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   02-SEP-2026, entry version 156.
DE   RecName: Full=Voltage-gated potassium channel regulatory subunit KCNG4 {ECO:0000305};
DE   AltName: Full=Potassium voltage-gated channel subfamily G member 4;
DE   AltName: Full=Voltage-gated potassium channel subunit Kv6.3 {ECO:0000250|UniProtKB:Q8TDN1};
DE   AltName: Full=Voltage-gated potassium channel subunit Kv6.4 {ECO:0000250|UniProtKB:Q8TDN1};
GN   Name=Kcng4 {ECO:0000312|MGI:MGI:1913983};
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: Regulatory subunit of the voltage-gated potassium (Kv)
CC       channel which, when coassembled with KCNB1, modulates the kinetics
CC       parameters of the heterotetrameric channel namely the time course of
CC       activation, deactivation and inactivation and on the voltage-dependence
CC       of activation. Potassium channel subunit that does not form functional
CC       channels by itself. Reduces the deactivation rate. Modulates the
CC       threshold for activation by shifting by approximately 20 mV in
CC       hyperpolarizing direction. Markedly changes the inactivation by
CC       shifting the voltage dependence of inactivation by approximately 40 mV
CC       in hyperpolarizing direction. Acceleratee activation and enhances the
CC       time course of activation. {ECO:0000250|UniProtKB:Q8TDN1}.
CC   -!- SUBUNIT: Heterotetramer with KCNB1. Does not form homomultimer.
CC       {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 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. Kv6.4/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_006531289.5.
DR   AlphaFoldDB; Q80XM3; -.
DR   SMR; Q80XM3; -.
DR   FunCoup; Q80XM3; 11.
DR   STRING; 10090.ENSMUSP00000056552; -.
DR   iPTMnet; Q80XM3; -.
DR   PhosphoSitePlus; Q80XM3; -.
DR   PaxDb; 10090-ENSMUSP00000056552; -.
DR   ProteomicsDB; 263495; -.
DR   ABCD; Q80XM3; 1 sequenced antibody.
DR   Antibodypedia; 30581; 100 antibodies from 26 providers.
DR   DNASU; 66733; -.
DR   Ensembl; ENSMUST00000061828.10; ENSMUSP00000056552.4; ENSMUSG00000045246.13.
DR   GeneID; 66733; -.
DR   KEGG; mmu:66733; -.
DR   UCSC; uc009nqb.1; mouse.
DR   AGR; MGI:1913983; -.
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; VQARNKC; -.
DR   OrthoDB; 296522at2759; -.
DR   PhylomeDB; Q80XM3; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 66733; 0 hits in 76 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 cell types or tissues.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005654; C:nucleoplasm; ISO:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR   GO; GO:0015459; F:potassium channel regulator activity; ISS:UniProtKB.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:GO_Central.
DR   GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR   GO; GO:0001508; P:action potential; IBA:GO_Central.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   GO; GO:1901379; P:regulation of potassium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0043266; P:regulation of potassium ion transport; ISO:GO_Central.
DR   FunFam; 1.20.120.350:FF:000024; Potassium voltage-gated channel subfamily G member 1; 1.
DR   FunFam; 1.10.287.70:FF:000005; potassium voltage-gated channel subfamily G member 1; 1.
DR   FunFam; 3.30.710.10:FF:000019; Potassium voltage-gated channel, subfamily G, member 1; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 1.
DR   InterPro; IPR005821; Ion_trans_dom.
DR   InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR   InterPro; IPR003971; K_chnl_volt-dep_Kv5/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:SF167; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY G MEMBER 4; 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; PR01494; KV9CHANNEL.
DR   PRINTS; PR01491; KVCHANNEL.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 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="Voltage-gated potassium channel regulatory subunit
FT                   KCNG4"
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
//