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Database: UniProt/SWISS-PROT
Entry: KCNH8_RAT
LinkDB: KCNH8_RAT
Original site: KCNH8_RAT 
ID   KCNH8_RAT               Reviewed;        1102 AA.
AC   Q9QWS8; O88877;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   28-NOV-2002, sequence version 2.
DT   16-APR-2014, entry version 115.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 8;
DE   AltName: Full=Ether-a-go-go-like potassium channel 3;
DE            Short=ELK channel 3;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv12.1;
GN   Name=Kcnh8; Synonyms=Elk1, Elk3;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=9714851; DOI=10.1111/j.1469-7793.1998.675bg.x;
RA   Shi W., Wang H.-S., Pan Z., Wymore R.S., Cohen I.S., McKinnon D.,
RA   Dixon J.E.;
RT   "Cloning of a mammalian elk potassium channel gene and EAG mRNA
RT   distribution in rat sympathetic ganglia.";
RL   J. Physiol. (Lond.) 511:675-682(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 9-379.
RC   TISSUE=Brain cortex;
RX   PubMed=9824707; DOI=10.1111/j.1469-7793.1998.647ba.x;
RA   Engeland B., Neu A., Ludwig J., Roeper J., Pongs O.;
RT   "Cloning and functional expression of rat ether-a-go-go-like K+
RT   channel genes.";
RL   J. Physiol. (Lond.) 513:647-654(1998).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=10718922; DOI=10.1046/j.1365-2826.2000.00447.x;
RA   Wulfsen I., Hauber H.-P., Schiemann D., Bauer C.K., Schwarz J.R.;
RT   "Expression of mRNA for voltage-dependent and inward-rectifying K
RT   channels in GH3/B6 cells and rat pituitary.";
RL   J. Neuroendocrinol. 12:263-272(2000).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=11425889;
RA   Saganich M.J., Machado E., Rudy B.;
RT   "Differential expression of genes encoding subthreshold-operating
RT   voltage-gated K+ channels in brain.";
RL   J. Neurosci. 21:4609-4624(2001).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC       channel. Elicits a slowly activating, outward rectifying current.
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 superior cervical, mesenteric and
CC       coeliac ganglia. Expressed in brain (piriform cortex, olfactory
CC       tubercle, cerebral cortex, hippocampus pyramidial cells and
CC       dentate gyrus and basal ganglia of caudate/putamen and accumbens
CC       nucleus). Expressed in pituitary.
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. Kv12.1/KCNH8 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; AF061957; AAC61520.1; -; mRNA.
DR   EMBL; AJ007632; CAA07591.1; -; mRNA.
DR   PIR; T17367; T17367.
DR   RefSeq; NP_659563.1; NM_145095.1.
DR   UniGene; Rn.30029; -.
DR   ProteinModelPortal; Q9QWS8; -.
DR   BindingDB; Q9QWS8; -.
DR   PaxDb; Q9QWS8; -.
DR   GeneID; 246325; -.
DR   KEGG; rno:246325; -.
DR   CTD; 131096; -.
DR   RGD; 2549; Kcnh8.
DR   eggNOG; COG2202; -.
DR   HOGENOM; HOG000230794; -.
DR   HOVERGEN; HBG052232; -.
DR   InParanoid; Q9QWS8; -.
DR   KO; K04911; -.
DR   PhylomeDB; Q9QWS8; -.
DR   NextBio; 623752; -.
DR   PRO; PR:Q9QWS8; -.
DR   Genevestigator; Q9QWS8; -.
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:0003705; F:RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity; IMP:RGD.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:RGD.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:RGD.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:RefGenome.
DR   GO; GO:0042391; P:regulation of membrane potential; IBA:RefGenome.
DR   GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IMP:GOC.
DR   GO; GO:0006366; P:transcription from RNA polymerase II promoter; IMP: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   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.
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   1102       Potassium voltage-gated channel subfamily
FT                                H member 8.
FT                                /FTId=PRO_0000054020.
FT   TOPO_DOM      1    225       Cytoplasmic (Potential).
FT   TRANSMEM    226    246       Helical; Name=Segment S1; (Potential).
FT   TOPO_DOM    247    255       Extracellular (Potential).
FT   TRANSMEM    256    276       Helical; Name=Segment S2; (Potential).
FT   TOPO_DOM    277    298       Cytoplasmic (Potential).
FT   TRANSMEM    299    319       Helical; Name=Segment S3; (Potential).
FT   TOPO_DOM    320    327       Extracellular (Potential).
FT   TRANSMEM    328    348       Helical; Voltage-sensor; Name=Segment S4;
FT                                (Potential).
FT   TOPO_DOM    349    353       Cytoplasmic (Potential).
FT   TRANSMEM    354    374       Helical; Name=Segment S5; (Potential).
FT   TOPO_DOM    375    419       Extracellular (Potential).
FT   INTRAMEM    420    440       Pore-forming; Name=Segment H5;
FT                                (Potential).
FT   TOPO_DOM    441    448       Extracellular (Potential).
FT   TRANSMEM    449    469       Helical; Name=Segment S6; (Potential).
FT   TOPO_DOM    470   1102       Cytoplasmic (Potential).
FT   DOMAIN       18     90       PAS.
FT   DOMAIN       93    145       PAC.
FT   NP_BIND     551    668       cNMP.
FT   MOTIF       434    439       Selectivity filter (By similarity).
FT   COMPBIAS    711    722       Poly-Glu.
FT   CARBOHYD    320    320       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    409    409       N-linked (GlcNAc...) (Potential).
FT   CONFLICT     71     71       F -> L (in Ref. 2; CAA07591).
FT   CONFLICT    187    187       K -> N (in Ref. 2; CAA07591).
FT   CONFLICT    296    296       I -> T (in Ref. 2; CAA07591).
FT   CONFLICT    370    370       M -> I (in Ref. 2; CAA07591).
SQ   SEQUENCE   1102 AA;  123231 MW;  A135CC36E2E7F1A3 CRC64;
     MPVMKGLLAP QNTFLDTIAT RFDGTHSNFI LANAQVAKGF PIVYCSDGFC ELAGFARTEV
     MQKSCSCKFL FGVETNEQLM LQIEKSLEEK VEFKGEIMFY KKNGAPFWCL LDIVPIKNEK
     GDVVLFLASF KDITDTKVKI TSEDKKEDRA KGRSRAGSHF DSARRRSRAV LYHISGHLQR
     REKNKLKINN NVFVDKPAFP EYKVSDAKKS KFILLHFSTF KAGWDWLILL ATFYVAVTVP
     YNVCFIGNED LSTTRSTTVS DIAVEILFII DIILNFRTTY VSKSGQVIFE ARSICIHYVT
     TWFIIDLIAA LPFDLLYAFN VTVVSLVHLL KTVRLLRLLR LLQKLDRYSQ HSTIVLTLLM
     SMFALLAHWM ACIWYVIGKM EREDNSLLKW EVGWLHELGK RLESPYYGNN TLGGPSIRSA
     YIAALYFTLS SLTSVGFGNV SANTDAEKIF SICTMLIGAL MHALVFGNVT AIIQRMYSRW
     SLYHTRTKDL KDFIRVHHLP QQLKQRMLEY FQTTWSVNNG IDSNELLKDF PDELRSDITM
     HLNKEILQLS LFECASRGCL RSLSLHIKTS FCAPGEYLLR QGDALQAIYF VCSGSMEVLK
     DSMVLAILGK GDLIGANLSI KDQVIKTNAD VKALTYCDLQ CIILKGLFEV LGLYPEYAHK
     FVEDIQHDLT YNLREGHESD VISRLSNKST VPQAEPKGNG SIKKRLPSIV EDEEEEEVEE
     EETTSLSPIY TRGSSVSHSK KTGSSKSYLG LSLKQLTSGT VPFHSPIRVS SANSPKTKQE
     ADPPNHGTRK EKNLKVQLCS LGTAGTPELS PRIVDGIEDG NSSEETQTFD FGSEQIRPEP
     RISPSLGESE IGAAFLFIKA EETKQQINKL NSEVTTLTQE VSQLGKDMRS IMQLLENILS
     PQQPSQFCSL HPTSICPSRE SFQTRVSWSA HQPCLHLQAN GAHLYHGNVT SDIWSVDPSL
     VGSNPQRTEA HEQSPVDSEL HHSPNLAYSP SHCQVIQEGH LQFLRCISPH SDTTLTPLQS
     ISATLSSSVC SSSETSLHLV LPSRSEEGSI THGPVSSFSL ENLPGSWDRE GMMSASTEPL
     ENFPVEVVTS TADVKDSKAI NV
//
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