KCNK3_MOUSE
ID KCNK3_MOUSE Reviewed; 409 AA.
AC O35111; O35163;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Potassium channel subfamily K member 3;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-1;
DE AltName: Full=Cardiac two pore background K(+) channel;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 1;
DE AltName: Full=Two pore potassium channel KT3.1;
DE Short=Two pore K(+) channel KT3.1;
DE AltName: Full=cTBAK-1;
GN Name=Kcnk3; Synonyms=Ctbak, Task, Task1;
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].
RC TISSUE=Heart;
RX PubMed=9506712; DOI=10.1161/01.res.82.4.513;
RA Kim D., Fujita A., Horio Y., Kurachi Y.;
RT "Cloning and functional expression of a novel cardiac two-pore background
RT K+ channel (cTBAK-1).";
RL Circ. Res. 82:513-518(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Heart;
RX PubMed=10748056; DOI=10.1074/jbc.m001948200;
RA Lopes C.M.B., Gallagher P.G., Buck M.E., Butler M.H., Goldstein S.A.N.;
RT "Proton block and voltage gating are potassium-dependent in the cardiac
RT leak channel Kcnk3.";
RL J. Biol. Chem. 275:16969-16978(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-409.
RX PubMed=9312005; DOI=10.1093/emboj/16.17.5464;
RA Duprat F., Lesage F., Fink M., Reyes R., Heurteaux C., Lazdunski M.;
RT "TASK, a human background K+ channel to sense external pH variations near
RT physiological pH.";
RL EMBO J. 16:5464-5471(1997).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: pH-dependent, voltage-insensitive, background potassium
CC channel protein. Rectification direction results from potassium ion
CC concentration on either side of the membrane. Acts as an outward
CC rectifier when external potassium concentration is low. When external
CC potassium concentration is high, current is inward.
CC {ECO:0000250|UniProtKB:O14649}.
CC -!- SUBUNIT: Homodimer. Heterodimer with KCNK1.
CC {ECO:0000250|UniProtKB:O14649}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14649};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
CC -!- TISSUE SPECIFICITY: Very strong expression in heart, also detected in
CC kidney, brain, skin, testis, lung, skeletal muscle, small intestine and
CC stomach. Not detected in liver, thymus or spleen.
CC -!- MISCELLANEOUS: Inactivated by barium.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {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; AB008537; BAA25436.1; -; mRNA.
DR EMBL; AF241798; AAF81418.1; -; Genomic_DNA.
DR EMBL; AF242508; AAF81418.1; JOINED; Genomic_DNA.
DR EMBL; AF065162; AAG29339.1; -; mRNA.
DR EMBL; AF006824; AAC53367.1; -; mRNA.
DR EMBL; AB013345; BAA28349.1; -; mRNA.
DR CCDS; CCDS19160.1; -.
DR RefSeq; NP_034738.1; NM_010608.2.
DR AlphaFoldDB; O35111; -.
DR SMR; O35111; -.
DR STRING; 10090.ENSMUSP00000098987; -.
DR GlyGen; O35111; 1 site.
DR iPTMnet; O35111; -.
DR PhosphoSitePlus; O35111; -.
DR PaxDb; O35111; -.
DR PeptideAtlas; O35111; -.
DR PRIDE; O35111; -.
DR ProteomicsDB; 269270; -.
DR ABCD; O35111; 1 sequenced antibody.
DR Antibodypedia; 13387; 238 antibodies from 28 providers.
DR DNASU; 16527; -.
DR Ensembl; ENSMUST00000066295; ENSMUSP00000098987; ENSMUSG00000049265.
DR GeneID; 16527; -.
DR KEGG; mmu:16527; -.
DR UCSC; uc008wvr.1; mouse.
DR CTD; 3777; -.
DR MGI; MGI:1100509; Kcnk3.
DR VEuPathDB; HostDB:ENSMUSG00000049265; -.
DR eggNOG; KOG4404; Eukaryota.
DR GeneTree; ENSGT00940000158248; -.
DR HOGENOM; CLU_022504_4_0_1; -.
DR InParanoid; O35111; -.
DR OMA; TCMEQSH; -.
DR OrthoDB; 1109218at2759; -.
DR PhylomeDB; O35111; -.
DR TreeFam; TF313947; -.
DR Reactome; R-MMU-1299316; TWIK-releated acid-sensitive K+ channel (TASK).
DR Reactome; R-MMU-5576886; Phase 4 - resting membrane potential.
DR BioGRID-ORCS; 16527; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Kcnk3; mouse.
DR PRO; PR:O35111; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O35111; protein.
DR Bgee; ENSMUSG00000049265; Expressed in adrenal gland and 143 other tissues.
DR Genevisible; O35111; MM.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0005216; F:ion channel activity; ISO:MGI.
DR GO; GO:0005252; F:open rectifier potassium channel activity; ISO:MGI.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0022841; F:potassium ion leak channel activity; ISS:UniProtKB.
DR GO; GO:0008022; F:protein C-terminus binding; ISO:MGI.
DR GO; GO:0044548; F:S100 protein binding; ISO:MGI.
DR GO; GO:0007420; P:brain development; IEA:Ensembl.
DR GO; GO:0071456; P:cellular response to hypoxia; ISO:MGI.
DR GO; GO:0071294; P:cellular response to zinc ion; IEA:Ensembl.
DR GO; GO:0090102; P:cochlea development; IEA:Ensembl.
DR GO; GO:0034220; P:ion transmembrane transport; ISO:MGI.
DR GO; GO:0051481; P:negative regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; ISO:MGI.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; ISO:MGI.
DR GO; GO:0060075; P:regulation of resting membrane potential; ISO:MGI.
DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:MGI.
DR GO; GO:0030322; P:stabilization of membrane potential; IBA:GO_Central.
DR InterPro; IPR003280; 2pore_dom_K_chnl.
DR InterPro; IPR003092; 2pore_dom_K_chnl_TASK.
DR InterPro; IPR013099; K_chnl_dom.
DR InterPro; IPR005406; KCNK3.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR PANTHER; PTHR11003:SF138; PTHR11003:SF138; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01584; TASK1CHANNEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 1: Evidence at protein level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..409
FT /note="Potassium channel subfamily K member 3"
FT /id="PRO_0000101745"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 78..101
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 108..128
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 129..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 184..207
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 244..409
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 4
FT /note="Q -> E (in Ref. 3; AAC53367)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="V -> I (in Ref. 3; AAC53367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 409 AA; 45068 MW; 35236E011AAC5687 CRC64;
MKRQNVRTLA LIVCTFTYLL VGAAVFDALE SEPEMIERQR LELRQLELRA RYNLSEGGYE
ELERVVLRLK PHKAGVQWRF AGSFYFAITV ITTIGYGHAA PSTDGGKVFC MFYALLGIPL
TLVMFQSLGE RINTFVRYLL HRAKRGLGMR HAEVSMANMV LIGFVSCIST LCIGAAAFSY
YERWTFFQAY YYCFITLTTI GFGDYVALQK DQALQTQPQY VAFSFVYILT GLTVIGAFLN
LVVLRFMTMN AEDEKRDAEH RALLTHNGQA VGLGGLSCLS GSLGDGVRPR DPVTCAAAAG
GVGVGVGGSG FRNVYAEVLH FQSMCSCLWY KSREKLQYSI PMIIPRDLST SDTCVEHSHS
SPGGGGRYSD TPSHPCLCSG TQRSAISSVS TGLHSLAAFR GLMKRRSSV
