Kcnk6
entrez
116491
canonical
uniprot
G3V8R8
canonical
ensembl
ENSRNOG00055033381
resolver
ensembl
ENSRNOG00060032841
resolver
ensembl
ENSRNOG00065034067
resolver
ensp
ENSRNOP00055047607
resolver
ensp
ENSRNOP00060046988
resolver
ensp
ENSRNOP00065048183
resolver
enst
ENSRNOT00055057721
resolver
enst
ENSRNOT00060056907
resolver
enst
ENSRNOT00065058534
resolver
genesymbol
Kcnk6
resolver
uniprot
Q9ERU4
resolver
uniprot
Q9ERU5
resolver
uniprot_entry
KCNK6_RAT
resolver
uniprot_sec
Q9ERU4
resolver
uniprot_sec
Q9ERU5
resolver
activity_regulation
ACTIVITY REGULATION: Partially inhibited by extracellular acidification and volatile anesthetics such as chloroform and halothane. Activated by arachidonic acid. Not affected by cytosolic acidification. {ECO:0000269|PubMed:10887187, ECO:0000269|PubMed:28381826}.
uniprot
proteins
amino_acid_sequence
MRRGALLASALVAYAGYLALGALLVARLERPHEARLRAELGTLREQLLRHSPCVAAHALDAFVERVLAAGRLGRAVLANASGPANASDPAWDFASALFFASTLVTTVGYGYTTPLTDAGKAFSIVFALLGVPITMLLLTASAQRLSLLLTHAPLSWLSLRWGWHPQRAARWHLVALLMVIVAIFFLIPAAVFAYLEEAWSFLDAFYFCFISLSTIGLGDYVPGEAPGQPYRSLYKVLVTAYLFLGLVAMVLVLQTFRRVSDLHGLTELILLPDPDPARLHQDEDDQVDILDARTDLHQHLSAASHANYASIPR
uniprot
proteins
function
FUNCTION: K(+) channel that conducts outward rectifying currents at the membranes of the endolysosomal system (PubMed:10887187, PubMed:28381826). Active in lysosomes where it regulates lysosome numbers and size (PubMed:28381826). In macrophages, enables K(+) efflux coupled to ATP-induced NLRP3 inflammasome activation upon bacterial infection. Cooperates with ATP-gated P2RX7 channels to activate NLRP3 inflammasome, with P2RX7 conducting Ca(2+) and Na(+) influx that sets the membrane potential for K(+) efflux (By similarity). {ECO:0000250|UniProtKB:Q3TBV4, ECO:0000269|PubMed:10887187, ECO:0000269|PubMed:28381826}.; FUNCTION: [Isoform 2]: Does not display channel activity. {ECO:0000269|PubMed:10887187}.
uniprot
proteins
mass_dalton
34183
uniprot
proteins
mutagenesis
MUTAGEN 53; /note="C->S: Decreases K(+) current amplitude."; /evidence="ECO:0000269|PubMed:10887187"; MUTAGEN 79; /note="N->L: No effect on protein localization. ER-like localization; when associated with N-85."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 85; /note="N->L: No effect on protein localization. ER-like localization; when associated with N-79."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 270; /note="L->A: Alters lysosomal targeting signal. Favors localization at the plasma membrane resulting in decreased K(+) current; when associated with A-271."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 271; /note="L->A: Alters lysosomal targeting signal. Favors localization at the plasma membrane resulting in decreased K(+) current; when associated with A-270."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 284; /note="D->A: Alters lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane; when associated with A-285."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 285; /note="D->A: Alters lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane; when associated with A-284."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 289; /note="I->A: Disrupts lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane. Displays additive effects resulting in a 10-fold increase of K(+) current; when associated with A-308 or A-311."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 290; /note="L->A: Disrupts lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane. Displays additive effects resulting in a 10-fold increase of K(+) current; when associated with A-308 or A-311."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 308; /note="Y->A: Disrupts lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane. Displays additive effects resulting in a 10-fold increase of K(+) current; when associated with A-289 or A-290."; /evidence="ECO:0000269|PubMed:28381826"; MUTAGEN 311; /note="I->A: Alters lysosomal targeting signal. Increases localization and K(+) current at the plasma membrane. Displays additive effects resulting in a 10-fold increase of K(+) current; when associated with A-289 or A-290."; /evidence="ECO:0000269|PubMed:28381826
uniprot
proteins
post_translational_modification
PTM: N-glycosylation is necessary for targeting to lysosomes. {ECO:0000269|PubMed:28381826}.
uniprot
proteins
protein_family
Two pore domain potassium channel (TC 1.A.1.8) family
uniprot
proteins
pubmed
10887187
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
28381826
uniprot
proteins
sequence_length
313
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Late endosome membrane {ECO:0000269|PubMed:28381826}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y257}. Lysosome membrane {ECO:0000269|PubMed:28381826}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9Y257}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..25; /note="Helical; Name=M1"; /evidence="ECO:0000250|UniProtKB:Q9Y257"; TRANSMEM 121..141; /note="Helical; Name=M2"; /evidence="ECO:0000250|UniProtKB:Q9Y257"; TRANSMEM 173..193; /note="Helical; Name=M3"; /evidence="ECO:0000250|UniProtKB:Q9Y257"; TRANSMEM 236..256; /note="Helical; Name=M4"; /evidence="ECO:0000250|UniProtKB:Q9Y257
uniprot
proteins