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 01-MAY-2013, entry version 112.
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 -!- SIMILARITY: Contains 1 cyclic nucleotide-binding domain.
CC -!- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
CC -!- SIMILARITY: Contains 1 PAS (PER-ARNT-SIM) domain.
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DR EMBL; AF109143; AAD40578.1; -; mRNA.
DR EMBL; AC161198; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR IPI; IPI00126045; -.
DR UniGene; Mm.374793; -.
DR ProteinModelPortal; Q9WVJ0; -.
DR SMR; Q9WVJ0; 1-135, 455-509, 516-685.
DR PhosphoSite; Q9WVJ0; -.
DR PRIDE; Q9WVJ0; -.
DR MGI; MGI:1341723; Kcnh3.
DR eggNOG; COG2202; -.
DR HOGENOM; HOG000230794; -.
DR HOVERGEN; HBG052232; -.
DR OrthoDB; EOG4255S1; -.
DR ArrayExpress; Q9WVJ0; -.
DR Bgee; Q9WVJ0; -.
DR Genevestigator; Q9WVJ0; -.
DR GermOnline; ENSMUSG00000037579; Mus musculus.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR GO; GO:0023014; P:signal transduction by phosphorylation; IEA:GOC.
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 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; cNMP_binding; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; FALSE_NEG.
DR PROSITE; PS00889; CNMP_BINDING_2; FALSE_NEG.
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 (Potential).
FT TRANSMEM 229 249 Helical; Name=Segment S1; (Potential).
FT TOPO_DOM 250 259 Extracellular (Potential).
FT TRANSMEM 260 280 Helical; Name=Segment S2; (Potential).
FT TOPO_DOM 281 302 Cytoplasmic (Potential).
FT TRANSMEM 303 323 Helical; Name=Segment S3; (Potential).
FT TOPO_DOM 324 331 Extracellular (Potential).
FT TRANSMEM 332 352 Helical; Voltage-sensor; Name=Segment S4;
FT (Potential).
FT TOPO_DOM 353 361 Cytoplasmic (Potential).
FT TRANSMEM 362 382 Helical; Name=Segment S5; (Potential).
FT TOPO_DOM 383 456 Extracellular (Potential).
FT INTRAMEM 457 477 Pore-forming; Name=Segment H5;
FT (Potential).
FT TOPO_DOM 478 482 Extracellular (Potential).
FT TRANSMEM 483 503 Helical; Name=Segment S6; (Potential).
FT TOPO_DOM 504 1087 Cytoplasmic (Potential).
FT DOMAIN 18 90 PAS.
FT DOMAIN 93 145 PAC.
FT NP_BIND 585 700 cNMP.
FT MOTIF 468 473 Selectivity filter (By similarity).
FT COMPBIAS 954 1061 Pro-rich.
FT CARBOHYD 421 421 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 428 428 N-linked (GlcNAc...) (Potential).
FT CARBOHYD 439 439 N-linked (GlcNAc...) (Potential).
FT CONFLICT 5 5 R -> P (in Ref. 1; AAD40578).
FT CONFLICT 388 388 S -> N (in Ref. 1; AAD40578).
FT CONFLICT 433 434 SR -> GG (in Ref. 1; AAD40578).
FT CONFLICT 744 744 V -> I (in Ref. 1; AAD40578).
FT CONFLICT 806 806 S -> T (in Ref. 1; AAD40578).
FT CONFLICT 836 836 S -> G (in Ref. 1; AAD40578).
FT CONFLICT 840 840 P -> H (in Ref. 1; AAD40578).
FT CONFLICT 871 871 G -> V (in Ref. 1; AAD40578).
FT CONFLICT 889 889 M -> T (in Ref. 1; AAD40578).
FT CONFLICT 924 924 G -> V (in Ref. 1; AAD40578).
FT CONFLICT 928 928 E -> G (in Ref. 1; AAD40578).
FT CONFLICT 935 935 S -> C (in Ref. 1; AAD40578).
FT CONFLICT 971 971 Q -> H (in Ref. 1; AAD40578).
FT CONFLICT 1025 1025 S -> P (in Ref. 1; AAD40578).
FT CONFLICT 1052 1052 P -> S (in Ref. 1; AAD40578).
FT CONFLICT 1076 1076 T -> S (in Ref. 1; AAD40578).
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
//
