KCNH5_MOUSE
ID KCNH5_MOUSE Reviewed; 988 AA.
AC Q920E3; E9QPM0; Q8C035;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 5;
DE AltName: Full=Ether-a-go-go potassium channel 2;
DE Short=Eag2;
DE AltName: Full=Voltage-gated potassium channel subunit Kv10.2;
GN Name=Kcnh5; Synonyms=Eag2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 32-203.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RA Saganich M.J., Vega-Saenz de Miera E.C., Rudy B.;
RT "Cloning of the mouse eag2 potassium channel.";
RL Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-883, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Pore-forming (alpha) subunit of voltage-gated potassium
CC channel. Elicits a non-inactivating outward rectifying current (By
CC similarity). Channel properties may be modulated by cAMP and subunit
CC assembly. {ECO:0000250}.
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 -!- 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. Kv10.2/KCNH5 sub-subfamily. {ECO:0000305}.
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DR EMBL; AK032438; BAC27869.1; -; mRNA.
DR EMBL; AC110175; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131762; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CT010432; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF309565; AAL09442.1; -; mRNA.
DR CCDS; CCDS25980.1; -.
DR RefSeq; NP_766393.2; NM_172805.3.
DR AlphaFoldDB; Q920E3; -.
DR SMR; Q920E3; -.
DR BioGRID; 231963; 2.
DR STRING; 10090.ENSMUSP00000046864; -.
DR GlyGen; Q920E3; 1 site.
DR iPTMnet; Q920E3; -.
DR PhosphoSitePlus; Q920E3; -.
DR PaxDb; Q920E3; -.
DR PRIDE; Q920E3; -.
DR ProteomicsDB; 263496; -.
DR Antibodypedia; 11594; 60 antibodies from 18 providers.
DR DNASU; 238271; -.
DR Ensembl; ENSMUST00000042299; ENSMUSP00000046864; ENSMUSG00000034402.
DR GeneID; 238271; -.
DR KEGG; mmu:238271; -.
DR UCSC; uc007nwz.2; mouse.
DR CTD; 27133; -.
DR MGI; MGI:3584508; Kcnh5.
DR VEuPathDB; HostDB:ENSMUSG00000034402; -.
DR eggNOG; KOG0501; Eukaryota.
DR GeneTree; ENSGT00940000156540; -.
DR HOGENOM; CLU_005746_3_1_1; -.
DR InParanoid; Q920E3; -.
DR OMA; EKKEEWN; -.
DR OrthoDB; 464006at2759; -.
DR PhylomeDB; Q920E3; -.
DR TreeFam; TF313130; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 238271; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Kcnh5; mouse.
DR PRO; PR:Q920E3; -.
DR Proteomes; UP000000589; Chromosome 12.
DR RNAct; Q920E3; protein.
DR Bgee; ENSMUSG00000034402; Expressed in superior frontal gyrus and 60 other tissues.
DR Genevisible; Q920E3; MM.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
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:MGI.
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 1: Evidence at protein 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_0000054011"
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 721..741
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 838..893
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 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..668
FT /ligand="a nucleoside 3',5'-cyclic phosphate"
FT /ligand_id="ChEBI:CHEBI:58464"
FT MOD_RES 883
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
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 552
FT /note="R -> Q (in Ref. 1; BAC27869)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 111810 MW; 8CC29099AFC4755A 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
IQGSAQSDPE RSQLQVESRP LQNGASITGT SVVTVSQITP IQTSLAYVKT SESLKQNNRD
AMELKPNGGA EPKCLKVNSP IRMKNGNGKG WLRLKNNMGA QEEKKEDWNN VTKAESMGLL
SEDPKGSDSE NSVTKNPLRK TDSCDSGITK SDLRLDKAGE ARSPLEHSPS QADVKHSFYP
IPEQALQTTL QEVKHELKED IQLLSCRMTA LEKQVAEILK LLSEKSVPQT SSPKPQIPLQ
VPPQIPCQDI FSVSRPESPE SDKDEINF
