KCNK9

KCNK9
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3P1N, 3P1O, 3P1P, 3P1Q, 3P1R, 3P1S, 3SMK, 3SML, 3SMM, 3SMN, 3SMO, 3SPR, 3UX0, 4FR3, 3SP5
Identifiers
Aliases	KCNK9, K2p9.1, KT3.2, TASK-3, TASK3, potassium two pore domain channel subfamily K member 9, BIBARS, TASK32
External IDs	OMIM: 605874; MGI: 3521816; HomoloGene: 56758; GeneCards: KCNK9; OMA:KCNK9 - orthologs
Gene location (Human)
Chr.	Chromosome 8 (human)
End	139,704,109 bp
RNA expression pattern
	Top expressed in
	cerebellar hemisphere; ; right hemisphere of cerebellum; ; cerebellar vermis; ; right frontal lobe; ; secondary oocyte; ; Brodmann area 9; ; prefrontal cortex; ; primary visual cortex; ; Brodmann area 23; ; Hypothalamus;
	n/a
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	voltage-gated potassium channel activity; protein homodimerization activity; protein heterodimerization activity; potassium channel activity; potassium ion leak channel activity;
Cellular component	integral component of membrane; plasma membrane; membrane; synaptic vesicle; integral component of plasma membrane;
Biological process	potassium ion transport; ion transport; stabilization of membrane potential; potassium ion transmembrane transport;
	Sources:Amigo / QuickGO
Orthologs
	51305
	223604
	ENSG00000169427
	n/a
	Q9NPC2
	Q3LS21
	NM_001282534
	NM_001033876
	NP_001269463
	NP_001029048
	Wikidata
View/Edit Human	View/Edit Mouse

Potassium channel subfamily K member 9 is a protein that in humans is encoded by the KCNK9 gene.

This gene encodes K_2P9.1, one of the members of the superfamily of potassium channel proteins containing two pore-forming P domains. This open channel is highly expressed in the cerebellum. It is inhibited by extracellular acidification and arachidonic acid, and strongly inhibited by phorbol 12-myristate 13-acetate. Phorbol 12-myristate 13-acetate is also known as 12-O-tetradecanoylphorbol-13-acetate (TPA). TASK channels are additionally inhibited by hormones and transmitters that signal through GqPCRs. The resulting cellular depolarization is thought to regulate processes such as motor control and aldosterone secretion. Despite early controversy about the exact mechanism underlying this inhibition, the current view is that Diacyl-glycerol, produced by the breakdown of Phosphatidylinositol-4,5-bis-phosphate by Phospholipase Cβ causes channel closure.