 2;
DE Short=ELK channel 2;
DE Short=mElk2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv12.2;
GN Name=Kcnh3; Synonyms=Elk2;
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;
RX PubMed=10191308; DOI=10.1523/jneurosci.19-08-02906.1999;
RA Trudeau M.C., Titus S.A., Branchaw J.L., Ganetzky B., Robertson G.A.;
RT "Functional analysis of a mouse brain Elk-type K+ channel.";
RL J. Neurosci. 19:2906-2918(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J;
RA Jegla T., Lee V., Huynh T.;
RT "Coding sequence of the mouse potassium channel Kcnh3.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits an outward current with fast inactivation. 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.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in brain, but not in other tissues.
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. Kv12.2/KCNH3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF109143; AAD40578.1; -; mRNA.
DR EMBL; AY380579; AAQ90188.1; -; mRNA.
DR EMBL; AC161198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466550; EDL04139.1; -; Genomic_DNA.
DR EMBL; BC141013; AAI41014.1; -; mRNA.
DR EMBL; BC145145; AAI45146.1; -; mRNA.
DR CCDS; CCDS27817.1; -.
DR RefSeq; NP_034731.3; NM_010601.3.
DR AlphaFoldDB; Q9WVJ0; -.
DR SMR; Q9WVJ0; -.
DR STRING; 10090.ENSMUSP00000040548; -.
DR GuidetoPHARMACOLOGY; 576; -.
DR GlyGen; Q9WVJ0; 3 sites.
DR iPTMnet; Q9WVJ0; -.
DR PhosphoSitePlus; Q9WVJ0; -.
DR PaxDb; Q9WVJ0; -.
DR PRIDE; Q9WVJ0; -.
DR ProteomicsDB; 263400; -.
DR Antibodypedia; 25968; 99 antibodies from 20 providers.
DR DNASU; 16512; -.
DR Ensembl; ENSMUST00000041415; ENSMUSP00000040548; ENSMUSG00000037579.
DR GeneID; 16512; -.
DR KEGG; mmu:16512; -.
DR UCSC; uc011zzc.1; mouse.
DR CTD; 23416; -.
DR MGI; MGI:1341723; Kcnh3.
DR VEuPathDB; HostDB:ENSMUSG00000037579; -.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000161742; -.
DR InParanoid; Q9WVJ0; -.
DR OMA; YIGQQEI; -.
DR OrthoDB; 247304at2759; -.
DR TreeFam; TF313130; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16512; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnh3; mouse.
DR PRO; PR:Q9WVJ0; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q9WVJ0; protein.
DR Bgee; ENSMUSG00000037579; Expressed in superior frontal gyrus and 78 other tissues.
DR Genevisible; Q6U1M1; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; 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; IPR003950; K_chnl_volt-dep_ELK.
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; PR01465; ELKCHANNEL.
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 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..1095
FT /note="Potassium voltage-gated channel subfamily H member
FT 3"
FT /id="PRO_0000054006"
FT TOPO_DOM 1..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..464
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 465..485
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 486..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..1095
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..90
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 740..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 854..883
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 965..1069
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 476..481
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 764..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 854..871
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 996..1016
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 593..708
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 447
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 5
FT /note="R -> P (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 388
FT /note="S -> N (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 433..442
FT /note="SSSSGSGGGR -> GG (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 472
FT /note="S -> G (in Ref. 2; AAQ90188)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="M -> T (in Ref. 2; AAQ90188)"
FT /evidence="ECO:0000305"
FT CONFLICT 500
FT /note="G -> A (in Ref. 2; AAQ90188)"
FT /evidence="ECO:0000305"
FT CONFLICT 752
FT /note="V -> I (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="S -> T (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 844
FT /note="S -> G (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 848
FT /note="P -> H (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 879
FT /note="G -> V (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 897
FT /note="M -> T (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 932
FT /note="G -> V (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 936
FT /note="E -> G (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="S -> C (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 979
FT /note="Q -> H (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 1033
FT /note="S -> P (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 1060
FT /note="P -> S (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
FT CONFLICT 1084
FT /note="T -> S (in Ref. 1; AAD40578)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1095 AA; 118244 MW; C2C3A26090E37A50 CRC64;
MPAMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVAGLF PVVYCSDGFC DLTGFSRAEV
MQRGCACSFL YGPDTSELVR QQIRKALDEH KEFKAELILY RKSGLPFWCL LDVIPIKNEK
GEVALFLVSH KDISETKNRG GPDNWKERGG GRRRYGRAGS KGFNANRRRS RAVLYHLSGH
LQKQPKGKHK LNKGVFGEKP NLPEYKVAAI RKSPFILLHC GALRATWDGF ILLATLYVAV
TVPYSVCVST AREPSAARGP PSVCDLAVEV LFILDIVLNF RTTFVSKSGQ VVFAPKSICL
HYVTTWFLLD VIAALPFDLL HAFKVNVYVG AHLLKTVRLL RLLRLLPRLD RYSQYSAVVL
TLLMAVFALL AHWVACVWFY IGQQEIESSE SELPEIGWLQ ELARRLETPY YLVSRSPDGG
NSSGQSENCS SSSSSSGSGG GRGSEANGTG LELLGGPSLR SAYITSLYFA LSSLTSVGFG
NVSANTDTEK IFSICTMLIG ALMHAVVFGN VTAIIQRMYA RRFLYHSRTR DLRDYIRIHR
IPKPLKQRML EYFQATWAVN NGIDTTELLQ SLPDELRADI AMHLHKEVLQ LPLFEAASRG
CLRALSLALR PAFCTPGEYL IHQGDALQAL YFVCSGSMEV LKGGTVLAIL GKGDLIGCEL
PQREQVVKAN ADVKGLTYCV LQCLQLAGLH ESLALYPEFA PRFSRGLRGE LSYNLGAGGV
SAEVDTSSLS GDNTLMSTLE EKETDGEQGH TVSPAPADEP SSPLLSPGCT SSSSAAKLLS
PRRTAPRPRL GGRGRPSRAG VLKPEAGPSA HPRSLDGLQL PPMPWNVPPD LSPRVVDGIE
DGCSSDQPKF SFRVGQSGPE CSSSPSPGTE SGLLTVPLGP SEARNTDTLD KLRQAVMELS
EQVLQMREGL QSLRQAVQLI LVPQGEGQCP RGSGEEPCPA TASGLLQPLR VDTGASSYCL
QPPAGSVLSG TWPHPRPGQP PPLMAPWPWG PPASQSSPWP RATALWTSTS DSEPPGSGDL
CSEPSTPASP PPSEEGARTG TPAPVSQAEA TSTGEPPPGP GGRALPWDPH SLEMVLIGCH
GPGTVQWTQE EGTGV
