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   24-JAN-2024, entry version 179.
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)
CC       (TC 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   GlyCosmos; Q9WVJ0; 3 sites, No reported glycans.
DR   GlyGen; Q9WVJ0; 3 sites.
DR   iPTMnet; Q9WVJ0; -.
DR   PhosphoSitePlus; Q9WVJ0; -.
DR   PaxDb; 10090-ENSMUSP00000040548; -.
DR   ProteomicsDB; 263400; -.
DR   Antibodypedia; 25968; 119 antibodies from 20 providers.
DR   DNASU; 16512; -.
DR   Ensembl; ENSMUST00000041415.5; ENSMUSP00000040548.4; ENSMUSG00000037579.8.
DR   GeneID; 16512; -.
DR   KEGG; mmu:16512; -.
DR   UCSC; uc011zzc.1; mouse.
DR   AGR; MGI:1341723; -.
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; 66005at2759; -.
DR   TreeFam; TF313130; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 16512; 1 hit in 77 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 80 other cell types or tissues.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1200.260; -; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10217:SF481; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 3; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 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; PR01465; ELKCHANNEL.
DR   SMART; SM00100; cNMP; 1.
DR   SMART; SM00086; PAC; 1.
DR   SUPFAM; SSF51206; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
DR   PROSITE; PS50042; CNMP_BINDING_3; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   Genevisible; Q6U1M1; MM.
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
//