ID   KCNG3_MOUSE             Reviewed;         433 AA.
AC   P59053;
DT   25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2002, sequence version 1.
DT   24-JAN-2024, entry version 151.
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   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] (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.
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:Q8TAE7}.
CC   -!- SUBUNIT: Heterotetramer with KCNB1. Does not form homomultimers.
CC       {ECO:0000250|UniProtKB:Q8TAE7}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8TAE7};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8TAE7}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q8TAE7}. Note=Has to be associated with KCNB1 or
CC       possibly another partner to get inserted in the plasma membrane.
CC       Colocalizes with KCNB1 at the plasma membrane. Remains intracellular in
CC       the absence of KCNB1. {ECO:0000250|UniProtKB:Q8TAE7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Kv10.1b;
CC         IsoId=P59053-1; Sequence=Displayed;
CC       Name=2; Synonyms=Kv10.1a;
CC         IsoId=P59053-2; Sequence=VSP_001027;
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. Kv6.3/KCNG3 sub-subfamily. {ECO:0000305}.
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DR   EMBL; AF454551; AAM93552.1; -; mRNA.
DR   EMBL; AF454552; AAM93553.1; -; mRNA.
DR   CCDS; CCDS28996.1; -. [P59053-1]
DR   RefSeq; NP_705732.1; NM_153512.1. [P59053-1]
DR   RefSeq; XP_006524263.1; XM_006524200.3. [P59053-2]
DR   AlphaFoldDB; P59053; -.
DR   SMR; P59053; -.
DR   STRING; 10090.ENSMUSP00000054910; -.
DR   iPTMnet; P59053; -.
DR   PhosphoSitePlus; P59053; -.
DR   MaxQB; P59053; -.
DR   PaxDb; 10090-ENSMUSP00000054910; -.
DR   PeptideAtlas; P59053; -.
DR   Antibodypedia; 29754; 189 antibodies from 23 providers.
DR   DNASU; 225030; -.
DR   Ensembl; ENSMUST00000051482.2; ENSMUSP00000054910.2; ENSMUSG00000045053.3. [P59053-1]
DR   Ensembl; ENSMUST00000234613.2; ENSMUSP00000157121.2; ENSMUSG00000045053.3. [P59053-2]
DR   GeneID; 225030; -.
DR   KEGG; mmu:225030; -.
DR   UCSC; uc008dsd.1; mouse. [P59053-1]
DR   UCSC; uc008dse.1; mouse. [P59053-2]
DR   AGR; MGI:2663923; -.
DR   CTD; 170850; -.
DR   MGI; MGI:2663923; Kcng3.
DR   VEuPathDB; HostDB:ENSMUSG00000045053; -.
DR   eggNOG; KOG3713; Eukaryota.
DR   GeneTree; ENSGT00940000159658; -.
DR   HOGENOM; CLU_011722_4_1_1; -.
DR   InParanoid; P59053; -.
DR   OMA; FYNEMVY; -.
DR   OrthoDB; 1478695at2759; -.
DR   PhylomeDB; P59053; -.
DR   TreeFam; TF313103; -.
DR   Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR   BioGRID-ORCS; 225030; 2 hits in 79 CRISPR screens.
DR   ChiTaRS; Kcng3; mouse.
DR   PRO; PR:P59053; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; P59053; Protein.
DR   Bgee; ENSMUSG00000045053; Expressed in secondary oocyte and 31 other cell types or tissues.
DR   GO; GO:0005783; C:endoplasmic reticulum; 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:0005249; F:voltage-gated potassium channel activity; ISO:MGI.
DR   GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR   GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR   GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR   CDD; cd18422; BTB_POZ_KCNG3; 1.
DR   Gene3D; 1.10.287.70; -; 1.
DR   Gene3D; 1.20.120.350; Voltage-gated potassium channels. Chain C; 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; IPR027359; Volt_channel_dom_sf.
DR   PANTHER; PTHR11537:SF91; POTASSIUM VOLTAGE-GATED CHANNEL SUBFAMILY G MEMBER 3; 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   SMART; SM00225; BTB; 1.
DR   SUPFAM; SSF54695; POZ domain; 1.
DR   SUPFAM; SSF81324; Voltage-gated potassium channels; 1.
PE   2: Evidence at transcript 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..433
FT                   /note="Potassium voltage-gated channel subfamily G member
FT                   3"
FT                   /id="PRO_0000054078"
FT   TOPO_DOM        1..165
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        166..187
FT                   /note="Helical; Name=Segment S1"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        188..217
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        218..239
FT                   /note="Helical; Name=Segment S2"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        240..250
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        251..271
FT                   /note="Helical; Name=Segment S3"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        272..281
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        282..302
FT                   /note="Helical; Voltage-sensor; Name=Segment S4"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        303..317
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        318..339
FT                   /note="Helical; Name=Segment S5"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        340..357
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        358..369
FT                   /note="Helical; Name=Pore helix"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   INTRAMEM        370..377
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        378..384
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TRANSMEM        385..413
FT                   /note="Helical; Name=Segment S6"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   TOPO_DOM        414..433
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   MOTIF           370..375
FT                   /note="Selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:P63142"
FT   VAR_SEQ         209..219
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.1"
FT                   /id="VSP_001027"
SQ   SEQUENCE   433 AA;  49247 MW;  E9A7C010F4B0CA6C CRC64;
     MTFGRGGAAS VVLNVGGARY SLSRELLKDF PLRRVSRLHG CRSERDVLEV CDDYDRERNE
     YFFDRHSEAF GFILLYVRGH GKLRFAPRMC ELSFYNEMIY WGLEGAHLEY CCQRRLDDRM
     SDTHTFHAAD ELGREQPRPA GPEAAPSRRW LERMRRTFEE PTSSLAAQIL ASVSVVFVIV
     SMVVLCASTL PDWRAAVADN RSLDDRSRYS ASPGREPSGI IEAICIGWFT AECIVRFIVS
     KNKCEFVKRP LNIIDLLAIT PYYISVLMTV FTGENSQLQR AGVTLRVLRM MRIFWVIKLA
     RHFIGLQTLG LTLKRCYREM AMLLVFICVA MAIFSALSQL LEHGLDLETS NKDFASIPAA
     CWWVIISMTT VGYGDMYPIT VPGRILGGVC VVSGIVLLAL PITFIYHSFV QCYHELKFRS
     ARYSRSLSAE FLN
//