KCNK9_RAT
ID KCNK9_RAT Reviewed; 396 AA.
AC Q9ES08; Q923V6; Q9JLD4;
DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 10-JAN-2006, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Potassium channel subfamily K member 9;
DE AltName: Full=Acid-sensitive potassium channel protein TASK-3;
DE AltName: Full=TWIK-related acid-sensitive K(+) channel 3;
DE AltName: Full=Two pore potassium channel KT3.2;
DE Short=Two pore K(+) channel KT3.2;
GN Name=Kcnk9; Synonyms=Task3;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP OF HIS-98.
RC STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
RX PubMed=10734076; DOI=10.1074/jbc.275.13.9340;
RA Kim Y., Bang H., Kim D.;
RT "TASK-3, a new member of the tandem pore K+ channel family.";
RL J. Biol. Chem. 275:9340-9347(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=Wistar;
RX PubMed=11875121; DOI=10.1210/mend.16.3.0788;
RA Czirjak G., Enyedi P.;
RT "TASK-3 dominates the background potassium conductance in rat adrenal
RT glomerulosa cells.";
RL Mol. Endocrinol. 16:621-629(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-237, AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley;
RX PubMed=11431495; DOI=10.1152/jn.2001.86.1.130;
RA Vega-Saenz de Miera E., Lau D.H.P., Zhadina M., Pountney D., Coetzee W.A.,
RA Rudy B.;
RT "KT3.2 and KT3.3, two novel human two-pore K(+) channels closely related to
RT TASK-1.";
RL J. Neurophysiol. 86:130-142(2001).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=11749039; DOI=10.1006/mcne.2001.1045;
RA Karschin C., Wischmeyer E., Preisig-Mueller R., Rajan S., Derst C.,
RA Grzeschik K.-H., Daut J., Karschin A.;
RT "Expression pattern in brain of TASK-1, TASK-3, and a tandem pore domain
RT K(+) channel subunit, TASK-5, associated with the central auditory nervous
RT system.";
RL Mol. Cell. Neurosci. 18:632-648(2001).
CC -!- FUNCTION: pH-dependent, voltage-insensitive, background potassium
CC channel protein. {ECO:0000269|PubMed:10734076,
CC ECO:0000269|PubMed:11875121}.
CC -!- SUBUNIT: Homodimer. Heterodimer with KCNK1.
CC {ECO:0000250|UniProtKB:Q9NPC2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NPC2};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9NPC2}.
CC -!- TISSUE SPECIFICITY: Highly expressed in the CNS and at lower levels in
CC the colon, kidney, liver, lung, spleen, stomach and skeletal muscle.
CC The highest expression was found in the olfactory nuclei, piriform
CC cortex, cerebellum, antedorsal thalmic nucleus, pontine nucleus, dorsal
CC raphe and several nuclei in the medulla. Shows a non-homogeneous
CC distribution in the hippocampus. Expressed at highest levels in the
CC lateral posterior and inferior portions and at medium levels in
CC neocortex. {ECO:0000269|PubMed:10734076, ECO:0000269|PubMed:11431495,
CC ECO:0000269|PubMed:11749039, ECO:0000269|PubMed:11875121}.
CC -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC 1.A.1.8) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF60229.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF192366; AAF60229.1; ALT_FRAME; mRNA.
DR EMBL; AF391084; AAK69764.1; -; mRNA.
DR EMBL; AF257082; AAG33128.1; -; mRNA.
DR RefSeq; NP_445857.2; NM_053405.2.
DR RefSeq; XP_017450625.1; XM_017595136.1.
DR AlphaFoldDB; Q9ES08; -.
DR SMR; Q9ES08; -.
DR DIP; DIP-61122N; -.
DR IntAct; Q9ES08; 1.
DR STRING; 10116.ENSRNOP00000012408; -.
DR BindingDB; Q9ES08; -.
DR ChEMBL; CHEMBL4295; -.
DR GlyGen; Q9ES08; 1 site.
DR PaxDb; Q9ES08; -.
DR Ensembl; ENSRNOT00000012408; ENSRNOP00000012408; ENSRNOG00000009265.
DR GeneID; 84429; -.
DR KEGG; rno:84429; -.
DR UCSC; RGD:621451; rat.
DR CTD; 51305; -.
DR RGD; 621451; Kcnk9.
DR eggNOG; KOG4404; Eukaryota.
DR GeneTree; ENSGT00940000159791; -.
DR HOGENOM; CLU_022504_4_0_1; -.
DR InParanoid; Q9ES08; -.
DR OMA; TAWFGQV; -.
DR OrthoDB; 1109218at2759; -.
DR PhylomeDB; Q9ES08; -.
DR TreeFam; TF313947; -.
DR Reactome; R-RNO-1299316; TWIK-releated acid-sensitive K+ channel (TASK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q9ES08; -.
DR Proteomes; UP000002494; Chromosome 7.
DR Bgee; ENSRNOG00000009265; Expressed in frontal cortex and 1 other tissue.
DR Genevisible; Q9ES08; RN.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:0005267; F:potassium channel activity; ISO:RGD.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; ISO:RGD.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; ISO:RGD.
DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
DR GO; GO:0006813; P:potassium ion transport; IDA:RGD.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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; IPR005407; KCNK9.
DR PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01585; TASK3CHANNEL.
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; Voltage-gated channel.
FT CHAIN 1..396
FT /note="Potassium channel subfamily K member 9"
FT /id="PRO_0000101756"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..88
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 89..101
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 102..107
FT /note="Extracellular"
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 TOPO_DOM 180..194
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT INTRAMEM 195..207
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 208..218
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..396
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 53
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 98
FT /note="H->D: Reduces sensitivity to alterations in external
FT pH."
FT /evidence="ECO:0000269|PubMed:10734076"
SQ SEQUENCE 396 AA; 44357 MW; 734EB0EEA1ED1828 CRC64;
MKRQNVRTLS LIACTFTYLL VGAAVFDALE SDHEMREEEK LKAEEVRLRG KYNISSDDYQ
QLELVILQSE PHRAGVQWKF AGSFYFAITV ITTIGYGHAA PGTDAGKAFC MFYAVLGIPL
TLVMFQSLGE RMNTFVRYLL KRIKKCCGMR NTEVSMENMV TVGFFSCMGT LCLGAAAFSQ
CEDWSFFHAY YYCFITLTTI GFGDFVALQS KGALQRKPFY VAFSFMYILV GLTVIGAFLN
LVVLRFLTMN TDEDLLEGEV AQILAGNPRR VVVRVPQSRK RHHPMYFLRK YGRTLCYLCF
PGANWGDDDD DDDDAVENVV VTTPVPPAVA AAAAAATPGP STRNVRATVH SVSCRVEEIP
PDVLRNTYFR SPFGAIPPGM HTCGENHRLH IRRKSI
