KCNH1_MOUSE
ID KCNH1_MOUSE Reviewed; 989 AA.
AC Q60603; Q32MR6; Q3USQ9;
DT 28-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=Potassium voltage-gated channel subfamily H member 1;
DE AltName: Full=Ether-a-go-go potassium channel 1;
DE Short=EAG channel 1;
DE Short=EAG1;
DE Short=m-eag;
DE AltName: Full=Voltage-gated potassium channel subunit Kv10.1;
GN Name=Kcnh1; Synonyms=Eag;
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 [MRNA].
RC TISSUE=Brain;
RX PubMed=8159766; DOI=10.1073/pnas.91.8.3438;
RA Warmke J.W., Ganetzky B.;
RT "A family of potassium channel genes related to eag in Drosophila and
RT mammals.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3438-3442(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAE24272.1};
RC TISSUE=Corpora quadrigemina {ECO:0000312|EMBL:BAE24272.1};
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP ACTIVITY REGULATION, LACK OF CYCLIC NUCLEOTIDE BINDING, FUNCTION,
RP SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=19671703; DOI=10.1074/jbc.m109.016337;
RA Brelidze T.I., Carlson A.E., Zagotta W.N.;
RT "Absence of direct cyclic nucleotide modulation of mEAG1 and hERG1 channels
RT revealed with fluorescence and electrophysiological methods.";
RL J. Biol. Chem. 284:27989-27997(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-974; SER-978 AND SER-981, AND
RP IDENTIFICATION BY 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).
RN [7]
RP INTERACTION WITH RABEP1.
RX PubMed=22841712; DOI=10.1016/j.febslet.2012.07.055;
RA Ninkovic M., Mitkovski M., Kohl T., Stuhmer W., Pardo L.A.;
RT "Physical and functional interaction of KV10.1 with Rabaptin-5 impacts ion
RT channel trafficking.";
RL FEBS Lett. 586:3077-3084(2012).
RN [8]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=23424202; DOI=10.1093/hmg/ddt076;
RA Ufartes R., Schneider T., Mortensen L.S., de Juan Romero C., Hentrich K.,
RA Knoetgen H., Beilinson V., Moebius W., Tarabykin V., Alves F., Pardo L.A.,
RA Rawlins J.N., Stuehmer W.;
RT "Behavioural and functional characterization of Kv10.1 (Eag1) knockout
RT mice.";
RL Hum. Mol. Genet. 22:2247-2262(2013).
RN [9]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25556795; DOI=10.1113/jphysiol.2014.281600;
RA Mortensen L.S., Schmidt H., Farsi Z., Barrantes-Freer A., Rubio M.E.,
RA Ufartes R., Eilers J., Sakaba T., Stuehmer W., Pardo L.A.;
RT "KV 10.1 opposes activity-dependent increase in Ca2+ influx into the
RT presynaptic terminal of the parallel fibre-Purkinje cell synapse.";
RL J. Physiol. (Lond.) 593:181-196(2015).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 552-707, DOMAIN,
RP CALMODULIN-BINDING REGION, AND MUTAGENESIS OF VAL-628; 697-LEU--TYR-699;
RP TYR-699; 699-TYR--LEU-701 AND 705-ILE--PHE-707.
RX PubMed=22732247; DOI=10.1016/j.jmb.2012.06.025;
RA Marques-Carvalho M.J., Sahoo N., Muskett F.W., Vieira-Pires R.S.,
RA Gabant G., Cadene M., Schonherr R., Morais-Cabral J.H.;
RT "Structural, biochemical, and functional characterization of the cyclic
RT nucleotide binding homology domain from the mouse EAG1 potassium channel.";
RL J. Mol. Biol. 423:34-46(2012).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 6-136 AND 552-724, FUNCTION,
RP SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF 7-ARG-ARG-8; ARG-57;
RP GLU-627 AND ASP-642.
RX PubMed=23975098; DOI=10.1038/nature12487;
RA Haitin Y., Carlson A.E., Zagotta W.N.;
RT "The structural mechanism of KCNH-channel regulation by the eag domain.";
RL Nature 501:444-448(2013).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 28-137.
RX PubMed=23555008; DOI=10.1371/journal.pone.0059265;
RA Adaixo R., Harley C.A., Castro-Rodrigues A.F., Morais-Cabral J.H.;
RT "Structural properties of PAS domains from the KCNH potassium channels.";
RL PLoS ONE 8:E59265-E59265(2013).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 727-743 IN COMPLEX WITH CALM,
RP MUTAGENESIS OF VAL-737; LEU-740 AND PHE-741, AND INTERACTION WITH CALM.
RX PubMed=27618660; DOI=10.1016/j.str.2016.07.020;
RA Marques-Carvalho M.J., Oppermann J., Munoz E., Fernandes A.S., Gabant G.,
RA Cadene M., Heinemann S.H., Schoenherr R., Morais-Cabral J.H.;
RT "Molecular insights into the mechanism of calmodulin inhibition of the EAG1
RT potassium channel.";
RL Structure 24:1742-1754(2016).
CC -!- FUNCTION: Pore-forming (alpha) subunit of a voltage-gated delayed
CC rectifier potassium channel (PubMed:19671703, PubMed:23975098). Channel
CC properties are modulated by subunit assembly. Mediates IK(NI) current
CC in myoblasts. Involved in the regulation of cell proliferation and
CC differentiation, in particular adipogenic and osteogenic
CC differentiation in bone marrow-derived mesenchymal stem cells (MSCs)
CC (By similarity). {ECO:0000250|UniProtKB:O95259,
CC ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:23975098}.
CC -!- ACTIVITY REGULATION: Channel activity is inhibited by interaction with
CC Ca(2+)-bound calmodulin. Interaction of a single pore-forming alpha
CC subunit with a calmodulin chain is sufficient to promote channel
CC closure (By similarity). Channel activity is not regulated by cyclic
CC nucleotides (PubMed:19671703). Channel activity is inhibited by binding
CC intracellular phosphatidylinositol-3,5-bisphosphate and
CC phosphatidylinositol-4,5-bisphosphate (PIP2), but is not inhibited by
CC phosphatidylinositol 4-phosphate (By similarity).
CC {ECO:0000250|UniProtKB:O95259, ECO:0000269|PubMed:19671703}.
CC -!- SUBUNIT: The potassium channel is composed of a homo- or
CC heterotetrameric complex of pore-forming alpha subunits that can
CC associate with modulating beta subunits. Heteromultimer with KCNH5/EAG2
CC (By similarity). Interacts with ALG10B (By similarity). Interacts with
CC RABEP1 (PubMed:22841712). Interacts (via C-terminus) with CTTN.
CC Interacts (via C-terminal cytoplasmic region) with Ca(2+)-bound
CC calmodulin (PubMed:27618660). {ECO:0000250|UniProtKB:O95259,
CC ECO:0000269|PubMed:22841712, ECO:0000269|PubMed:27618660}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19671703,
CC ECO:0000269|PubMed:23975098}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O95259}. Nucleus inner membrane
CC {ECO:0000250|UniProtKB:O95259}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:O95259}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:Q63472}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q63472}. Presynaptic cell membrane
CC {ECO:0000269|PubMed:25556795}. Perikaryon
CC {ECO:0000250|UniProtKB:Q63472}. Postsynaptic density membrane
CC {ECO:0000250|UniProtKB:Q63472}. Early endosome membrane
CC {ECO:0000250|UniProtKB:O95259}. Note=Perinuclear KCNH1 is located to
CC NPC-free islands. {ECO:0000250|UniProtKB:O95259}.
CC -!- TISSUE SPECIFICITY: Detected in brain (at protein level)
CC (PubMed:23424202, PubMed:25556795). Highly expressed in olfactory bulb.
CC Detected in brain cortex, hippocampus, brain stem, striatum, thalamus,
CC hypothalamus and spinal cord (PubMed:23424202).
CC {ECO:0000269|PubMed:23424202, ECO:0000269|PubMed:25556795}.
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. {ECO:0000250|UniProtKB:Q63472}.
CC -!- DOMAIN: The C-terminal region interacts with the cyclic nucleotide-
CC binding domain and contributes to regulate channel gating.
CC {ECO:0000269|PubMed:23975098, ECO:0000305|PubMed:22732247}.
CC -!- DOMAIN: The PAS and PAC domain interact with the cyclic nucleotide-
CC binding domain and contribute to the regulation of channel gating
CC (PubMed:23975098). Calmodulin binding clamps together the PAS and PAC
CC domain with the cyclic nucleotide-binding domain from a neighboring
CC subunit and causes a conformation change that leads to channel closure.
CC {ECO:0000250|UniProtKB:Q63472, ECO:0000269|PubMed:23975098}.
CC -!- DOMAIN: The cyclic nucleotide-binding domain lacks residues that are
CC essential for nucleotide-binding and cannot bind cyclic nucleotides
CC (PubMed:19671703). Instead, residues from the C-terminal domain (the
CC so-called intrinsic ligand) bind in the cavity that would be expected
CC to bind cyclic nucleotides. Interaction with the C-terminal region
CC hinders interaction with CALM and reduces the affinity for CALM.
CC {ECO:0000269|PubMed:19671703, ECO:0000269|PubMed:22732247,
CC ECO:0000269|PubMed:23975098}.
CC -!- PTM: Channel activity is regulated via tyrosine
CC phosphorylation/dephosphorylation by SRC and PTPN6.
CC {ECO:0000250|UniProtKB:O95259}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype. Mice are viable and
CC fertile, and have normal brain morphology. Likewise, there is no change
CC in the electrophysiological properties of cerebellar Purkinje cells and
CC in the shape and frequency of action potentials.
CC {ECO:0000269|PubMed:23424202}.
CC -!- SIMILARITY: Belongs to the potassium channel family. H (Eag) (TC
CC 1.A.1.20) subfamily. Kv10.1/KCNH1 sub-subfamily. {ECO:0000305}.
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DR EMBL; U04294; AAA62474.1; -; mRNA.
DR EMBL; AK140193; BAE24272.1; -; mRNA.
DR EMBL; CH466555; EDL12967.1; -; Genomic_DNA.
DR EMBL; BC109013; AAI09014.1; -; mRNA.
DR CCDS; CCDS15627.1; -.
DR PIR; I48912; I48912.
DR RefSeq; NP_034730.1; NM_010600.3.
DR PDB; 4F8A; X-ray; 2.20 A; A=552-707.
DR PDB; 4HOI; X-ray; 1.85 A; A/B/C/D=28-137.
DR PDB; 4LLO; X-ray; 2.00 A; A/C/E/G=552-724, B/D/F/H=6-136.
DR PDB; 5HIT; X-ray; 2.85 A; B=727-743.
DR PDBsum; 4F8A; -.
DR PDBsum; 4HOI; -.
DR PDBsum; 4LLO; -.
DR PDBsum; 5HIT; -.
DR AlphaFoldDB; Q60603; -.
DR SMR; Q60603; -.
DR BioGRID; 200892; 4.
DR IntAct; Q60603; 1.
DR MINT; Q60603; -.
DR STRING; 10090.ENSMUSP00000077563; -.
DR GlyGen; Q60603; 2 sites.
DR iPTMnet; Q60603; -.
DR PhosphoSitePlus; Q60603; -.
DR PaxDb; Q60603; -.
DR PRIDE; Q60603; -.
DR ProteomicsDB; 269200; -.
DR DNASU; 16510; -.
DR GeneID; 16510; -.
DR KEGG; mmu:16510; -.
DR UCSC; uc007edo.2; mouse.
DR CTD; 3756; -.
DR MGI; MGI:1341721; Kcnh1.
DR eggNOG; KOG0501; Eukaryota.
DR InParanoid; Q60603; -.
DR OrthoDB; 464006at2759; -.
DR PhylomeDB; Q60603; -.
DR TreeFam; TF313130; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 16510; 4 hits in 71 CRISPR screens.
DR ChiTaRS; Kcnh1; mouse.
DR PRO; PR:Q60603; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q60603; protein.
DR Genevisible; Q60603; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030673; C:axolemma; ISO:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR GO; GO:0099056; C:integral component of presynaptic membrane; ISO:MGI.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005637; C:nuclear inner membrane; ISO:MGI.
DR GO; GO:0098688; C:parallel fiber to Purkinje cell synapse; IDA:SynGO.
DR GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0098839; C:postsynaptic density membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034705; C:potassium channel complex; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0071889; F:14-3-3 protein binding; ISO:MGI.
DR GO; GO:0005516; F:calmodulin binding; ISO:MGI.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:1902936; F:phosphatidylinositol bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0099508; F:voltage-gated ion channel activity involved in regulation of presynaptic membrane potential; IDA:SynGO.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071277; P:cellular response to calcium ion; ISS:UniProtKB.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0048015; P:phosphatidylinositol-mediated signaling; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; ISS:UniProtKB.
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 GO; GO:0099509; P:regulation of presynaptic cytosolic calcium ion concentration; IDA:SynGO.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IDA:SynGO.
DR GO; GO:0001964; P:startle response; ISO:MGI.
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; IPR030170; EAG1.
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:SF530; PTHR10217:SF530; 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.
DR PROSITE; PS50112; PAS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calmodulin-binding; Cell membrane; Cell projection; Endosome;
KW Glycoprotein; Ion channel; Ion transport; Lipid-binding; Membrane; Nucleus;
KW Phosphoprotein; Postsynaptic cell membrane; Potassium; Potassium channel;
KW Potassium transport; Reference proteome; Synapse; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..989
FT /note="Potassium voltage-gated channel subfamily H member
FT 1"
FT /id="PRO_0000053995"
FT TOPO_DOM 1..220
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 221..241
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 242..248
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 249..269
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 270..290
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 291..309
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 310..345
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 346..368
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 369..377
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 378..399
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 400..448
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT INTRAMEM 449..470
FT /note="Pore-forming; Name=Segment H5"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 471..477
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TRANSMEM 478..498
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT TOPO_DOM 499..989
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT DOMAIN 14..94
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 151..162
FT /note="Required for phosphatidylinositol bisphosphate
FT binding"
FT /evidence="ECO:0000250|UniProtKB:O95259"
FT REGION 673..770
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000269|PubMed:22732247,
FT ECO:0000269|PubMed:27618660"
FT REGION 699..701
FT /note="Interaction with cyclic nucleotide-binding pocket"
FT /evidence="ECO:0000269|PubMed:22732247"
FT REGION 857..905
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 924..964
FT /note="CAD (involved in subunit assembly)"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT REGION 961..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 463..468
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q63472"
FT COMPBIAS 857..874
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 881..897
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 961..975
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 974
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 978
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 981
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 415
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 433
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 7..8
FT /note="RR->AA,EE: Strongly shifts the voltage-dependent
FT channel activation to more depolarized membrane
FT potentials."
FT /evidence="ECO:0000269|PubMed:23975098"
FT MUTAGEN 57
FT /note="R->D: Decreases the rate of channel opening. No
FT effect; when associated with R-642."
FT /evidence="ECO:0000269|PubMed:23975098"
FT MUTAGEN 627
FT /note="E->A,R: Strongly shifts the voltage-dependent
FT channel activation to much more depolarized membrane
FT potentials."
FT /evidence="ECO:0000269|PubMed:23975098"
FT MUTAGEN 628
FT /note="V->A,L: Mildly increases the affinity for CALM."
FT /evidence="ECO:0000269|PubMed:22732247"
FT MUTAGEN 642
FT /note="D->R: Decreases the rate of channel opening. No
FT effect; when associated with D-57."
FT /evidence="ECO:0000269|PubMed:23975098"
FT MUTAGEN 697..699
FT /note="LTY->ATA: Increases the affinity for CALM."
FT /evidence="ECO:0000269|PubMed:22732247"
FT MUTAGEN 699..701
FT /note="YNL->ANA: Increases the affinity for CALM."
FT /evidence="ECO:0000269|PubMed:22732247"
FT MUTAGEN 699
FT /note="Y->W: Mildly increases the affinity for CALM."
FT /evidence="ECO:0000269|PubMed:22732247"
FT MUTAGEN 705..707
FT /note="IVF->AAA: Decreases the affinity for CALM."
FT /evidence="ECO:0000269|PubMed:22732247"
FT MUTAGEN 737
FT /note="V->A: No effect on affinity for CALM; when
FT associated with A-740."
FT /evidence="ECO:0000269|PubMed:27618660"
FT MUTAGEN 737
FT /note="V->S: Decreases affinity for CALM 230-fold; when
FT associated with S-740."
FT /evidence="ECO:0000269|PubMed:27618660"
FT MUTAGEN 740
FT /note="L->A: No effect on affinity for CALM; when
FT associated with A-737."
FT /evidence="ECO:0000269|PubMed:27618660"
FT MUTAGEN 740
FT /note="L->S: Decreases affinity for CALM 230-fold; when
FT associated with S-737."
FT /evidence="ECO:0000269|PubMed:27618660"
FT MUTAGEN 741
FT /note="F->S: Decreases affinity for CALM about 30-fold."
FT /evidence="ECO:0000269|PubMed:27618660"
FT CONFLICT 808
FT /note="V -> M (in Ref. 1; AAA62474 and 2; BAE24272)"
FT HELIX 17..22
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4HOI"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:4HOI"
FT HELIX 47..53
FT /evidence="ECO:0007829|PDB:4HOI"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:4HOI"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:4HOI"
FT HELIX 77..88
FT /evidence="ECO:0007829|PDB:4HOI"
FT STRAND 93..100
FT /evidence="ECO:0007829|PDB:4HOI"
FT STRAND 106..117
FT /evidence="ECO:0007829|PDB:4HOI"
FT STRAND 123..132
FT /evidence="ECO:0007829|PDB:4HOI"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:4HOI"
FT STRAND 555..559
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 565..571
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 573..576
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 580..582
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 587..596
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 598..602
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 607..609
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 613..615
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 617..624
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 626..630
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 633..638
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 643..645
FT /evidence="ECO:0007829|PDB:4LLO"
FT TURN 647..651
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 658..673
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 674..683
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 685..694
FT /evidence="ECO:0007829|PDB:4LLO"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 710..718
FT /evidence="ECO:0007829|PDB:4LLO"
FT HELIX 736..741
FT /evidence="ECO:0007829|PDB:5HIT"
SQ SEQUENCE 989 AA; 111282 MW; AEC4C730E253DDC1 CRC64;
MTMAGGRRGL VAPQNTFLEN IVRRSNDTNF VLGNAQIVDW PIVYSNDGFC KLSGYHRAEV
MQKSSACSFM YGELTDKDTV EKVRQTFENY EMNSFEILMY KKNRTPVWFF VKIAPIRNEQ
DKVVLFLCTF SDITAFKQPI EDDSCKGWGK FARLTRALTS SRGVLQQLAP SVQKGENVHK
HSRLAEVLQL GSDILPQYKQ EAPKTPPHII LHYCVFKTTW DWIILILTFY TAILVPYNVS
FKTRQNNVAW LVVDSIVDVI FLVDIVLNFH TTFVGPAGEV ISDPKLIRMN YLKTWFVIDL
LSCLPYDVIN AFENVDEVSA FMGDPGKIGF ADQIPPPLEG RESQGISSLF SSLKVVRLLR
LGRVARKLDH YIEYGAAVLV LLVCVFGLAA HWMACIWYSI GDYEIFDEDT KTIRNNSWLY
QLALDIGTPY QFNGSGSGKW EGGPSKNSVY ISSLYFTMTS LTSVGFGNIA PSTDIEKIFA
VAIMMIGSLL YATIFGNVTT IFQQMYANTN RYHEMLNSVR DFLKLYQVPK GLSERVMDYI
VSTWSMSRGI DTEKVLQICP KDMRADICVH LNRKVFKEHP AFRLASDGCL RALAMEFQTV
HCAPGDLIYH AGESVDSLCF VVSGSLEVIQ DDEVVAILGK GDVFGDVFWK EATLAQSCAN
VRALTYCDLH VIKRDALQKV LEFYTAFSHS FSRNLILTYN LRKRIVFRKI SDVKREEEER
MKRKNEAPLI LPPDHPVRRL FQRFRQQKEA RLAAERGGRD LDDLDVEKGN ALTDHTSANH
SLVKASVVTV RESPATPVSF QAATTSTVSD HAKLHAPGSE CLGPKAVSCD PAKRKGWARF
KDACGKGEDW NKVSKAESME TLPERTKAPG EATLKKTDSC DSGITKSDLR LDNVGETRSP
QDRSPILAEV KHSFYPIPEQ TLQATVLEVK YELKEDIKAL NAKMTSIEKQ LSEILRILMS
RGSAQSPQET GEISRPQSPE SDRDIFGAS
