Kcnk3
entrez
16527
canonical
uniprot
O35111
canonical
ensembl
ENSMUSG00000049265
resolver
ensp
ENSMUSP00000098987
resolver
enst
ENSMUST00000066295
resolver
genesymbol
Kcnk3
resolver
genesymbol_syn
Ctbak
resolver
genesymbol_syn
Task
resolver
genesymbol_syn
Task1
resolver
uniprot
O35163
resolver
uniprot_entry
KCNK3_MOUSE
resolver
uniprot_sec
O35163
resolver
activity_regulation
ACTIVITY REGULATION: Activated by halothane and isoflurane. Inhibited by external acidification, diacylglycerol and anandamide. Inactivated by barium. {ECO:0000269|PubMed:12634929, ECO:0000269|PubMed:9506712}.
uniprot
proteins
amino_acid_sequence
MKRQNVRTLALIVCTFTYLLVGAAVFDALESEPEMIERQRLELRQLELRARYNLSEGGYEELERVVLRLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVRYLLHRAKRGLGMRHAEVSMANMVLIGFVSCISTLCIGAAAFSYYERWTFFQAYYYCFITLTTIGFGDYVALQKDQALQTQPQYVAFSFVYILTGLTVIGAFLNLVVLRFMTMNAEDEKRDAEHRALLTHNGQAVGLGGLSCLSGSLGDGVRPRDPVTCAAAAGGVGVGVGGSGFRNVYAEVLHFQSMCSCLWYKSREKLQYSIPMIIPRDLSTSDTCVEHSHSSPGGGGRYSDTPSHPCLCSGTQRSAISSVSTGLHSLAAFRGLMKRRSSV
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 (By similarity) (PubMed:12634929, PubMed:18034154, PubMed:18250325, PubMed:28988768, PubMed:9506712). Changes ion selectivity and becomes permeable to Na(+) ions in response to extracellular acidification. Protonation of the pH sensor His-98 stabilizes C-type inactivation conformation likely converting the channel from outward K(+)-conducting, to inward Na(+)-conducting to nonconductive state. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity). Allows K(+) currents with fast-gating kinetics important for the repolarization and hyperpolarization phases of action potentials (By similarity) (PubMed:18250325). In cerebellar granule cells, heteromeric KCNK3:KCNK9 channel may hyperpolarize the resting membrane potential to limit intrinsic neuronal excitability, but once the action potential threshold is reached, it may support high-frequency action potential firing and increased neuronal excitability (Probable). Dispensable for central chemosensory respiration i.e. breathing controlled by brainstem CO2/pH, it rather conducts pH-sensitive currents and controls the firing rate of serotonergic raphe neurons involved in potentiation of the respiratory chemoreflex. Additionally, imparts chemosensitivity to type 1 cells in carotid bodies which respond to a decrease in arterial oxygen pressure or an increase in carbon dioxide pressure or pH to initiate adaptive changes in pulmonary ventilation (PubMed:18094244, PubMed:18753386). In adrenal gland, contributes to the maintenance of a hyperpolarized resting membrane potential of aldosterone-producing cells at zona glomerulosa and limits aldosterone release as part of a regulatory mechanism that controls arterial blood pressure and electrolyte homeostasis (PubMed:18034154, PubMed:18250325). In brown adipocytes, mediates K(+) efflux that counteracts norepinephrine-induced membrane depolarization, limits Ca(2+) efflux and downstream cAMP and PKA signaling, ultimately attenuating lipid oxidation and adaptive thermogenesis (PubMed:28988768). {ECO:0000250|UniProtKB:O14649, ECO:0000250|UniProtKB:O54912, ECO:0000269|PubMed:12634929, ECO:0000269|PubMed:18034154, ECO:0000269|PubMed:18094244, ECO:0000269|PubMed:18250325, ECO:0000269|PubMed:18753386, ECO:0000269|PubMed:28988768, ECO:0000269|PubMed:9506712, ECO:0000305|PubMed:17728447}.
uniprot
proteins
mass_dalton
45068
uniprot
proteins
mutagenesis
MUTAGEN 72; /note="H->N: Increases sensitivity to extracellular pH variations. Can bind two protons per molecule similarly to wild-type."; /evidence="ECO:0000269|PubMed:12634929"; MUTAGEN 73; /note="K->N: No effect on the sensitivity to extracellular pH variations."; /evidence="ECO:0000269|PubMed:12634929"; MUTAGEN 98; /note="H->D: Decreases inhibition of K(+) currents by extracellular acidification. Can bind one proton per molecule."; /evidence="ECO:0000269|PubMed:12634929"; MUTAGEN 98; /note="H->N: Decreases inhibition of K(+) currents by extracellular acidification. Can bind one proton per molecule."; /evidence="ECO:0000269|PubMed:12634929"; MUTAGEN 210; /note="K->N: Decreases sensitivity to extracellular pH variations. Can bind two protons per molecule similarly to wild-type."; /evidence="ECO:0000269|PubMed:12634929
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
10748056
uniprot
proteins
pubmed
12634929
uniprot
proteins
pubmed
17728447
uniprot
proteins
pubmed
18034154
uniprot
proteins
pubmed
18094244
uniprot
proteins
pubmed
18250325
uniprot
proteins
pubmed
18753386
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
28988768
uniprot
proteins
pubmed
40108405
uniprot
proteins
pubmed
9312005
uniprot
proteins
pubmed
9506712
uniprot
proteins
sequence_length
409
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:40108405}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14649}.
uniprot
proteins
transmembrane_region
TRANSMEM 9..29; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 108..128; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 159..179; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 223..243; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins