KCNG4_MOUSE
ID KCNG4_MOUSE Reviewed; 506 AA.
AC Q80XM3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Potassium voltage-gated channel subfamily G member 4;
DE AltName: Full=Voltage-gated potassium channel subunit Kv6.4;
GN Name=Kcng4;
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].
RA Preisig-Mueller R., Derst C., Schnitzler M.M., Daut J.;
RT "Cloning and characterization of two novel gamma Kv subunits.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
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).
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.
CC {ECO:0000250|UniProtKB:Q8TDN1}.
CC -!- SUBUNIT: Heterotetramer with KCNB1. {ECO:0000250|UniProtKB:Q8TDN1}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TDN1};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TDN1}. Note=Has to
CC be associated with KCNB1 or possibly another partner to get inserted in
CC the plasma membrane. Colocalizes with KCNB1 at the plasma membrane.
CC Remains intracellular in the absence of KCNB1.
CC {ECO:0000250|UniProtKB:Q8TDN1}.
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. Kv6.4/KCNG4 sub-subfamily. {ECO:0000305}.
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DR EMBL; BC043936; AAH43936.1; -; mRNA.
DR EMBL; AF450109; AAP46290.1; -; mRNA.
DR CCDS; CCDS22710.1; -.
DR RefSeq; NP_080010.2; NM_025734.2.
DR RefSeq; XP_006531352.1; XM_006531289.3.
DR AlphaFoldDB; Q80XM3; -.
DR SMR; Q80XM3; -.
DR STRING; 10090.ENSMUSP00000056552; -.
DR iPTMnet; Q80XM3; -.
DR PhosphoSitePlus; Q80XM3; -.
DR PaxDb; Q80XM3; -.
DR PRIDE; Q80XM3; -.
DR ABCD; Q80XM3; 1 sequenced antibody.
DR Antibodypedia; 30581; 109 antibodies from 25 providers.
DR DNASU; 66733; -.
DR Ensembl; ENSMUST00000061828; ENSMUSP00000056552; ENSMUSG00000045246.
DR Ensembl; ENSMUST00000164382; ENSMUSP00000129687; ENSMUSG00000045246.
DR GeneID; 66733; -.
DR KEGG; mmu:66733; -.
DR UCSC; uc009nqb.1; mouse.
DR CTD; 93107; -.
DR MGI; MGI:1913983; Kcng4.
DR VEuPathDB; HostDB:ENSMUSG00000045246; -.
DR eggNOG; KOG3713; Eukaryota.
DR GeneTree; ENSGT00940000156938; -.
DR HOGENOM; CLU_011722_4_1_1; -.
DR InParanoid; Q80XM3; -.
DR OMA; YVLPWST; -.
DR OrthoDB; 686359at2759; -.
DR PhylomeDB; Q80XM3; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 66733; 0 hits in 71 CRISPR screens.
DR PRO; PR:Q80XM3; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q80XM3; protein.
DR Bgee; ENSMUSG00000045246; Expressed in facial nucleus and 61 other tissues.
DR Genevisible; Q80XM3; MM.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS: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; 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 SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript 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..506
FT /note="Potassium voltage-gated channel subfamily G member
FT 4"
FT /id="PRO_0000320142"
FT TOPO_DOM 1..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 217..238
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 239..259
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 260..281
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 282..292
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 293..312
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 313..326
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 327..351
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 352..366
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 367..388
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 389..403
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 404..415
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 416..423
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 424..430
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 431..459
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 460..506
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 416..421
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
SQ SEQUENCE 506 AA; 57177 MW; 7CA48F0F71D58213 CRC64;
MPMSSRDRDL HPGHHHFGSC SPLSQLWPGP EPKSVKGLYY SRARKVGNQD ASPEANLKEI
LVNVGGQRYL LPWSTLDAFP LSRLSRLRLC RSHEEITQLC DDYDEDSQEF FFDRNPSAFG
VIVSFLAAGK LVLLREMCAL SFREELSYWG IEETNLERCC LRKLLKKLEE AAELRREEAA
QRQQQRQACH SEVQASRWAR SMNQLREMVE DPQSGLPGKV FACLSVLFVA TTAVSLCVST
MPDFRAEEGK GECTRKCYYI FVVESICVAW FSLEFCLRFV QAPNKCQFFR GPLNVIDILA
ISPYYVSLAV SDESPEAGER PSSSSYLEKV GLVLRVLRAL RILYVMRLAR HSLGLQTLGL
TVRRCAREFG LLMLFLAVAV TLFSPLVYVA ENESGRVLEF TSIPASYWWA IISMTTVGYG
DMVPRSVPGQ MVALSSILSG ILIMAFPATS IFHTFSHSYL ELKREQEQVQ ARLRRLQNTN
SASERELLSD VDDLVPEGLT SPGRYM
