KCNG3_MOUSE
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 03-AUG-2022, entry version 143.
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 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; P59053; -.
DR PeptideAtlas; P59053; -.
DR PRIDE; P59053; -.
DR Antibodypedia; 29754; 157 antibodies from 23 providers.
DR DNASU; 225030; -.
DR Ensembl; ENSMUST00000051482; ENSMUSP00000054910; ENSMUSG00000045053. [P59053-1]
DR Ensembl; ENSMUST00000234613; ENSMUSP00000157121; ENSMUSG00000045053. [P59053-2]
DR GeneID; 225030; -.
DR KEGG; mmu:225030; -.
DR UCSC; uc008dsd.1; mouse. [P59053-1]
DR UCSC; uc008dse.1; mouse. [P59053-2]
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; CYHELKM; -.
DR OrthoDB; 818306at2759; -.
DR PhylomeDB; P59053; -.
DR TreeFam; TF313103; -.
DR Reactome; R-MMU-1296072; Voltage gated Potassium channels.
DR BioGRID-ORCS; 225030; 2 hits in 74 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 30 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA: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: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 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 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
