KCNK9
entrez
51305
canonical
uniprot
Q9NPC2
canonical
ensembl
ENSG00000169427
resolver
ensp
ENSP00000302166
resolver
ensp
ENSP00000429847
resolver
ensp
ENSP00000430676
resolver
ensp
ENSP00000496915
resolver
ensp
ENSP00000498198
resolver
enst
ENST00000303015
resolver
enst
ENST00000520439
resolver
enst
ENST00000522317
resolver
enst
ENST00000648164
resolver
enst
ENST00000650269
resolver
genesymbol
KCNK9
resolver
genesymbol_syn
TASK3
resolver
hgnc
HGNC:6283
resolver
uniprot
Q2M290
resolver
uniprot
Q540F2
resolver
uniprot_entry
KCNK9_HUMAN
resolver
uniprot_sec
Q2M290
resolver
uniprot_sec
Q540F2
resolver
activity_regulation
ACTIVITY REGULATION: Inhibited by extracellular acidification adopting a nonconductive conformation at pH 6.0. Inhibited by phorbol 12-myristate 13-acetate (PMA). {ECO:0000269|PubMed:11042359, ECO:0000269|PubMed:11431495}.
uniprot
proteins
amino_acid_sequence
MKRQNVRTLSLIVCTFTYLLVGAAVFDALESDHEMREEEKLKAEEIRIKGKYNISSEDYRQLELVILQSEPHRAGVQWKFAGSFYFAITVITTIGYGHAAPGTDAGKAFCMFYAVLGIPLTLVMFQSLGERMNTFVRYLLKRIKKCCGMRNTDVSMENMVTVGFFSCMGTLCIGAAAFSQCEEWSFFHAYYYCFITLTTIGFGDYVALQTKGALQKKPLYVAFSFMYILVGLTVIGAFLNLVVLRFLTMNSEDERRDAEERASLAGNRNSMVIHIPEEPRPSRPRYKADVPDLQSVCSCTCYRSQDYGGRSVAPQNSFSAKLAPHYFHSISYKIEEISPSTLKNSLFPSPISSISPGLHSFTDHQRLMKRRKSV
uniprot
proteins
disease_involvement
DISEASE: Birk-Barel syndrome (BIBARS) [MIM:612292]: A syndrome characterized by intellectual disability, hypotonia, hyperactivity, and facial dysmorphism. BIBARS transmission pattern is consistent with autosomal dominant inheritance with paternal imprinting. {ECO:0000269|PubMed:18678320, ECO:0000269|PubMed:27151206, ECO:0000269|PubMed:30690205}. Note=The disease is caused by variants affecting the gene represented in this entry.
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 (PubMed:11042359, PubMed:11431495, PubMed:26919430, PubMed:38630723). 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 (PubMed:22948150, PubMed:38630723). Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity) (PubMed:23169818, PubMed:38630723). Allows K(+) currents with fast-gating kinetics important for the repolarization and hyperpolarization phases of action potentials (By similarity). In granule neurons, hyperpolarizes the resting membrane potential to limit intrinsic neuronal excitability, but once the action potential threshold is reached, supports high-frequency action potential firing and increased neuronal excitability. Homomeric and/or heteromeric KCNK3:KCNK9 channels operate in cerebellar granule cells, whereas heteromeric KCNK1:KCNK9 enables currents in hippocampal dentate gyrus granule neurons (By similarity). 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 (By similarity). In retinal ganglion cells, mediates outward currents that regulate action potentials in response to acidification of the synaptic cleft. Involved in transmission of image-forming and nonimage-forming visual information in the retina (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q3LS21, ECO:0000250|UniProtKB:Q9ES08, ECO:0000269|PubMed:11042359, ECO:0000269|PubMed:11431495, ECO:0000269|PubMed:22948150, ECO:0000269|PubMed:23169818, ECO:0000269|PubMed:26919430, ECO:0000269|PubMed:38630723}.
uniprot
proteins
mass_dalton
42264
uniprot
proteins
mutagenesis
MUTAGEN 78; /note="W->A,L,F: Impairs channel inhibition by extracellular acidification."; /evidence="ECO:0000269|PubMed:38630723"; MUTAGEN 93; /note="T->C: Abolishes voltage gating. Conducts currents with linear I-V relationship characteristic of classical leak channels."; /evidence="ECO:0000269|PubMed:26919430"; MUTAGEN 98; /note="H->D,N: Impairs channel inhibition by extracellular acidification. Does not affect channel ion selectivity."; /evidence="ECO:0000269|PubMed:22948150, ECO:0000269|PubMed:38630723"; MUTAGEN 199; /note="T->C: Abolishes voltage gating. Conducts currents with linear I-V relationship characteristic of classical leak channels."; /evidence="ECO:0000269|PubMed:26919430
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
10747866
uniprot
proteins
pubmed
11042359
uniprot
proteins
pubmed
11431495
uniprot
proteins
pubmed
12676587
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
18678320
uniprot
proteins
pubmed
22948150
uniprot
proteins
pubmed
23169818
uniprot
proteins
pubmed
26919430
uniprot
proteins
pubmed
27151206
uniprot
proteins
pubmed
30690205
uniprot
proteins
pubmed
38630723
uniprot
proteins
sequence_length
374
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23169818}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q3LS21}; Multi-pass membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q3LS21}. Note=Colocalizes with MAP2 in the soma and proximal dendrites of dentate gyrus granule cells. {ECO:0000250|UniProtKB:Q3LS21}.
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 219..239; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins