GenomeNet

Database: UniProt
Entry: Q9WVJ0
LinkDB: Q9WVJ0
Original site: Q9WVJ0 
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   28-MAR-2018, entry version 151.
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; Myomorpha;
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 [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.,
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).
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
RT   project: 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.
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) (TC
CC       1.A.1.20) subfamily. Kv12.2/KCNH3 sub-subfamily. {ECO:0000305}.
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   UniGene; Mm.374793; -.
DR   ProteinModelPortal; Q9WVJ0; -.
DR   SMR; Q9WVJ0; -.
DR   STRING; 10090.ENSMUSP00000040548; -.
DR   GuidetoPHARMACOLOGY; 576; -.
DR   iPTMnet; Q9WVJ0; -.
DR   PhosphoSitePlus; Q9WVJ0; -.
DR   PaxDb; Q9WVJ0; -.
DR   PRIDE; Q9WVJ0; -.
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   eggNOG; KOG0498; Eukaryota.
DR   eggNOG; ENOG410XPSE; LUCA.
DR   GeneTree; ENSGT00900000140833; -.
DR   HOGENOM; HOG000230794; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; Q9WVJ0; -.
DR   KO; K04906; -.
DR   OMA; PLMAPWP; -.
DR   OrthoDB; EOG091G0OXR; -.
DR   TreeFam; TF313130; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   PRO; PR:Q9WVJ0; -.
DR   Proteomes; UP000000589; Chromosome 15.
DR   Bgee; ENSMUSG00000037579; -.
DR   Genevisible; Q6U1M1; MM.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; 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   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   1095       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    464       Extracellular. {ECO:0000255}.
FT   INTRAMEM    465    485       Pore-forming; Name=Segment H5.
FT                                {ECO:0000255}.
FT   TOPO_DOM    486    490       Extracellular. {ECO:0000255}.
FT   TRANSMEM    491    511       Helical; Name=Segment S6. {ECO:0000255}.
FT   TOPO_DOM    512   1095       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     593    708       cNMP.
FT   MOTIF       476    481       Selectivity filter. {ECO:0000250}.
FT   COMPBIAS    962   1069       Pro-rich.
FT   CARBOHYD    421    421       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    428    428       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    447    447       N-linked (GlcNAc...) asparagine.
FT                                {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    442       SSSSGSGGGR -> GG (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    472    472       S -> G (in Ref. 2; AAQ90188).
FT                                {ECO:0000305}.
FT   CONFLICT    497    497       M -> T (in Ref. 2; AAQ90188).
FT                                {ECO:0000305}.
FT   CONFLICT    500    500       G -> A (in Ref. 2; AAQ90188).
FT                                {ECO:0000305}.
FT   CONFLICT    752    752       V -> I (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    814    814       S -> T (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    844    844       S -> G (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    848    848       P -> H (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    879    879       G -> V (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    897    897       M -> T (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    932    932       G -> V (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    936    936       E -> G (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    943    943       S -> C (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT    979    979       Q -> H (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1033   1033       S -> P (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1060   1060       P -> S (in Ref. 1; AAD40578).
FT                                {ECO:0000305}.
FT   CONFLICT   1084   1084       T -> S (in Ref. 1; AAD40578).
FT                                {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
//
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