{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O95069","secondaryAccessions":["A1Z1V3","A8K618","B2RCS4","B7ZL56","D3DTA5","Q5DP47","Q5DP48","Q9NRT2","Q9UNE3"],"uniProtkbId":"KCNK2_HUMAN","entryAudit":{"firstPublicDate":"2001-02-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-04-17","entryVersion":189,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Potassium channel subfamily K member 2"}},"alternativeNames":[{"fullName":{"value":"Outward rectifying potassium channel protein TREK-1"}},{"fullName":{"value":"TREK-1 K(+) channel subunit"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.15"}],"value":"Two pore domain potassium channel TREK1"}},{"fullName":{"value":"Two pore potassium channel TPKC1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.15"}],"value":"K2P2.1"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11319556"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:6277"}],"value":"KCNK2"},"synonyms":[{"value":"TREK"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.15"}],"value":"TREK1"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10321245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10784345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11319556"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23169818"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"30573346"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38605031"}],"value":"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:10321245, PubMed:10784345, PubMed:11319556, PubMed:23169818, PubMed:30573346, PubMed:38605031). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity). 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 (By similarity). 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 (By similarity). 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(+) (By similarity)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}],"value":"Does not display channel activity but reduces the channel activity of isoform 1 and isoform 2 and reduces cell surface expression of isoform 2"}],"commentType":"FUNCTION","molecule":"Isoform 4"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"K(+)(in) = K(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29463"},{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10321245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10784345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11319556"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate(out) = L-glutamate(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66336"},{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chloride(in) = chloride(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29823"},{"database":"ChEBI","id":"CHEBI:17996"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Rb(+)(in) = Rb(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:78547"},{"database":"ChEBI","id":"CHEBI:49847"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Cs(+)(in) = Cs(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:78555"},{"database":"ChEBI","id":"CHEBI:49547"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10321245"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10784345"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11319556"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"38605031"}],"value":"Activated by various stimuli including intracellular acidic pH, mechanical stretch and polyunsaturated fatty acids such as arachidonic acid. Activated by volatile anesthetics such as chloroform, halothane, and isoflurane"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"},{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26642364"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.15"}],"value":"Homodimer; disulfide-linked (Ref.15). Forms heterodimers with other 2-pore domain K(+) channel subunits, such as KCNK1, KCNK4, KCNK10 and KCNK18 (By similarity). Interacts with AKAP5; the channel is recruited to postsynaptic microdomains by AKAP5 where it can integrate neurotransmitter receptor signals. Part of a complex composed of AKAP5 and ADRB2. Upon AKAP5 binding, the channel is no longer sensitive to intracellular acidification, membrane stretch or arachidonic acid stimuli (By similarity). Interacts with POPDC1; the interaction enhances KCNK2 surface expression and is inhibited by cAMP (PubMed:26642364). Interacts (via N-terminus) with G protein subunit GNG4 (via C-terminus); this interaction confers ion selectivity to L-glutamate and Cl(-) anions (By similarity)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 2","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10784345"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 3","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23169818"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Isoform 4","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}],"value":"Localizes at the Ranvier nodes of myelinated afferent nerves"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}],"value":"Cell projection, axon","id":"SL-0279"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"}],"value":"Cell projection, dendrite","id":"SL-0283"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P97438"}],"value":"Postsynaptic density membrane","id":"SL-0520"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q920B6"}],"value":"Cell membrane, sarcolemma","id":"SL-0238"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"synonyms":[{"value":"TREK-1b"}],"isoformIds":["O95069-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"synonyms":[{"value":"TREK-1a"}],"isoformIds":["O95069-2"],"sequenceIds":["VSP_024429"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"synonyms":[{"value":"TREK-1c"}],"isoformIds":["O95069-3"],"sequenceIds":["VSP_024428"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"synonyms":[{"value":"TREK-1e"}],"isoformIds":["O95069-4"],"sequenceIds":["VSP_024428","VSP_047567","VSP_047568"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24196565"}],"value":"Detected in kidney, adrenal gland and brain where it is preferentially expressed in the amygdala but not found in thalamus, hypothalamus, hippocampus or substantia nigra"}],"commentType":"TISSUE SPECIFICITY","molecule":"Isoform 3"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9Y257"}],"value":"Each subunit contributes two pore-forming helices (PH1 and PH2), which assemble to form a single pore with M2 and M4 transmembrane helices lining the central cavity and M1 and M3 facing the lipid bilayer (By similarity). The transmembrane helices are bridged by two selectivity filters that coordinate the permeant ions (By similarity). Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation (By similarity)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"The C-terminal region of isoform 4 mediates its intracellular retention"}],"commentType":"DOMAIN","molecule":"Isoform 4"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11319556"}],"value":"Phosphorylation at Ser-348 controls the reversible conversion from a leak channel to a voltage-dependent channel"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the two pore domain potassium channel (TC 1.A.1.8) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"Potassium channel subfamily K member 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