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   24-JAN-2024, entry version 148.
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 18 dpc 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)
CC       (TC 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   GlyCosmos; Q9R1T9; 1 site, No reported glycans.
DR   GlyGen; Q9R1T9; 1 site.
DR   PhosphoSitePlus; Q9R1T9; -.
DR   PaxDb; 10116-ENSRNOP00000025518; -.
DR   GeneID; 114032; -.
DR   KEGG; rno:114032; -.
DR   UCSC; RGD:621415; rat.
DR   AGR; RGD:621415; -.
DR   CTD; 23415; -.
DR   RGD; 621415; Kcnh4.
DR   eggNOG; KOG0498; Eukaryota.
DR   InParanoid; Q9R1T9; -.
DR   OrthoDB; 66005at2759; -.
DR   PhylomeDB; Q9R1T9; -.
DR   Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR   PRO; PR:Q9R1T9; -.
DR   Proteomes; UP000002494; Unplaced.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
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:0042391; P:regulation of membrane potential; IBA:GO_Central.
DR   CDD; cd00038; CAP_ED; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.1200.260; -; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 2.60.120.10; Jelly Rolls; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR000595; cNMP-bd_dom.
DR   InterPro; IPR018490; cNMP-bd_dom_sf.
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   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR10217:SF630; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 4; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 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; cAMP-binding domain-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 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
//