KCNG1_HUMAN
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 03-AUG-2022, entry version 179.
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 voltage-sensor and is
CC 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}.
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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. [Q9UIX4-1]
DR RefSeq; XP_011527108.1; XM_011528806.1. [Q9UIX4-1]
DR AlphaFoldDB; Q9UIX4; -.
DR SMR; Q9UIX4; -.
DR BioGRID; 109957; 20.
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; Q9UIX4; -.
DR PeptideAtlas; Q9UIX4; -.
DR PRIDE; Q9UIX4; -.
DR ProteomicsDB; 84574; -. [Q9UIX4-1]
DR ProteomicsDB; 84575; -. [Q9UIX4-2]
DR Antibodypedia; 13829; 122 antibodies from 21 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 CTD; 3755; -.
DR DisGeNET; 3755; -.
DR GeneCards; KCNG1; -.
DR HGNC; HGNC:6248; KCNG1.
DR HPA; ENSG00000026559; Tissue enhanced (brain, 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; GQLKFCT; -.
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; 10 hits in 1058 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 145 other tissues.
DR ExpressionAtlas; Q9UIX4; baseline and differential.
DR Genevisible; Q9UIX4; HS.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
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:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
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 Gene3D; 1.20.120.350; -; 1.
DR Gene3D; 3.30.710.10; -; 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; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR PRINTS; PR01492; KV6CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
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
