KCNKI_RAT
ID KCNKI_RAT Reviewed; 405 AA.
AC Q6Q1P3;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Potassium channel subfamily K member 18;
DE AltName: Full=Tresk-2;
DE AltName: Full=Two-pore-domain potassium channel TRESK;
GN Name=Kcnk18; Synonyms=Tresk-2, Tresk2;
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], AND FUNCTION.
RC STRAIN=Sprague-Dawley; TISSUE=Spinal cord;
RX PubMed=16192517; DOI=10.1213/01.ane.0000168447.87557.5a;
RA Keshavaprasad B., Liu C., Au J.D., Kindler C.H., Cotten J.F., Yost C.S.;
RT "Species-specific differences in response to anesthetics and other
RT modulators by the K2P channel TRESK.";
RL Anesth. Analg. 101:1042-1049(2005).
CC -!- FUNCTION: Outward rectifying potassium channel. Produces rapidly
CC activating outward rectifier K(+) currents. May function as background
CC potassium channel that sets the resting membrane potential. Channel
CC activity is directly activated by calcium signal. Activated by the
CC G(q)-protein coupled receptor pathway. The calcium signal robustly
CC activates the channel via calcineurin, whereas the anchoring of 14-3-
CC 3/YWHAH interferes with the return of the current to the resting state
CC after activation. Inhibited also by arachidonic acid and other
CC naturally occurring unsaturated free fatty acids. Channel activity is
CC also enhanced by volatile anesthetics, such as isoflurane. Appears to
CC be the primary target of hydroxy-alpha-sanshool, an ingredient of
CC Schezuan pepper. May be involved in the somatosensory function with
CC special respect to pain sensation (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:16192517}.
CC -!- SUBUNIT: Interacts with calcineurin. Interacts with YWHAH, in a
CC phosphorylation-dependent manner. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- PTM: N-glycosylated. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Ser-275 is required for the binding of 14-3-
CC 3eta/YWHAH. Calcineurin-mediated dephosphorylation of Ser-287 enhances
CC channel activity (By similarity). {ECO:0000250}.
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; AY567970; AAS68516.1; -; mRNA.
DR RefSeq; NP_001003820.1; NM_001003820.1.
DR AlphaFoldDB; Q6Q1P3; -.
DR STRING; 10116.ENSRNOP00000039866; -.
DR GlyGen; Q6Q1P3; 1 site.
DR PaxDb; Q6Q1P3; -.
DR PRIDE; Q6Q1P3; -.
DR ABCD; Q6Q1P3; 1 sequenced antibody.
DR Ensembl; ENSRNOT00000042977; ENSRNOP00000039866; ENSRNOG00000032706.
DR GeneID; 445371; -.
DR KEGG; rno:445371; -.
DR CTD; 338567; -.
DR RGD; 1303091; Kcnk18.
DR eggNOG; KOG1418; Eukaryota.
DR GeneTree; ENSGT00700000104522; -.
DR InParanoid; Q6Q1P3; -.
DR OMA; FCCTVIS; -.
DR OrthoDB; 774951at2759; -.
DR PhylomeDB; Q6Q1P3; -.
DR TreeFam; TF316115; -.
DR Reactome; R-RNO-1299344; TWIK-related spinal cord K+ channel (TRESK).
DR Reactome; R-RNO-5576886; Phase 4 - resting membrane potential.
DR PRO; PR:Q6Q1P3; -.
DR Proteomes; UP000002494; Chromosome 1.
DR ExpressionAtlas; Q6Q1P3; baseline.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0015269; F:calcium-activated potassium channel activity; ISO:RGD.
DR GO; GO:0015271; F:outward rectifier potassium channel activity; ISO:RGD.
DR GO; GO:0022841; F:potassium ion leak channel activity; IBA:GO_Central.
DR GO; GO:0071467; P:cellular response to pH; ISO:RGD.
DR GO; GO:0097623; P:potassium ion export 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; ISS:UniProtKB.
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 PANTHER; PTHR11003; PTHR11003; 1.
DR Pfam; PF07885; Ion_trans_2; 2.
DR PRINTS; PR01333; 2POREKCHANEL.
DR PRINTS; PR01095; TASKCHANNEL.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Ion channel; Ion transport; Membrane;
KW Phosphoprotein; Potassium; Potassium channel; Potassium transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..405
FT /note="Potassium channel subfamily K member 18"
FT /id="PRO_0000312502"
FT TRANSMEM 43..63
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 125..151
FT /note="Pore-forming; Name=Pore-forming 1"
FT /evidence="ECO:0000255"
FT TRANSMEM 153..173
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255"
FT INTRAMEM 337..351
FT /note="Pore-forming; Name=Pore-forming 2"
FT /evidence="ECO:0000255"
FT TRANSMEM 358..378
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 221..226
FT /note="Interaction with calcineurin"
FT /evidence="ECO:0000250"
FT REGION 272..277
FT /note="Interaction with YWHAH"
FT /evidence="ECO:0000250"
FT MOD_RES 275
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VV64"
FT MOD_RES 287
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6VV64"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 405 AA; 45351 MW; 1E71325617575A8C CRC64;
MEAEEPPEAR RRCPEALGKA SGCCPEAPGK ARGCCPEALG KLLPGLCFLC CLVTYALVGA
ALFSAVEGRP DPEAEENPEL KKFLDKLCNI LKCNLTVVEG SRKDLCEHLQ QLKPQWFKAP
EDWSFLSALF FCCTVFSTVG YGHMYPVTRL GKFLCMLYAL FGIPLMFLVL TDIGDILAAI
LSRAYSRFQA LLCLPRDISK WRPLLLCRKQ TDSKPADEAI PQIVIDAGAD ELLDPQPSRE
PASPSCNVEL FERLVAREKQ NELQPPMRPV ERSNSCPELV LGRLSCSILS NLDEVGQQVE
RLDIPLPVIA LVIFAYISCA AAILPFWETD LGFEDAFYFC FVTLTTIGFG DIVLVHPHFF
LFFSIYIIVG MEILFIAFKL MQNRLLHTYK TLMLFVCQRE VSLPC
