KCNH3_RAT
ID KCNH3_RAT Reviewed; 1087 AA.
AC O89047;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 3;
DE AltName: Full=Brain-specific eag-like channel 1;
DE Short=BEC1;
DE AltName: Full=Ether-a-go-go-like potassium channel 2;
DE Short=ELK channel 2;
DE Short=rElk2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv12.2;
GN Name=Kcnh3; Synonyms=Elk2;
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 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 NUCLEOTIDE SEQUENCE [MRNA] OF 120-273.
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).
RN [4]
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).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits an outward current with fast 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 and embryonic brain, in
CC particular in cerebellum, brain stem, hippocampus, cortex and striatum.
CC Detected at slightly lower levels in heart, spinal cord, olfactory
CC bulb, pituitary and medulla. In the hippocampus expression is strongest
CC in the pyramidal cell body layers of the dentate gyrus. Also found in
CC pituitary. {ECO:0000269|PubMed:10718922}.
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. Kv12.2/KCNH3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AJ007627; CAA07586.1; -; mRNA.
DR EMBL; AB022697; BAA83591.1; -; mRNA.
DR EMBL; AF073892; AAC61522.1; -; mRNA.
DR PIR; T31100; T31100.
DR RefSeq; NP_058804.1; NM_017108.1.
DR AlphaFoldDB; O89047; -.
DR SMR; O89047; -.
DR STRING; 10116.ENSRNOP00000047211; -.
DR GlyGen; O89047; 3 sites.
DR PaxDb; O89047; -.
DR Ensembl; ENSRNOT00000086611; ENSRNOP00000071001; ENSRNOG00000057315.
DR GeneID; 27150; -.
DR KEGG; rno:27150; -.
DR UCSC; RGD:71070; rat.
DR CTD; 23416; -.
DR RGD; 71070; Kcnh3.
DR eggNOG; KOG0498; Eukaryota.
DR GeneTree; ENSGT00940000161742; -.
DR HOGENOM; CLU_005746_6_0_1; -.
DR InParanoid; O89047; -.
DR OMA; YIGQQEI; -.
DR OrthoDB; 247304at2759; -.
DR PhylomeDB; O89047; -.
DR TreeFam; TF313130; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:O89047; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000057315; Expressed in frontal cortex and 8 other tissues.
DR Genevisible; O89047; RN.
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; 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.
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..1087
FT /note="Potassium voltage-gated channel subfamily H member
FT 3"
FT /id="PRO_0000054007"
FT TOPO_DOM 1..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..259
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 260..280
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 281..302
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 324..331
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 332..352
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 353..361
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 362..382
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..456
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 457..477
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 478..482
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 483..503
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 504..1087
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..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 137..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 975..1061
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 468..473
FT /note="Selectivity filter"
FT /evidence="ECO:0000250"
FT COMPBIAS 137..154
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 756..771
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1008
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 585..700
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 428
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1087 AA; 117580 MW; 16B5AFFC3B0A405B CRC64;
MPAMRGLLAP QNTFLDTIAT RFDGTHSNFV LGNAQVAGLF PVVYCSDGFC DLTGFSRAEV
MQRGCACSFL YGPDTSELVR QQIRKALDEH KEFKAELILY RKSGLPFWCL LDVIPIKNEK
GEVALFLVSH KDISETKNRG GPDNWKERGG GRRRYGRAGS KGFNANRRRS RAVLYHLSGH
LQKQPKGKHK LNKGVFGEKP NLPEYKVAAI RKSPFILLHC GALRATWDGF ILLATLYVAV
TVPYSVCVST AREPSAARGP PSVCDLAVEV LFILDIVLNF RTTFVSKSGQ VVFAPKSICL
HYVTTWFLLD VIAALPFDLL HAFKVNVYVG AHLLKTVRLL RLLRLLPRLD RYSQYSAVVL
TLLMAVFALL AHWVACVWFY IGQQEIENSE SELPEIGWLQ ELARRLETPY YLVSRSPDGG
NSSGQSENCS SSGGGSEANG TGLELLGGPS LRSAYITSLY FALSSLTSVG FGNVSANTDT
EKIFSICTML IGALMHAVVF GNVTAIIQRM YARRFLYHSR TRDLRDYIRI HRIPKPLKQR
MLEYFQATWA VNNGIDTTEL LQSLPDELRA DIAMHLHKEV LQLPLFEAAS RGCLRALSLA
LRPAFCTPGE YLIHQGDALQ ALYFVCSGSM EVLKGGTVLA ILGKGDLIGC ELPQREQVVK
ANADVKGLTY CVLQCLQLAG LHESLALYPE FAPRFSRGLR GELSYNLGAG GVSAEVDTSS
LSGDNTLMST LEEKETDGEQ GHTISPAPAD EPSSPLLSPG CTSSSSAAKL LSPRRTAPRP
RLGGRGRPSR AGVLKPEAGP SAHPRTLDGL QLPPMPWNVP PDLSPRVVDG IEDGCGSDQH
KFSFRVGQSG PECSSSPSPG TESGLLTVPL VPSEARNTDT LDKLRQAVTE LSEQVLQMRE
GLQSLRQAVQ LILVPQGEGQ CPRVSGEGPC PATASGLLQP LRVDTGASSY CLQPPAGSVL
SGTWPHPRPG HPPPLMAPWP WGPPASQSSP WPRATALWTS TSDSEPPGSG DLCSEPSTPA
SPPPPEEGAR TGTPAPVSQA EATSTGEPPP GSGGRALPWD PHSLEMVLIG CHGPGSVQWT
QEEGTGV
