KCNG1_RAT
ID KCNG1_RAT Reviewed; 514 AA.
AC D4AD53;
DT 22-JUL-2015, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Potassium voltage-gated channel subfamily G member 1;
DE AltName: Full=Voltage-gated potassium channel subunit Kv6.1;
GN Name=Kcng1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
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 [3]
RP FUNCTION, SUBUNIT, INTERACTION WITH KCNB1, AND SUBCELLULAR LOCATION.
RX PubMed=8980147; DOI=10.1016/s0014-5793(96)01316-6;
RA Post M.A., Kirsch G.E., Brown A.M.;
RT "Kv2.1 and electrically silent Kv6.1 potassium channel subunits combine and
RT express a novel current.";
RL FEBS Lett. 399:177-182(1996).
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:8980147).
CC {ECO:0000269|PubMed:8980147}.
CC -!- SUBUNIT: Heterotetramer with KCNB1 (PubMed:8980147).
CC {ECO:0000269|PubMed:8980147}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8980147};
CC Multi-pass membrane protein {ECO:0000305}.
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; AABR06027705; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027706; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027707; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027708; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027709; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027710; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR06027711; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH474005; EDL96362.1; -; Genomic_DNA.
DR EMBL; CH474005; EDL96363.1; -; Genomic_DNA.
DR RefSeq; NP_001100015.1; NM_001106545.1.
DR RefSeq; XP_008760706.1; XM_008762484.2.
DR RefSeq; XP_017447105.1; XM_017591616.1.
DR AlphaFoldDB; D4AD53; -.
DR SMR; D4AD53; -.
DR STRING; 10116.ENSRNOP00000045232; -.
DR PhosphoSitePlus; D4AD53; -.
DR PaxDb; D4AD53; -.
DR PRIDE; D4AD53; -.
DR Ensembl; ENSRNOT00000081648; ENSRNOP00000069311; ENSRNOG00000054314.
DR GeneID; 296395; -.
DR KEGG; rno:296395; -.
DR UCSC; RGD:631416; rat.
DR CTD; 3755; -.
DR RGD; 631416; Kcng1.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000159686; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; D4AD53; -.
DR OMA; GQLKFCT; -.
DR OrthoDB; 686359at2759; -.
DR PhylomeDB; D4AD53; -.
DR TreeFam; TF313103; -.
DR Reactome; R-RNO-1296072; Voltage gated Potassium channels.
DR PRO; PR:D4AD53; -.
DR Proteomes; UP000002494; Chromosome 3.
DR Proteomes; UP000234681; Chromosome 3.
DR Bgee; ENSRNOG00000054314; Expressed in frontal cortex and 6 other tissues.
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: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; IDA:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; IDA: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 Cell membrane; Ion channel; Ion transport; Membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Voltage-gated channel.
FT CHAIN 1..514
FT /note="Potassium voltage-gated channel subfamily G member
FT 1"
FT /id="PRO_0000433466"
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..514
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 181..205
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 COMPBIAS 181..197
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 514 AA; 58027 MW; 8D8B20102EA43FF5 CRC64;
MTLLPGDNSD YDYSALSCAS DTSFHPAFFP QRQAIKGVFY RRAQRLGPQD DLHQSISLGD
RRRQIIINVG GIKYSLPWTT LDEFPLTRLG QLKACTNFDD ILSVCDDYDV TCNEFFFDRN
PGAFGTILTF LRAGKLRLLR EMCALSFQEE LLYWGIAEDH LDGCCKRRYL QKIEEFAEMM
EREDEEEALD SEDQESEGPS TSEGRLSRCM RRLRDMVEKP HSGLPGKVFA CLSVLFVTVT
AVNLSVSTLP SLREEEEQGQ CSQMCHNVFI VESVCVGWFS LEFLLRFIQA PSKFAFLRSP
LTLIDLVAIL PYYVTLLVDG AASSRRKPST GNSYLDKVGL VLRVLRALRI LYVMRLARHS
LGLQTLGLTA RRCTREFGLL LLFLCVAIAL FAPLLYVIEN EMADSPEFTS IPACYWWAVI
TMTTVGYGDM VPRSTPGQVV ALSSILSGIL LMAFPVTSIF HTFSRSYLEL KQEQERVLIR
RAQYLIKTKS QLSGMSQDSD ILFGSASSDT RDNN
