KCNK10
entrez
54207
canonical
uniprot
P57789
canonical
ensembl
ENSG00000100433
resolver
ensp
ENSP00000310568
resolver
ensp
ENSP00000312811
resolver
ensp
ENSP00000343104
resolver
genesymbol
KCNK10
resolver
genesymbol_syn
TREK2
resolver
hgnc
HGNC:6273
resolver
uniprot
B2R8T4
resolver
uniprot
B2RCT3
resolver
uniprot
B5TJL4
resolver
uniprot
Q6B014
resolver
uniprot
Q8TDK7
resolver
uniprot
Q8TDK8
resolver
uniprot
Q9HB59
resolver
uniprot_entry
KCNKA_HUMAN
resolver
uniprot_sec
B2R8T4
resolver
uniprot_sec
B2RCT3
resolver
uniprot_sec
B5TJL4
resolver
uniprot_sec
Q6B014
resolver
uniprot_sec
Q8TDK7
resolver
uniprot_sec
Q8TDK8
resolver
uniprot_sec
Q9HB59
resolver
activity_regulation
ACTIVITY REGULATION: Activated by various stimuli including acidic pH, anesthetics chloroform, halothane and isoflurane, mechanical stretch, lipids such as arachidonic, docosahexaenoic and linoleic polyunsaturated fatty acids and lysophosphatidylcholine and lysophosphatidylinositol lysophospholipids (PubMed:10880510, PubMed:25766236, PubMed:26919430, PubMed:38605031). Inhibited by norfluoxetine, the active metabolite of antidepressant fluoxetine (Prozac) (PubMed:25766236). {ECO:0000269|PubMed:10880510, ECO:0000269|PubMed:25766236, ECO:0000269|PubMed:26919430, ECO:0000269|PubMed:38605031}.
uniprot
proteins
amino_acid_sequence
MFFLYTDFFLSLVAVPAAAPVCQPKSATNGQPPAPAPTPTPRLSISSRATVVARMEGTSQGGLQTVMKWKTVVAIFVVVVVYLVTGGLVFRALEQPFESSQKNTIALEKAEFLRDHVCVSPQELETLIQHALDADNAGVSPIGNSSNNSSHWDLGSAFFFAGTVITTIGYGNIAPSTEGGKIFCILYAIFGIPLFGFLLAGIGDQLGTIFGKSIARVEKVFRKKQVSQTKIRVISTILFILAGCIVFVTIPAVIFKYIEGWTALESIYFVVVTLTTVGFGDFVAGGNAGINYREWYKPLVWFWILVGLAYFAAVLSMIGDWLRVLSKKTKEEVGEIKAHAAEWKANVTAEFRETRRRLSVEIHDKLQRAATIRSMERRRLGLDQRAHSLDMLSPEKRSVFAALDTGRFKASSQESINNRPNNLRLKGPEQLNKHGQGASEDNIINKFGSTSRLTKRKNKDLKKTLPEDVQKIYKTFRNYSLDEEKKEEETEKMCNSDNSSTAMLTDCIQQHAELENGMIPTDTKDREPENNSLLEDRN
uniprot
proteins
function
FUNCTION: K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Converts to voltage-independent 'leak' conductance mode upon stimulation by various stimuli including mechanical membrane stretch, acidic pH, heat and lipids (PubMed:10880510, PubMed:25766236, PubMed:26919430, PubMed:38605031). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (PubMed:30573346). In trigeminal ganglia sensory neurons, the heterodimer of KCNK10/TREK-2 and KCNK18/TRESK inhibits neuronal firing and neurogenic inflammation by stabilizing the resting membrane potential at K(+) equilibrium potential as well as by regulating the threshold of action potentials and the spike frequency (By similarity). Permeable to other monovalent ions such as Rb(+) and Cs(+) (PubMed:26919430). {ECO:0000250|UniProtKB:Q8BUW1, ECO:0000269|PubMed:10880510, ECO:0000269|PubMed:25766236, ECO:0000269|PubMed:26919430, ECO:0000269|PubMed:30573346, ECO:0000269|PubMed:38605031}.
uniprot
proteins
mass_dalton
59765
uniprot
proteins
mutagenesis
MUTAGEN 98; /note="E->Q: Loss of channel gating by extracellular pH."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 151; /note="H->A: Loss of channel gating by extracellular pH."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 174; /note="A->P: Loss of channel gating by extracellular pH."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 210; /note="F->A: Reduces channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 232; /note="R->A: Reduces channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 239; /note="F->A: No effect on channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 310; /note="Y->A: Near complete loss of channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 310; /note="Y->F: Reduces channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 315; /note="L->W: Reduces norfluoxetine inhibition."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 317; /note="M->A: Reduces channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236"; MUTAGEN 321; /note="W->A: Reduces channel gating by mechanical membrane stretch."; /evidence="ECO:0000269|PubMed:25766236
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
10880510
uniprot
proteins
pubmed
11897838
uniprot
proteins
pubmed
12508121
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18516069
uniprot
proteins
pubmed
25766236
uniprot
proteins
pubmed
26919430
uniprot
proteins
pubmed
30573346
uniprot
proteins
pubmed
38605031
uniprot
proteins
sequence_length
538
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8BUW1}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 72..92; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 182..202; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 234..254; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 299..319; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins