ID KCNG1_HUMAN Reviewed; 513 AA. AC Q9UIX4; A8K3S4; O43528; Q5JXL5; Q9BRC1; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=Potassium voltage-gated channel subfamily G member 1; DE AltName: Full=Voltage-gated potassium channel subunit Kv6.1; DE AltName: Full=kH2; GN Name=KCNG1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=9434767; DOI=10.1006/bbrc.1997.7830; RA Su K., Kyaw H., Fan P., Zeng Z., Shell B.K., Carter K.C., Li Y.; RT "Isolation, characterization, and mapping of two human potassium RT channels."; RL Biochem. Biophys. Res. Commun. 241:675-681(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11780052; DOI=10.1038/414865a; RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 20."; RL Nature 414:865-871(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Muscle; 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 [6] RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=19074135; DOI=10.1074/jbc.m808786200; RA Mederos y Schnitzler M., Rinne S., Skrobek L., Renigunta V., RA Schlichthorl G., Derst C., Gudermann T., Daut J., Preisig-Muller R.; RT "Mutation of histidine 105 in the T1 domain of the potassium channel Kv2.1 RT disrupts heteromerization with Kv6.3 and Kv6.4."; RL J. Biol. Chem. 284:4695-4704(2009). CC -!- FUNCTION: Potassium channel subunit that does not form functional CC channels by itself. Can form functional heterotetrameric channels with CC KCNB1; modulates the delayed rectifier voltage-gated potassium channel CC activation and deactivation rates of KCNB1 (PubMed:19074135). CC {ECO:0000269|PubMed:19074135}. CC -!- SUBUNIT: Heterotetramer with KCNB1 (PubMed:19074135). CC {ECO:0000269|PubMed:19074135}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19074135}; CC Multi-pass membrane protein {ECO:0000305}. Note=Colocalizes with KCNB1 CC at the plasma membrane (PubMed:19074135). CC {ECO:0000269|PubMed:19074135}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9UIX4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9UIX4-2; Sequence=VSP_001024, VSP_001025; CC -!- TISSUE SPECIFICITY: Expressed in brain and placenta, and at much lower CC levels in kidney and pancreas (PubMed:9434767). CC {ECO:0000269|PubMed:9434767}. CC -!- DOMAIN: The transmembrane segment S4 functions as a voltage-sensor and CC is characterized by a series of positively charged amino acids at every CC third position. Channel opening and closing is effected by a CC conformation change that affects the position and orientation of the CC voltage-sensor paddle formed by S3 and S4 within the membrane. A CC transmembrane electric field that is positive inside would push the CC positively charged S4 segment outwards, thereby opening the pore, while CC a field that is negative inside would pull the S4 segment inwards and CC close the pore. Changes in the position and orientation of S4 are then CC transmitted to the activation gate formed by the inner helix bundle via CC the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}. CC -!- SIMILARITY: Belongs to the potassium channel family. G (TC 1.A.1.2) CC subfamily. Kv6.1/KCNG1 sub-subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF033383; AAC05635.1; -; mRNA. DR EMBL; AK290689; BAF83378.1; -; mRNA. DR EMBL; AL050404; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL121785; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471077; EAW75605.1; -; Genomic_DNA. DR EMBL; BC006367; AAH06367.1; -; mRNA. DR CCDS; CCDS13436.1; -. [Q9UIX4-1] DR PIR; JC5920; JC5920. DR RefSeq; NP_002228.2; NM_002237.3. [Q9UIX4-1] DR RefSeq; XP_006723848.1; XM_006723785.2. [Q9UIX4-1] DR RefSeq; XP_011527102.1; XM_011528800.1. [Q9UIX4-1] DR RefSeq; XP_011527103.1; XM_011528801.1. [Q9UIX4-1] DR RefSeq; XP_011527104.1; XM_011528802.1. [Q9UIX4-1] DR RefSeq; XP_011527105.1; XM_011528803.2. [Q9UIX4-1] DR RefSeq; XP_011527106.1; XM_011528804.1. [Q9UIX4-1] DR RefSeq; XP_011527107.1; XM_011528805.2. DR RefSeq; XP_011527108.1; XM_011528806.1. [Q9UIX4-1] DR AlphaFoldDB; Q9UIX4; -. DR SMR; Q9UIX4; -. DR BioGRID; 109957; 22. DR IntAct; Q9UIX4; 4. DR STRING; 9606.ENSP00000360626; -. DR ChEMBL; CHEMBL2362996; -. DR DrugBank; DB00228; Enflurane. DR DrugBank; DB01110; Miconazole. DR DrugBank; DB01069; Promethazine. DR DrugCentral; Q9UIX4; -. DR TCDB; 1.A.1.2.27; the voltage-gated ion channel (vic) superfamily. DR iPTMnet; Q9UIX4; -. DR PhosphoSitePlus; Q9UIX4; -. DR BioMuta; KCNG1; -. DR DMDM; 24418479; -. DR MassIVE; Q9UIX4; -. DR PaxDb; 9606-ENSP00000360626; -. DR PeptideAtlas; Q9UIX4; -. DR ProteomicsDB; 84574; -. [Q9UIX4-1] DR ProteomicsDB; 84575; -. [Q9UIX4-2] DR Antibodypedia; 13829; 144 antibodies from 22 providers. DR DNASU; 3755; -. DR Ensembl; ENST00000371571.5; ENSP00000360626.4; ENSG00000026559.14. [Q9UIX4-1] DR GeneID; 3755; -. DR KEGG; hsa:3755; -. DR MANE-Select; ENST00000371571.5; ENSP00000360626.4; NM_002237.4; NP_002228.2. DR UCSC; uc002xwa.5; human. [Q9UIX4-1] DR AGR; HGNC:6248; -. DR CTD; 3755; -. DR DisGeNET; 3755; -. DR GeneCards; KCNG1; -. DR HGNC; HGNC:6248; KCNG1. DR HPA; ENSG00000026559; Tissue enriched (endometrium). DR MIM; 603788; gene. DR neXtProt; NX_Q9UIX4; -. DR OpenTargets; ENSG00000026559; -. DR PharmGKB; PA30034; -. DR VEuPathDB; HostDB:ENSG00000026559; -. DR eggNOG; KOG3713; Eukaryota. DR GeneTree; ENSGT00940000159686; -. DR HOGENOM; CLU_011722_4_1_1; -. DR InParanoid; Q9UIX4; -. DR OMA; CAFRNIL; -. DR OrthoDB; 1478695at2759; -. DR PhylomeDB; Q9UIX4; -. DR TreeFam; TF313103; -. DR PathwayCommons; Q9UIX4; -. DR Reactome; R-HSA-1296072; Voltage gated Potassium channels. DR SignaLink; Q9UIX4; -. DR BioGRID-ORCS; 3755; 12 hits in 1138 CRISPR screens. DR ChiTaRS; KCNG1; human. DR GeneWiki; KCNG1; -. DR GenomeRNAi; 3755; -. DR Pharos; Q9UIX4; Tclin. DR PRO; PR:Q9UIX4; -. DR Proteomes; UP000005640; Chromosome 20. DR RNAct; Q9UIX4; Protein. DR Bgee; ENSG00000026559; Expressed in cortical plate and 147 other cell types or tissues. DR ExpressionAtlas; Q9UIX4; baseline and differential. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IBA:GO_Central. DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB. DR GO; GO:0005267; F:potassium channel activity; NAS:UniProtKB. DR GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB. DR GO; GO:0006813; P:potassium ion transport; NAS:UniProtKB. DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro. DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB. DR CDD; cd18421; BTB_POZ_KCNG1_2; 1. DR Gene3D; 1.10.287.70; -; 1. DR Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1. DR InterPro; IPR000210; BTB/POZ_dom. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR003968; K_chnl_volt-dep_Kv. DR InterPro; IPR003969; K_chnl_volt-dep_Kv6. DR InterPro; IPR011333; SKP1/BTB/POZ_sf. DR InterPro; IPR003131; T1-type_BTB. DR InterPro; IPR027359; Volt_channel_dom_sf. DR PANTHER; PTHR11537:SF88; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY G MEMBER 1; 1. DR PANTHER; PTHR11537; VOLTAGE-GATED POTASSIUM CHANNEL; 1. DR Pfam; PF02214; BTB_2; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. DR PRINTS; PR01492; KV6CHANNEL. DR PRINTS; PR01491; KVCHANNEL. DR SMART; SM00225; BTB; 1. DR SUPFAM; SSF54695; POZ domain; 1. DR SUPFAM; SSF81324; Voltage-gated potassium channels; 1. DR Genevisible; Q9UIX4; HS. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Ion channel; Ion transport; Membrane; KW Potassium; Potassium channel; Potassium transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport; Voltage-gated channel. FT CHAIN 1..513 FT /note="Potassium voltage-gated channel subfamily G member FT 1" FT /id="PRO_0000054073" FT TOPO_DOM 1..224 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 225..246 FT /note="Helical; Name=Segment S1" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 247..267 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 268..289 FT /note="Helical; Name=Segment S2" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 290..300 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 301..321 FT /note="Helical; Name=Segment S3" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 322..338 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 339..359 FT /note="Helical; Voltage-sensor; Name=Segment S4" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 360..374 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 375..396 FT /note="Helical; Name=Segment S5" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 397..411 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT INTRAMEM 412..423 FT /note="Helical; Name=Pore helix" FT /evidence="ECO:0000250|UniProtKB:P63142" FT INTRAMEM 424..431 FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 432..438 FT /note="Extracellular" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TRANSMEM 439..467 FT /note="Helical; Name=Segment S6" FT /evidence="ECO:0000250|UniProtKB:P63142" FT TOPO_DOM 468..513 FT /note="Cytoplasmic" FT /evidence="ECO:0000250|UniProtKB:P63142" FT REGION 184..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 424..429 FT /note="Selectivity filter" FT /evidence="ECO:0000250|UniProtKB:P63142" FT VAR_SEQ 259..275 FT /note="GHCSQMCHNVFIVESVC -> VRAHAPRGNAPPRGKGL (in isoform FT 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001024" FT VAR_SEQ 276..513 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001025" FT VARIANT 304 FT /note="I -> M (in dbSNP:rs17791052)" FT /id="VAR_053860" FT CONFLICT 426 FT /note="G -> D (in Ref. 1; AAC05635)" FT /evidence="ECO:0000305" FT CONFLICT 465 FT /note="R -> P (in Ref. 1; AAC05635)" FT /evidence="ECO:0000305" SQ SEQUENCE 513 AA; 57913 MW; A002F1C0EF2FBDC5 CRC64; MTLLPGDNSD YDYSALSCTS DASFHPAFLP QRQAIKGAFY RRAQRLRPQD EPRQGCQPED RRRRIIINVG GIKYSLPWTT LDEFPLTRLG QLKACTNFDD ILNVCDDYDV TCNEFFFDRN PGAFGTILTF LRAGKLRLLR EMCALSFQEE LLYWGIAEDH LDGCCKRRYL QKIEEFAEMV EREEEDDALD SEGRDSEGPA EGEGRLGRCM RRLRDMVERP HSGLPGKVFA CLSVLFVTVT AVNLSVSTLP SLREEEEQGH CSQMCHNVFI VESVCVGWFS LEFLLRLIQA PSKFAFLRSP LTLIDLVAIL PYYITLLVDG AAAGRRKPGA GNSYLDKVGL VLRVLRALRI LYVMRLARHS LGLQTLGLTA RRCTREFGLL LLFLCVAIAL FAPLLYVIEN EMADSPEFTS IPACYWWAVI TMTTVGYGDM VPRSTPGQVV ALSSILSGIL LMAFPVTSIF HTFSRSYLEL KQEQERVMFR RAQFLIKTKS QLSVSQDSDI LFGSASSDTR DNN //