ID   KCNH5_RAT               Reviewed;         988 AA.
AC   Q9EPI9; O88893; Q9QXT2;
DT   28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   24-JAN-2024, entry version 171.
DE   RecName: Full=Potassium voltage-gated channel subfamily H member 5;
DE   AltName: Full=Ether-a-go-go potassium channel 2;
DE            Short=rEAG2;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv10.2;
GN   Name=Kcnh5; Synonyms=Eag2;
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].
RC   STRAIN=Sprague-Dawley; TISSUE=Thalamus;
RX   PubMed=10594062; DOI=10.1523/jneurosci.19-24-10789.1999;
RA   Saganich M.J., Vega-Saenz de Miera E., Nadal M.S., Baker H., Coetzee W.A.,
RA   Rudy B.;
RT   "Cloning of components of a novel subthreshold-activating K+ channel with a
RT   unique pattern of expression in the cerebral cortex.";
RL   J. Neurosci. 19:10789-10802(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Cerebellum;
RX   PubMed=10882483; DOI=10.1006/mcne.2000.0851;
RA   Ludwig J., Weseloh R., Karschin C., Liu Q., Netzer R., Engeland B.,
RA   Stansfeld C., Pongs O.;
RT   "Cloning and functional expression of rat eag2, a new member of the ether-
RT   a-go-go family of potassium channels and comparison of its distribution
RT   with that of eag1.";
RL   Mol. Cell. Neurosci. 16:59-70(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 220-360.
RC   TISSUE=Brain;
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).
CC   -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC       channel. Elicits a non-inactivating outward rectifying current. 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. Heteromultimer with KCNH1/EAG
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC   -!- TISSUE SPECIFICITY: Detected in adult testis and in embryonic and adult
CC       brain, but not in other tissues. Highly expressed in specific brain
CC       areas, such as neocortex, olfactory bulb, primary olfactory cortex and
CC       brain stem. In cortex, expression is concentrated in a narrow band
CC       toward the middle lamella (layer IV). Moderately expressed in spinal
CC       cord, dorsal thalamic nuclei, medial hypothalamus, colliculus, lateral
CC       lemniscus, pontine nuclei and Islands of Calleja.
CC   -!- MISCELLANEOUS: The channel is down-regulated to 10% residual activity
CC       by 400 nano molar cytosolic calcium ions.
CC   -!- SIMILARITY: Belongs to the potassium channel family. H (Eag)
CC       (TC 1.A.1.20) subfamily. Kv10.2/KCNH5 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF185637; AAF19354.1; -; mRNA.
DR   EMBL; AJ250280; CAC20863.1; -; mRNA.
DR   EMBL; AF073891; AAC61521.1; -; mRNA.
DR   RefSeq; NP_598294.1; NM_133610.2.
DR   AlphaFoldDB; Q9EPI9; -.
DR   SMR; Q9EPI9; -.
DR   STRING; 10116.ENSRNOP00000013275; -.
DR   GlyCosmos; Q9EPI9; 1 site, No reported glycans.
DR   GlyGen; Q9EPI9; 1 site.
DR   iPTMnet; Q9EPI9; -.
DR   PhosphoSitePlus; Q9EPI9; -.
DR   SwissPalm; Q9EPI9; -.
DR   PaxDb; 10116-ENSRNOP00000013275; -.
DR   Ensembl; ENSRNOT00000013275.5; ENSRNOP00000013275.2; ENSRNOG00000009542.6.
DR   Ensembl; ENSRNOT00055034161; ENSRNOP00055027711; ENSRNOG00055020005.
DR   Ensembl; ENSRNOT00060048912; ENSRNOP00060040815; ENSRNOG00060028143.
DR   Ensembl; ENSRNOT00065031354; ENSRNOP00065024983; ENSRNOG00065018672.
DR   GeneID; 171146; -.
DR   KEGG; rno:171146; -.
DR   UCSC; RGD:621417; rat.
DR   AGR; RGD:621417; -.
DR   CTD; 27133; -.
DR   RGD; 621417; Kcnh5.
DR   eggNOG; KOG0501; Eukaryota.
DR   GeneTree; ENSGT00940000156540; -.
DR   HOGENOM; CLU_005746_3_1_1; -.
DR   InParanoid; Q9EPI9; -.
DR   OMA; PMNKTET; -.
DR   OrthoDB; 66005at2759; -.
DR   PhylomeDB; Q9EPI9; -.
DR   TreeFam; TF313130; -.
DR   Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR   PRO; PR:Q9EPI9; -.
DR   Proteomes; UP000002494; Chromosome 6.
DR   Bgee; ENSRNOG00000009542; Expressed in frontal cortex and 1 other cell type or tissue.
DR   GO; GO:0009986; C:cell surface; ISO:RGD.
DR   GO; GO:0034702; C:monoatomic ion channel complex; IEA:UniProtKB-KW.
DR   GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR   GO; GO:0044325; F:transmembrane transporter binding; IPI:RGD.
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:0010389; P:regulation of G2/M transition of mitotic cell cycle; ISO:RGD.
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; IPR003949; K_chnl_volt-dep_EAG.
DR   InterPro; IPR003938; K_chnl_volt-dep_EAG/ELK/ERG.
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:SF533; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY H MEMBER 5; 1.
DR   PANTHER; PTHR10217; VOLTAGE AND LIGAND GATED POTASSIUM CHANNEL; 1.
DR   Pfam; PF00027; cNMP_binding; 1.
DR   Pfam; PF00520; Ion_trans; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   PRINTS; PR01463; EAGCHANLFMLY.
DR   PRINTS; PR01464; EAGCHANNEL.
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   Genevisible; Q9EPI9; RN.
PE   2: Evidence at transcript level;
KW   Calmodulin-binding; Glycoprotein; Ion channel; Ion transport;
KW   Isopeptide bond; Membrane; Phosphoprotein; Potassium; Potassium channel;
KW   Potassium transport; Reference proteome; Transmembrane;
KW   Transmembrane helix; Transport; Ubl conjugation; Voltage-gated channel.
FT   CHAIN           1..988
FT                   /note="Potassium voltage-gated channel subfamily H member
FT                   5"
FT                   /id="PRO_0000054012"
FT   TOPO_DOM        1..217
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..243
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        244..264
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        265..291
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        292..312
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        313..319
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        341..346
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        347..367
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        368..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..446
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        447..467
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        468..988
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          14..86
FT                   /note="PAS"
FT   DOMAIN          91..143
FT                   /note="PAC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00141"
FT   REGION          704..715
FT                   /note="Calmodulin-binding"
FT                   /evidence="ECO:0000255"
FT   REGION          718..742
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          839..897
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..948
FT                   /note="CAD (involved in subunit assembly)"
FT                   /evidence="ECO:0000250"
FT   REGION          946..965
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           432..437
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        845..864
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..883
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         550..667
FT                   /ligand="a nucleoside 3',5'-cyclic phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58464"
FT   MOD_RES         883
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q920E3"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        785
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NCM2"
FT   CONFLICT        397
FT                   /note="G -> R (in Ref. 1; AAF19354)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   988 AA;  111830 MW;  888AE96759F64C4A CRC64;
     MPGGKRGLVA PQNTFLENIV RRSSESSFLL GNAQIVDWPV VYSNDGFCKL SGYHRADVMQ
     KSSTCSFMYG ELTDKKTIEK VRQTFDNYES NCFEVLLYKK NRTPVWFYMQ IAPIRNEHEK
     VVLFLCTFKD ITLFKQPIED DSTKGWTKFA RLTRALTNSR SVLQQLTPMN KTETVHKHSR
     LAEVLQLGSD ILPQYKQEAP KTPPHIILHY CAFKTTWDWV ILILTFYTAI MVPYNVSFKT
     KQNNIAWLVL DSVVDVIFLV DIVLNFHTTF VGPGGEVISD PKLIRMNYLK TWFVIDLLSC
     LPYDIINAFE NVDEGISSLF SSLKVVRLLR LGRVARKLDH YLEYGAAVLV LLVCVFGLVA
     HWLACIWYSI GDYEVIDEVT NTIQIDSWLY QLALSIGTPY RYNTSAGIWE GGPSKDSLYV
     SSLYFTMTSL TTIGFGNIAP TTDVEKMFSV AMMMVGSLLY ATIFGNVTTI FQQMYANTNR
     YHEMLNNVRD FLKLYQVPKG LSERVMDYIV STWSMSKGID TEKVLSICPK DMRADICVHL
     NRKVFNEHPA FRLASDGCLR ALAVEFQTIH CAPGDLIYHA GESVDALCFV VSGSLEVIQD
     EEVVAILGKG DVFGDIFWKE TTLAHACANV RALTYCDLHI IKREALLKVL DFYTAFANSF
     SRNLTLTCNL RKRIIFRKIS DVKKEEEERL RQKNEVTLSI PVDHPVRKLF QKFKQQKELR
     NQGSAQSDPE RSQLQVESRP LQNGASITGT SVVTVSQITP IQTSLAYVKT SETLKQNNRD
     AMELKPNGGA EPKCLKVNSP IRMKNGNGKG WLRLKNNMGA HEEKKEEWNN VTKAESMGLL
     SEDPKGSDSE NSVTKNPLRK TDSCDSGITK SDLRLDKAGE ARSPLEHSPS QADAKHPFYP
     IPEQALQTTL QEVKHELKED IQLLSCRMTA LEKQVAEILK LLSEKSVPQT SSPKPQIPLQ
     VPPQIPCQDI FSVSRPESPE SDKDEINF
//