Kcnk2
entrez
170899
canonical
uniprot
Q920B6
canonical
ensembl
ENSRNOG00000002653
resolver
ensembl
ENSRNOG00055010998
resolver
ensembl
ENSRNOG00060013583
resolver
ensembl
ENSRNOG00065016832
resolver
ensp
ENSRNOP00000003684
resolver
ensp
ENSRNOP00000068842
resolver
ensp
ENSRNOP00000077148
resolver
ensp
ENSRNOP00000087071
resolver
genesymbol
Kcnk2
resolver
genesymbol_syn
Trek
resolver
uniprot
A3QR52
resolver
uniprot
Q3MMY3
resolver
uniprot
Q5DNW4
resolver
uniprot
Q5DNW5
resolver
uniprot_entry
KCNK2_RAT
resolver
uniprot_sec
A3QR52
resolver
uniprot_sec
Q3MMY3
resolver
uniprot_sec
Q5DNW4
resolver
uniprot_sec
Q5DNW5
resolver
activity_regulation
ACTIVITY REGULATION: Activated by various stimuli including intracellular acidic pH, mechanical stretch and polyunsaturated fatty acids such as arachidonic acid. {ECO:0000269|PubMed:16248991, ECO:0000269|PubMed:26919430}.
uniprot
proteins
amino_acid_sequence
MLASASRERPGYTAGVAAPDLLDPKSAAQNSKPRLSFSAKPTVLASRVESDSAINVMKWKTVSTIFLVVVLYLIIGATVFKALEQPQEISQRTTIVIQKQNFIAQHACVNSTELDELIQQIVTAINAGIIPLGNNSNQVSHWDLGSSFFFAGTVITTIGFGNISPRTEGGKIFCIIYALLGIPLFGFLLAGVGDQLGTIFGKGIAKVEDTFIKWNVSQTKIRIISTIIFILFGCVLFVALPAVIFKHIEGWSALDAIYFVVITLTTIGFGDYVAGGSDIEYLDFYKPVVWFWILVGLAYFAAVLSMIGDWLRVISKKTKEEVGEFRAHAAEWTANVTAEFKETRRRLSVEIYDKFQRATSVKRKLSAELAGNHNQELTPCRRTLSVNHLTSEREVLPPLLKAESIYLNGLTPHCAAEDIAVIENMK
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. Reversibly converts between a voltage-insensitive K(+) 'leak' channel and a voltage-dependent outward rectifying K(+) channel in a phosphorylation-dependent manner (PubMed:11319556, PubMed:16248991, PubMed:19571146, PubMed:24196565, PubMed:26919430). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (PubMed:24196565). In trigeminal ganglia sensory neurons, the heterodimer of KCNK2/TREK-1 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). At trigeminal A-beta afferent nerves, the heterodimer of KCNK2/TREK-1 and KCNK4/TRAAK is mostly coexpressed at nodes of Ranvier where it conducts voltage-independent mechanosensitive and thermosensitive currents, allowing rapid action potential repolarization, high speed and high frequence saltatory conduction on myelinated nerves to ensure prompt sensory responses (PubMed:31630908). In hippocampal astrocytes, the heterodimer of KCNK2/TREK-1 and KCNK1/TWIK-1 allows passive K(+) conductance under basal conditions, but changes ion selectivity and becomes permeable to L-glutamate and Cl(-) ions upon binding to G protein subunit GNG4 in stimulated astrocytes. Mediates rapid L-glutamate release in response to activation of G protein-coupled receptors such as F2R and CNR1 (PubMed:23021213). In hippocampal pyramidal neurons, the homodimer of KCNK2/TREK-1 contributes to gamma-aminobutyric acid (GABA) B-induced slow inhibitory postsynaptic potential. Associates with AKAP5 and Gs-protein-coupled receptor B2AR at postsynaptic dense bodies and converts to a leak channel no longer sensitive to stimulation by arachidonic acid, acidic pH or mechanical stress, nor inhibited by Gq-coupled receptors but still under the negative control of Gs-coupled receptors (By similarity). Permeable to other monovalent cations such as Rb(+) and Cs(+) (PubMed:26919430). {ECO:0000250|UniProtKB:P97438, ECO:0000269|PubMed:11319556, ECO:0000269|PubMed:16248991, ECO:0000269|PubMed:19571146, ECO:0000269|PubMed:23021213, ECO:0000269|PubMed:24196565, ECO:0000269|PubMed:26919430, ECO:0000269|PubMed:31630908}.; FUNCTION: [Isoform 5]: Does not display channel activity but reduces the channel activity of isoform 1, isoform 2 and isoform 4 and reduces cell surface expression of isoform 2. {ECO:0000269|PubMed:24196565}.
uniprot
proteins
mass_dalton
46912
uniprot
proteins
mutagenesis
MUTAGEN 155; /note="I->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 156; /note="T->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 157; /note="T->C: Loss of voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 158; /note="I->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 162; /note="N->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 163; /note="I->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 265; /note="T->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 266; /note="T->C: Loss of voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 267; /note="I->C: No effect on voltage-dependent channel gating."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN Q920B6-2:144; /note="G->E: Loss of G protein-coupled receptor-induced anion conductance in astrocytes."; /evidence="ECO:0000269|PubMed:23021213
uniprot
proteins
post_translational_modification
PTM: Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel. {ECO:0000250|UniProtKB:O95069}.
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
11319556
uniprot
proteins
pubmed
11897838
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
16248991
uniprot
proteins
pubmed
19571146
uniprot
proteins
pubmed
23021213
uniprot
proteins
pubmed
24196565
uniprot
proteins
pubmed
26919430
uniprot
proteins
pubmed
31630908
uniprot
proteins
sequence_length
426
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: [Isoform 5]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24196565}; Multi-pass membrane protein {ECO:0000269|PubMed:24196565}.; SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:31630908}. Cell projection, dendrite {ECO:0000250|UniProtKB:P97438}. Postsynaptic density membrane {ECO:0000250|UniProtKB:P97438}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000269|PubMed:16248991}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes at the Ranvier nodes of myelinated afferent nerves. {ECO:0000269|PubMed:31630908}.
uniprot
proteins
transmembrane_region
TRANSMEM 58..80; /note="Helical; Name=M1"; /evidence="ECO:0000250|UniProtKB:O95069"; TRANSMEM 171..197; /note="Helical; Name=M2"; /evidence="ECO:0000250|UniProtKB:O95069"; TRANSMEM 225..244; /note="Helical; Name=M3"; /evidence="ECO:0000250|UniProtKB:O95069"; TRANSMEM 286..307; /note="Helical; Name=M4"; /evidence="ECO:0000250|UniProtKB:O95069
uniprot
proteins