KCNG3_HUMAN
ID KCNG3_HUMAN Reviewed; 436 AA.
AC Q8TAE7; Q53SC1;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Potassium voltage-gated channel subfamily G member 3;
DE AltName: Full=Voltage-gated potassium channel subunit Kv10.1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv6.3;
GN Name=KCNG3;
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), FUNCTION, SUBUNIT, INTERACTION WITH
RP KCNB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11852086; DOI=10.1016/s0014-5793(02)02267-6;
RA Sano Y., Mochizuki S., Miyake A., Kitada C., Inamura K., Yokoi H.,
RA Nozawa K., Matsushime H., Furuichi K.;
RT "Molecular cloning and characterization of Kv6.3, a novel modulatory
RT subunit for voltage-gated K(+) channel Kv2.1.";
RL FEBS Lett. 512:230-234(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBUNIT, INTERACTION WITH
RP KCNB1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12060745; DOI=10.1073/pnas.122617999;
RA Ottschytsch N., Raes A., Van Hoorick D., Snyders D.J.;
RT "Obligatory heterotetramerization of three previously uncharacterized Kv
RT channel alpha-subunits identified in the human genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:7986-7991(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RA Vega-Saenz de Miera E.C., Rudy B.;
RT "Kv10.1a and Kv10.1b: two novel alternatively spliced potassium channel
RT subunits.";
RL Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 [7]
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 (PubMed:11852086). Can form functional
CC heterotetrameric channels with KCNB1; this promotes a reduction in the
CC rate of activation and inactivation of the delayed rectifier voltage-
CC gated potassium channel KCNB1 (PubMed:11852086, PubMed:19074135).
CC {ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:19074135}.
CC -!- SUBUNIT: Heterotetramer with KCNB1 (PubMed:11852086, PubMed:12060745,
CC PubMed:19074135). Does not form homomultimers (PubMed:12060745).
CC {ECO:0000269|PubMed:11852086, ECO:0000269|PubMed:12060745,
CC ECO:0000269|PubMed:19074135}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11852086,
CC ECO:0000269|PubMed:12060745, ECO:0000269|PubMed:19074135}; Multi-pass
CC membrane protein {ECO:0000305}. Cytoplasm
CC {ECO:0000269|PubMed:12060745}. Note=Has to be associated with KCNB1 or
CC possibly another partner to get inserted in the plasma membrane
CC (PubMed:12060745). Colocalizes with KCNB1 at the plasma membrane
CC (PubMed:12060745, PubMed:19074135). Remains intracellular in the
CC absence of KCNB1 (PubMed:12060745). {ECO:0000269|PubMed:12060745,
CC ECO:0000269|PubMed:19074135}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Kv10.1b;
CC IsoId=Q8TAE7-1; Sequence=Displayed;
CC Name=2; Synonyms=Kv10.1a;
CC IsoId=Q8TAE7-2; Sequence=VSP_001026;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, liver, testis, small
CC intestine, colon, thymus and adrenal gland (PubMed:11852086,
CC PubMed:12060745). {ECO:0000269|PubMed:11852086,
CC ECO:0000269|PubMed:12060745}.
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. Kv6.3/KCNG3 sub-subfamily. {ECO:0000305}.
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DR EMBL; AB070604; BAB85520.1; -; mRNA.
DR EMBL; AF348982; AAL83909.1; -; mRNA.
DR EMBL; AF454547; AAM93548.1; -; mRNA.
DR EMBL; AF454548; AAM93549.1; -; mRNA.
DR EMBL; AC025750; AAY24039.1; -; Genomic_DNA.
DR EMBL; CH471053; EAX00319.1; -; Genomic_DNA.
DR EMBL; BC071558; AAH71558.1; -; mRNA.
DR CCDS; CCDS1809.1; -. [Q8TAE7-1]
DR CCDS; CCDS42674.1; -. [Q8TAE7-2]
DR RefSeq; NP_579875.1; NM_133329.5. [Q8TAE7-1]
DR RefSeq; NP_758847.1; NM_172344.2. [Q8TAE7-2]
DR AlphaFoldDB; Q8TAE7; -.
DR SMR; Q8TAE7; -.
DR BioGRID; 128090; 7.
DR IntAct; Q8TAE7; 1.
DR STRING; 9606.ENSP00000304127; -.
DR ChEMBL; CHEMBL2362996; -.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR DrugCentral; Q8TAE7; -.
DR iPTMnet; Q8TAE7; -.
DR PhosphoSitePlus; Q8TAE7; -.
DR BioMuta; KCNG3; -.
DR DMDM; 24418472; -.
DR MassIVE; Q8TAE7; -.
DR PaxDb; Q8TAE7; -.
DR PeptideAtlas; Q8TAE7; -.
DR PRIDE; Q8TAE7; -.
DR ProteomicsDB; 73867; -. [Q8TAE7-1]
DR ProteomicsDB; 73868; -. [Q8TAE7-2]
DR Antibodypedia; 29754; 157 antibodies from 23 providers.
DR DNASU; 170850; -.
DR Ensembl; ENST00000306078.2; ENSP00000304127.1; ENSG00000171126.8. [Q8TAE7-1]
DR Ensembl; ENST00000394973.4; ENSP00000378424.4; ENSG00000171126.8. [Q8TAE7-2]
DR GeneID; 170850; -.
DR KEGG; hsa:170850; -.
DR MANE-Select; ENST00000306078.2; ENSP00000304127.1; NM_133329.6; NP_579875.1.
DR UCSC; uc002rsm.4; human. [Q8TAE7-1]
DR CTD; 170850; -.
DR DisGeNET; 170850; -.
DR GeneCards; KCNG3; -.
DR HGNC; HGNC:18306; KCNG3.
DR HPA; ENSG00000171126; Tissue enriched (brain).
DR MIM; 606767; gene.
DR neXtProt; NX_Q8TAE7; -.
DR OpenTargets; ENSG00000171126; -.
DR PharmGKB; PA30036; -.
DR VEuPathDB; HostDB:ENSG00000171126; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000159658; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; Q8TAE7; -.
DR OMA; CYHELKM; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; Q8TAE7; -.
DR TreeFam; TF313103; -.
DR PathwayCommons; Q8TAE7; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q8TAE7; -.
DR BioGRID-ORCS; 170850; 14 hits in 1073 CRISPR screens.
DR ChiTaRS; KCNG3; human.
DR GeneWiki; KCNG3; -.
DR GenomeRNAi; 170850; -.
DR Pharos; Q8TAE7; Tclin.
DR PRO; PR:Q8TAE7; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TAE7; protein.
DR Bgee; ENSG00000171126; Expressed in islet of Langerhans and 56 other tissues.
DR Genevisible; Q8TAE7; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
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; IDA:GO_Central.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA: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:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR003971; K_chnl_volt-dep_Kv9.
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; PR01494; KV9CHANNEL.
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; Cytoplasm; Ion channel; Ion transport;
KW Membrane; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Voltage-gated channel.
FT CHAIN 1..436
FT /note="Potassium voltage-gated channel subfamily G member
FT 3"
FT /id="PRO_0000054077"
FT TOPO_DOM 1..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 169..190
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 191..220
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 221..242
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 243..253
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 254..274
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 275..284
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 285..305
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 306..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 321..342
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 343..360
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 361..372
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 373..380
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 381..387
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 388..416
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 417..436
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT MOTIF 373..378
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT VAR_SEQ 212..222
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_001026"
SQ SEQUENCE 436 AA; 49593 MW; 3C289CFF0B462513 CRC64;
MTFGRSGAAS VVLNVGGARY SLSRELLKDF PLRRVSRLHG CRSERDVLEV CDDYDRERNE
YFFDRHSEAF GFILLYVRGH GKLRFAPRMC ELSFYNEMIY WGLEGAHLEY CCQRRLDDRM
SDTYTFYSAD EPGVLGRDEA RPGGAEAAPS RRWLERMRRT FEEPTSSLAA QILASVSVVF
VIVSMVVLCA STLPDWRNAA ADNRSLDDRS RYSAGPGREP SGIIEAICIG WFTAECIVRF
IVSKNKCEFV KRPLNIIDLL AITPYYISVL MTVFTGENSQ LQRAGVTLRV LRMMRIFWVI
KLARHFIGLQ TLGLTLKRCY REMVMLLVFI CVAMAIFSAL SQLLEHGLDL ETSNKDFTSI
PAACWWVIIS MTTVGYGDMY PITVPGRILG GVCVVSGIVL LALPITFIYH SFVQCYHELK
FRSARYSRSL STEFLN
