Kcnk10
entrez
72258
canonical
uniprot
Q8BUW1
canonical
ensembl
ENSMUSG00000033854
resolver
ensp
ENSMUSP00000105740
resolver
ensp
ENSMUSP00000152473
resolver
ensp
ENSMUSP00000152656
resolver
enst
ENSMUST00000221305
resolver
genesymbol
Kcnk10
resolver
uniprot
A0A1Y7VJZ9
resolver
uniprot
A0AAR0ST50
resolver
uniprot
F6YU65
resolver
uniprot
Q3LS20
resolver
uniprot
Q8BZB0
resolver
uniprot
Q9CX88
resolver
uniprot_entry
A0AAR0ST50_MOUSE
resolver
uniprot_entry
KCNKA_MOUSE
resolver
uniprot_entry
Q3LS20_MOUSE
resolver
uniprot_entry
Q8BZB0_MOUSE
resolver
uniprot_sec
A0A1Y7VJZ9
resolver
uniprot_sec
F6YU65
resolver
uniprot_sec
Q9CX88
resolver
activity_regulation
ACTIVITY REGULATION: Activated by stimuli such as mechanical stretch, acidic pH and polyunsaturated free fatty acids (PubMed:19667202, PubMed:27035963). Activated by a dihydroacridine analog, ML67-33 (PubMed:34458705). Inhibited by polycationic dye ruthenium red (PubMed:27035965). Selectively activated by T2A3 (2-[(4-chloro-3-methylphenyl)amino] benzoic acid) (PubMed:32641496). {ECO:0000269|PubMed:19667202, ECO:0000269|PubMed:27035963, ECO:0000269|PubMed:27035965, ECO:0000269|PubMed:32641496, ECO:0000269|PubMed:34458705}.
uniprot
proteins
amino_acid_sequence
MYFSYIGYFFLPPLVAVPAAAPPVCQPKSATNGHHPVPRLSISSRATVVARMEGASQGGLQTVMKWKTVVAIFVVVVVYLVTGGLVFRALEQPFESSQKNTIALEKAEFLRDHICVSPQELETLIQHALDADNAGVSPVGNSSNSSSHWDLGSAFFFAGTVITTIGYGNIAPSTEGGKIFCILYAIFGIPLFGFLLAGIGDQLGTIFGKSIARVEKVFRKKQVSQTKIRVISTILFILAGCIVFVTIPAVIFKYIEGWTALESIYFVVVTLTTVGFGDFVAGGNAGINYREWYKPLVWFWILVGLAYFAAVLSMIGDWLRVLSKKTKEEVGEIKAHAAEWKANVTAEFRETRRRLSVEIHDKLQRAATIRSMERRRLGLDQRAHSLDMLSPEKRSVFAALDTGRFKASSQESINNRPNNLRLKGPEQLTKHGQGASEDNIINKFGSTSKLTKRKNKDLKKTLPEDVQKIYKTFRNYSLDEEKKEDETEKMCNSDNSSTAMLTECIQQQAEMENGMVPTDTKDQGLENNSLLEDRN
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:27035963, PubMed:27035965). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (PubMed:19667202, PubMed:27035963, PubMed:27035965). 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 (PubMed:30573346, PubMed:32641496, PubMed:34458705). Permeable to other monovalent ions such as Rb(+) and Cs(+) (By similarity). {ECO:0000250|UniProtKB:P57789, ECO:0000269|PubMed:19667202, ECO:0000269|PubMed:27035963, ECO:0000269|PubMed:27035965, ECO:0000269|PubMed:30573346, ECO:0000269|PubMed:32641496, ECO:0000269|PubMed:34458705}.
uniprot
proteins
mass_dalton
59401
uniprot
proteins
mutagenesis
MUTAGEN 148; /note="H->A: Decreased basal mean amplitude of channel current."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 148; /note="H->K: Increased basal mean amplitude of channel current."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 279; /note="F->Y: No effect on extracellular pH sensing. Causes reduced inhibition induced by a pH shift from 7.2 to 8; when associated with S-284, D-285 and E-288. Inverts pH-dependent gating, with channel conductance being inhibited by acidic pH and activated by basic pH; when associated with S-284, D-285, E-288 and L-290."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 284; /note="N->S: No effect on extracellular pH sensing. Causes reduced inhibition induced by a pH shift from 7.2 to 8; when associated with Y-279, D-285 and E-288. Inverts pH-dependent gating, with channel conductance being inhibited by acidic pH and activated by basic pH; when associated with Y-279, D-285, E-288 and L-290."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 285; /note="A->D: No effect on extracellular pH sensing. Causes reduced inhibition induced by a pH shift from 7.2 to 8; when associated with S-279, S-284 and E-288. Inverts pH-dependent gating, with channel conductance being inhibited by acidic pH and activated by basic pH; when associated with Y-279, S-284, E-288 and L-290."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 288; /note="N->E: No effect on extracellular pH sensing. Causes reduced inhibition induced by a pH shift from 7.2 to 8; when associated with S-279, S-284 and D-285. Inverts pH-dependent gating, with channel conductance being inhibited by acidic pH and activated by basic pH; when associated with Y-279, S-284, D-285 and L-290."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN 290; /note="R->L: Loss of K(+) channel activity. Normal basal conductance but reduced inhibition induced by a pH shift from 7.2 to 8; when associated with Y-279. Inverts pH-dependent gating, with channel conductance being inhibited by acidic pH and activated by basic pH; when associated with Y-279, S-284, D-285 and E-288."; /evidence="ECO:0000269|PubMed:19667202"; MUTAGEN Q8BUW1-3:135; /note="D->I: Confers resistance to ruthenium red."; /evidence="ECO:0000269|PubMed:27035965"; MUTAGEN Q8BUW1-3:151; /note="H->A: Mimics the deprotonated state and decreases the basal current. In heterodimer with KCNK2, it displays KCNK2-like pH dependence."; /evidence="ECO:0000269|PubMed:27035963"; MUTAGEN Q8BUW1-3:151; /note="H->K: Mimics the protonated state and increases the basal current. In heterodimer with KCNK2, it displays KCNK2-like pH dependence."; /evidence="ECO:0000269|PubMed:27035963
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
19667202
uniprot
proteins
pubmed
27035963
uniprot
proteins
pubmed
27035965
uniprot
proteins
pubmed
30573346
uniprot
proteins
pubmed
32641496
uniprot
proteins
pubmed
34458705
uniprot
proteins
sequence_length
535
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27035965}; Multi-pass membrane protein {ECO:0000255}.
uniprot
proteins
transmembrane_region
TRANSMEM 69..89; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 179..199; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 231..251; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 296..316; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins