KCNH5_RAT
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 03-AUG-2022, entry version 163.
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) (TC
CC 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 GlyGen; Q9EPI9; 1 site.
DR iPTMnet; Q9EPI9; -.
DR PhosphoSitePlus; Q9EPI9; -.
DR PaxDb; Q9EPI9; -.
DR PRIDE; Q9EPI9; -.
DR Ensembl; ENSRNOT00000013275; ENSRNOP00000013275; ENSRNOG00000009542.
DR GeneID; 171146; -.
DR KEGG; rno:171146; -.
DR UCSC; RGD:621417; rat.
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; EKKEEWN; -.
DR OrthoDB; 464006at2759; -.
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 tissue.
DR Genevisible; Q9EPI9; RN.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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: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; IPR030171; EAG2.
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 PANTHER; PTHR10217:SF533; PTHR10217:SF533; 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; 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 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
