ID   KCNK9_CAVPO             Reviewed;         365 AA.
AC   Q9JL58;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 93.
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;
GN   Name=KCNK9; Synonyms=TASK3;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS
RP   OF HIS-98.
RC   TISSUE=Brain;
RX   PubMed=10747866; DOI=10.1074/jbc.m000030200;
RA   Rajan S., Wischmeyer E., Liu G.X., Preisig-Mueller R., Daut J.,
RA   Karschin A., Derst C.;
RT   "TASK-3, a novel tandem pore domain acid-sensitive K+ channel. An
RT   extracellular histidine as pH sensor.";
RL   J. Biol. Chem. 275:16650-16657(2000).
CC   -!- FUNCTION: pH-dependent, voltage-insensitive, background potassium
CC       channel protein. {ECO:0000269|PubMed:10747866}.
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 brain.
CC       {ECO:0000269|PubMed:10747866}.
CC   -!- SIMILARITY: Belongs to the two pore domain potassium channel (TC
CC       1.A.1.8) family. {ECO:0000305}.
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DR   EMBL; AF212827; AAF63706.1; -; mRNA.
DR   RefSeq; NP_001166448.1; NM_001172977.1.
DR   AlphaFoldDB; Q9JL58; -.
DR   SMR; Q9JL58; -.
DR   STRING; 10141.ENSCPOP00000017207; -.
DR   GeneID; 100135568; -.
DR   KEGG; cpoc:100135568; -.
DR   CTD; 51305; -.
DR   eggNOG; KOG4404; Eukaryota.
DR   InParanoid; Q9JL58; -.
DR   OrthoDB; 1109218at2759; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW.
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   PIRSF; PIRSF038061; K_channel_subfamily_K_type; 1.
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.
FT   CHAIN           1..365
FT                   /note="Potassium channel subfamily K member 9"
FT                   /id="PRO_0000101753"
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..365
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->N,Y: Reduces sensitivity to alterations in
FT                   external pH."
FT                   /evidence="ECO:0000269|PubMed:10747866"
SQ   SEQUENCE   365 AA;  40769 MW;  261DC973FF53AF91 CRC64;
     MKKQNVRTLS LIACTFTYLL VGAAVFDALE SDHEMREEEK LKAEEIRIRG KYNISTEDYR
     QLELVILQSE PHRAGVQWKF AGSFYFAITV ITTIGYGHAA PGTDAGKAFC MFYAVLGIPL
     TLVMFQSLGE RMNTFVRYLL KRIKKCCGMR NTEVSMENMV TVGFFSCMGT LCIGAAAFSQ
     CEEWSFFHAY YYCFITLTTI GFGDYVALQS KGALQRKPFY VAFSFMYILV GLTVIGAFLN
     LVVLRFLTMN SDEERGEGEE GAALPGNPSS VVTHISEEAR QVRQRYRGEG GDLQSVCSCA
     CYRSQPQNFG ATLAPQPLHS ISCRIEEISP STLKNSLFPS PISSVSPGLH SFGDNHRLML
     RRKSV