KCNH4_RAT
ID KCNH4_RAT Reviewed; 1017 AA.
AC Q9R1T9; O89048;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 4;
DE AltName: Full=Brain-specific eag-like channel 2;
DE Short=BEC2;
DE AltName: Full=Ether-a-go-go-like potassium channel 1;
DE Short=ELK channel 1;
DE Short=rElk1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv12.3;
GN Name=Kcnh4; 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], AND TISSUE SPECIFICITY.
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Brain;
RX PubMed=10455180; DOI=10.1074/jbc.274.35.25018;
RA Miyake A., Mochizuki S., Yokoi H., Kohda M., Furuichi K.;
RT "New ether-a-go-go K+ channel family members localized in human
RT telencephalon.";
RL J. Biol. Chem. 274:25018-25025(1999).
RN [3]
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 an outward current, but shows no inactivation. Channel
CC 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: Highly expressed in adult testis, and in adult and
CC embryonic brain. In adult brain found in piriform cortex, olfactory
CC tubercle, cerebral cortex, hippocampus pyramidial cells and dentate
CC gyrus and basal ganglia of caudate/putamen and accumbens nucleus.
CC Detected at intermediate levels in lung, spinal cord, and pituitary.
CC {ECO:0000269|PubMed:11425889, ECO:0000269|PubMed:9824707}.
CC -!- DEVELOPMENTAL STAGE: Expressed at day E18 in embryonic brain.
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. Kv12.3/KCNH4 sub-subfamily. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJ007628; CAA07587.1; -; mRNA.
DR EMBL; AB022699; BAA83593.1; -; mRNA.
DR PIR; T31354; T31354.
DR RefSeq; NP_446082.1; NM_053630.1.
DR AlphaFoldDB; Q9R1T9; -.
DR SMR; Q9R1T9; -.
DR STRING; 10116.ENSRNOP00000025518; -.
DR GlyGen; Q9R1T9; 1 site.
DR PaxDb; Q9R1T9; -.
DR PRIDE; Q9R1T9; -.
DR GeneID; 114032; -.
DR KEGG; rno:114032; -.
DR UCSC; RGD:621415; rat.
DR CTD; 23415; -.
DR RGD; 621415; Kcnh4.
DR eggNOG; KOG0498; Eukaryota.
DR InParanoid; Q9R1T9; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; Q9R1T9; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:Q9R1T9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
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; 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 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..1017
FT /note="Potassium voltage-gated channel subfamily H member
FT 4"
FT /id="PRO_0000054009"
FT TOPO_DOM 1..232
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 233..253
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 254..262
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..305
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 306..326
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 327..334
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..364
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 386..427
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 428..448
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 449..454
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 455..475
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 476..1017
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 14..90
FT /note="PAS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00140"
FT DOMAIN 93..145
FT /note="PAC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT REGION 139..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 690..749
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 972..1017
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 440..445
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 148..163
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 690..724
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 981..998
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1017
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 557..672
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 825
FT /note="R -> W (in Ref. 1; CAA07587)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1017 AA; 111404 MW; BFDB0F1B35437C9F CRC64;
MPVMKGLLAP QNTFLDTIAT RFDGTHSNFL LANAQGPRGF PIVYCSDGFC ELTGYGRTEV
MQKTCSCRFL YGPETSEPAL QRLQKALEGH QEHRAEICFY RKDGSAFWCL LDMMPIKNEL
GEVVLFLFSF KDISQSGGPG LGSPGIHGDN NNHENSLGRR GASSRLRSTR RQNRTVLHRL
TGHFGRRDQG SVKANSNVFE PKPSVPEYKV ASVGGSRCLL LHYSIPKAVW DGLILLATFY
VAVTVPYNVC FAGDDDTPIT SRHTLVSDIA VEMLFILDII LNFRTTYVSQ SGQVVSAPRS
IGLHYLATWF FVDLIAALPF DLLYVFNITV TSLVHLLKTV RLLRLLRLLQ KLERYSQCSA
VVLTLLMSVF ALLAHWMACV WYVIGRREME ANDPLLWDIG WLHELGKRLE EPYVNGSAGG
PSRRSAYIAA LYFTLSSLTS VGFGNVCANT DAEKIFSICT MLIGALMHAV VFGNVTAIIQ
RMYSRRSLYH SRMKDLKDFI RVHRLPRPLK QRMLEYFQTT WAVNSGIDAN ELLRDFPDEL
RADIAMHLNR EILQLPLFGA ASRGCLRALS LHIKTSFCAP GEFLLRRGDA LQAHYYVCSG
SLEVLRDNTV LAILGKGDLI GADIPELGQE PGAGAGCVLK TSADVKALTY CGLQQLSSRG
LAEVLRLYPE YVAAFRAGLP RDLTFNLRQG SENNGLGRFS RSPRLSQARS DTLGSSSDKT
LPSITETEGG MEPGAGSKPR RPLLLPNLSP ARPRGSLVSL LGEELPPFSA LVSSPSLSPT
PSPALAGRGS SPSLHGPPRG SAAWKPPQLL TPPLGTFGPP DLSPRIVDGI EDSSNTAEAP
TFRFSKRPEP TRTRSQAPLS GPRLSRELAT EAAEEVKEKV CRLNQEISRL NQEVSQLSRE
LRQVMGLLQA RLGPPSHPPD STWLPDLPCP HQRPPCISPH MSGPPPGLQN TTLAVVHCPA
SVGTVEIGAT PSELRSSMVP PFPSEPDPLG PSPVPEASPL TPSLLKHSFQ SGSDTFH
