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http://purl.uniprot.org/citations/9525933http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9525933http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9525933http://www.w3.org/2000/01/rdf-schema#comment"The initiation of mucin-type O-glycosylation is catalyzed by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases (ppGaNTase) (EC 2.4.1.41). By screening two mixed-stage Caenorhabditis elegans cDNA libraries, a total of 11 distinct sequence homologs of the ppGaNTase gene family were cloned, sequenced, and expressed as truncated recombinant proteins (gly-3, gly-4, gly-5a, gly-5b, gly-5c, gly-6a, gly-6b, gly-6c, gly-7, gly-8, and gly-9). All clones encoded type II membrane proteins that shared 60-80% amino acid sequence similarity with the catalytic domain of mammalian ppGaNTase enzymes. Two sets of cDNA clones (gly-5 and gly-6) contained variants that appeared to be produced by alternative message processing. gly-6c contained a reading frameshift and premature termination codon in the C-terminal lectin-like domain found in most other ppGaNTase proteins, and a second clone (gly-8) lacked the typical C-terminal region completely. Homogenates of nematodes and immunopurified preparations of the recombinant GLY proteins demonstrated that worms express functional ppGaNTase enzymes (GLY-3, GLY-4, GLY-5A, GLY-5B, and GLY-5C), which can O-glycosylate mammalian apomucin peptide sequences in vitro. In addition to demonstrating the existence of ppGaNTase enzymes in a nematode organism, the substantial diversity of these isoforms in C. elegans suggests that mucin O-glycosylation is catalyzed by a complex gene family, which is conserved among evolutionary-distinct organisms."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.14.8268"xsd:string
http://purl.uniprot.org/citations/9525933http://purl.org/dc/terms/identifier"doi:10.1074/jbc.273.14.8268"xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/author"Nehrke K."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/author"Nehrke K."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/author"Hagen F.K."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/author"Hagen F.K."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/pages"8268-8277"xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/pages"8268-8277"xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/title"cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/title"cDNA cloning and expression of a family of UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase sequence homologs from Caenorhabditis elegans."xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9525933http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/9525933http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9525933
http://purl.uniprot.org/citations/9525933http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/9525933
http://purl.uniprot.org/citations/9525933http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9525933
http://purl.uniprot.org/citations/9525933http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/9525933
http://purl.uniprot.org/uniprot/Q8I136http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9525933
http://purl.uniprot.org/embl-cds/AAC13672.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/9525933