KCNK1_HUMAN

Evidence for PS localization

GO

G2C

SynGO

SynaptomeDB

HPA (protein expression in neurons)

Functions

Ion channel that contributes to passive transmembrane potassium transport and to the regulation of the resting membrane potential in brain astrocytes, but also in kidney and in other tissues (PubMed, PubMed). Forms dimeric channels through which potassium ions pass in accordance with their electrochemical gradient. The channel is selective for K(+) ions at physiological potassium concentrations and at neutral pH, but becomes permeable to Na(+) at subphysiological K(+) levels and upon acidification of the extracellular medium (PubMed, PubMed). The homodimer has very low potassium channel activity, when expressed in heterologous systems, and can function as weakly inward rectifying potassium channel (PubMed, PubMed, PubMed, PubMed, PubMed, PubMed, PubMed). Channel activity is modulated by activation of serotonin receptors . Heterodimeric channels containing KCNK1 and KCNK2 have much higher activity, and may represent the predominant form in astrocytes . Heterodimeric channels containing KCNK1 and KCNK3 or KCNK9 have much higher activity (PubMed). Heterodimeric channels formed by KCNK1 and KCNK9 may contribute to halothane-sensitive currents (PubMed). Mediates outward rectifying potassium currents in dentate gyrus granule cells and contributes to the regulation of their resting membrane potential . Contributes to the regulation of action potential firing in dentate gyrus granule cells and down-regulates their intrinsic excitability . In astrocytes, the heterodimer formed by KCNK1 and KCNK2 is required for rapid glutamate release in response to activation of G-protein coupled receptors, such as F2R and CNR1 . Required for normal ion and water transport in the kidney . Contributes to the regulation of the resting membrane potential of pancreatic beta cells . The low channel activity of homodimeric KCNK1 may be due to sumoylation (PubMed, PubMed, PubMed). The low channel activity may be due to rapid internalization from the cell membrane and retention in recycling endosomes (PubMed). [View more on UniProt]

Protein features

Binary interactions with known binding regions

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Network

Isoforms

Disease-causing germline mutations

No data found.

Linear motifs

No annotated instance was found. To search for linear motifs, use the ELM prediction server.

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Molecular function

Biological process

Disease

No data found.

All partners