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Database: UniProt
Entry: Q9WVJ0
LinkDB: Q9WVJ0
Original site: Q9WVJ0 
ID   KCNH3_MOUSE             Reviewed;        1087 AA.
AC   Q9WVJ0; E9QMZ8;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 2.
DT   26-NOV-2014, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Brain;
RX   PubMed=10191308;
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 [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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC       channel. Elicits an outward current with fast inactivation.
CC       Channel 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
CC       every third position.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv12.2/KCNH3 sub-subfamily.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00060}.
CC   -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00141}.
CC   -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00140}.
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DR   EMBL; AF109143; AAD40578.1; -; mRNA.
DR   EMBL; AC161198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   UniGene; Mm.374793; -.
DR   ProteinModelPortal; Q9WVJ0; -.
DR   SMR; Q9WVJ0; 11-136, 455-510, 516-685.
DR   PhosphoSite; Q9WVJ0; -.
DR   PRIDE; Q9WVJ0; -.
DR   MGI; MGI:1341723; Kcnh3.
DR   eggNOG; COG2202; -.
DR   HOGENOM; HOG000230794; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; Q9WVJ0; -.
DR   Reactome; REACT_199077; Voltage gated Potassium channels.
DR   PRO; PR:Q9WVJ0; -.
DR   Bgee; Q9WVJ0; -.
DR   ExpressionAtlas; Q9WVJ0; baseline and differential.
DR   Genevestigator; Q9WVJ0; -.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:RefGenome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:RefGenome.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:RefGenome.
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; 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   SMART; SM00091; PAS; 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   Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
KW   Potassium; Potassium channel; Potassium transport; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
FT   CHAIN         1   1087       Potassium voltage-gated channel subfamily
FT                                H member 3.
FT                                /FTId=PRO_0000054006.
FT   TOPO_DOM      1    228       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    229    249       Helical; Name=Segment S1. {ECO:0000255}.
FT   TOPO_DOM    250    259       Extracellular. {ECO:0000255}.
FT   TRANSMEM    260    280       Helical; Name=Segment S2. {ECO:0000255}.
FT   TOPO_DOM    281    302       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    303    323       Helical; Name=Segment S3. {ECO:0000255}.
FT   TOPO_DOM    324    331       Extracellular. {ECO:0000255}.
FT   TRANSMEM    332    352       Helical; Voltage-sensor; Name=Segment S4.
FT                                {ECO:0000255}.
FT   TOPO_DOM    353    361       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    362    382       Helical; Name=Segment S5. {ECO:0000255}.
FT   TOPO_DOM    383    456       Extracellular. {ECO:0000255}.
FT   INTRAMEM    457    477       Pore-forming; Name=Segment H5.
FT                                {ECO:0000255}.
FT   TOPO_DOM    478    482       Extracellular. {ECO:0000255}.
FT   TRANSMEM    483    503       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    504   1087       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       18     90       PAS. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00140}.
FT   DOMAIN       93    145       PAC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00141}.
FT   NP_BIND     585    700       cNMP.
FT   MOTIF       468    473       Selectivity filter. {ECO:0000250}.
FT   COMPBIAS    954   1061       Pro-rich.
FT   CARBOHYD    421    421       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    428    428       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    439    439       N-linked (GlcNAc...). {ECO:0000255}.
FT   CONFLICT      5      5       R -> P (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    388    388       S -> N (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    433    434       SR -> GG (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    744    744       V -> I (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    806    806       S -> T (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    836    836       S -> G (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    840    840       P -> H (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    871    871       G -> V (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    889    889       M -> T (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    924    924       G -> V (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    928    928       E -> G (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    935    935       S -> C (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    971    971       Q -> H (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1025   1025       S -> P (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1052   1052       P -> S (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1076   1076       T -> S (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
SQ   SEQUENCE   1087 AA;  117667 MW;  05D419F7812E9D0A 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 SSSRGSEANG TGLELLGGPS LRSAYITSLY FALSSLTSVG FGNVSANTDT
     EKIFSICTML IGALMHAVVF GNVTAIIQRM YARRFLYHSR TRDLRDYIRI HRIPKPLKQR
     MLEYFQATWA VNNGIDTTEL LQSLPDELRA DIAMHLHKEV LQLPLFEAAS RGCLRALSLA
     LRPAFCTPGE YLIHQGDALQ ALYFVCSGSM EVLKGGTVLA ILGKGDLIGC ELPQREQVVK
     ANADVKGLTY CVLQCLQLAG LHESLALYPE FAPRFSRGLR GELSYNLGAG GVSAEVDTSS
     LSGDNTLMST LEEKETDGEQ GHTVSPAPAD EPSSPLLSPG CTSSSSAAKL LSPRRTAPRP
     RLGGRGRPSR AGVLKPEAGP SAHPRSLDGL QLPPMPWNVP PDLSPRVVDG IEDGCSSDQP
     KFSFRVGQSG PECSSSPSPG TESGLLTVPL GPSEARNTDT LDKLRQAVME LSEQVLQMRE
     GLQSLRQAVQ LILVPQGEGQ CPRGSGEEPC PATASGLLQP LRVDTGASSY CLQPPAGSVL
     SGTWPHPRPG QPPPLMAPWP WGPPASQSSP WPRATALWTS TSDSEPPGSG DLCSEPSTPA
     SPPPSEEGAR TGTPAPVSQA EATSTGEPPP GPGGRALPWD PHSLEMVLIG CHGPGTVQWT
     QEEGTGV
//
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