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http://purl.uniprot.org/citations/11680614http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11680614http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11680614http://www.w3.org/2000/01/rdf-schema#comment"We have cloned a novel member of the tandem pore K+ channel family from human brain cDNA. The novel cDNA encodes a 330-residue polypeptide of predicted molecular mass 36 kDa. We have named the channel TASK-5 owing to its sequence homology with TASK-1 and TASK-3. TASK-5 mRNA is expressed in pancreas, liver, kidney, lung, ovary, testis and heart. However, expression of TASK-5 in heterologous systems failed to elicit ionic currents. Removal of a putative endoplasmic reticulum retention sequence did not alter this finding and the distribution of channel proteins in HEK293 cells was similar for both TASK-1 and TASK-5. We tested whether TASK-5 could form heteromers with TASK-1. We show a mutant form of TASK-1 (H98N) to have a radically reduced sensitivity to acidification. Proton sensitivity could be rescued by injecting equimolar amounts of wild-type and mutant TASK-1 cRNA into Xenopus oocytes; the effect was that expected if half the channels formed are heteromers. Co-expression of TASK-5 with TASK-1 H98N does not affect the proton sensitivity of mutant TASK-1; thus TASK-5 appears not to form heteromers with TASK-1. Nonetheless, TASK-5 may require some other, unidentified partner subunit to form functional channels in the plasma membrane or it may form a channel in an intracellular organelle."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.org/dc/terms/identifier"doi:10.1007/s004240100620"xsd:string
http://purl.uniprot.org/citations/11680614http://purl.org/dc/terms/identifier"doi:10.1007/s004240100620"xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Ashmole I."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Ashmole I."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Goodwin P.A."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Goodwin P.A."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Stanfield P.R."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/author"Stanfield P.R."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/name"Pflugers Arch."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/name"Pflugers Arch."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/pages"828-833"xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/pages"828-833"xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/title"TASK-5, a novel member of the tandem pore K+ channel family."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/title"TASK-5, a novel member of the tandem pore K+ channel family."xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/volume"442"xsd:string
http://purl.uniprot.org/citations/11680614http://purl.uniprot.org/core/volume"442"xsd:string
http://purl.uniprot.org/citations/11680614http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11680614
http://purl.uniprot.org/citations/11680614http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11680614
http://purl.uniprot.org/citations/11680614http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11680614
http://purl.uniprot.org/citations/11680614http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11680614