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 03-AUG-2022, entry version 147.
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; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC 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+ channel
RT 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 channels
RT in GH3/B6 cells and rat pituitary.";
RL J. Neuroendocrinol. 12:263-272(2000).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11425889; DOI=10.1523/jneurosci.21-13-04609.2001;
RA Saganich M.J., Machado E., Rudy B.;
RT "Differential expression of genes encoding subthreshold-operating voltage-
RT 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 dentate
CC gyrus and basal ganglia of caudate/putamen and accumbens nucleus).
CC Expressed in pituitary. {ECO:0000269|PubMed:10718922,
CC ECO:0000269|PubMed:11425889}.
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) (TC
CC 1.A.1.20) subfamily. Kv12.1/KCNH8 sub-subfamily. {ECO:0000305}.
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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_145095.2.
DR AlphaFoldDB; Q9QWS8; -.
DR SMR; Q9QWS8; -.
DR STRING; 10116.ENSRNOP00000017246; -.
DR BindingDB; Q9QWS8; -.
DR GlyGen; Q9QWS8; 2 sites.
DR PaxDb; Q9QWS8; -.
DR PRIDE; Q9QWS8; -.
DR GeneID; 246325; -.
DR KEGG; rno:246325; -.
DR CTD; 131096; -.
DR RGD; 2549; Kcnh8.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q9QWS8; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; Q9QWS8; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q9QWS8; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; 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: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.
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..1102
FT /note="Potassium voltage-gated channel subfamily H member
FT 8"
FT /id="PRO_0000054020"
FT TOPO_DOM 1..225
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 226..246
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 247..255
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 277..298
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 320..327
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 328..348
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 349..353
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 354..374
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 375..419
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 420..440
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 441..448
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 449..469
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 470..1102
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..90
FT /note="PAS"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 683..744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 762..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 818..845
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..983
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 434..439
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 724..744
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 762..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 551..668
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 409
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 71
FT /note="F -> L (in Ref. 2; CAA07591)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="K -> N (in Ref. 2; CAA07591)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="I -> T (in Ref. 2; CAA07591)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="M -> I (in Ref. 2; CAA07591)"
FT /evidence="ECO:0000305"
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
