http://purl.uniprot.org/citations/29374258 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29374258 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/29374258 | http://www.w3.org/2000/01/rdf-schema#comment | "Many eukaryotic proteins are anchored to the cell surface via the glycolipid glycosylphosphatidylinositol (GPI). Mammalian GPIs have a conserved core but exhibit diverse N-acetylgalactosamine (GalNAc) modifications, which are added via a yet unresolved process. Here we identify the Golgi-resident GPI-GalNAc transferase PGAP4 and show by mass spectrometry that PGAP4 knockout cells lose GPI-GalNAc structures. Furthermore, we demonstrate that PGAP4, in contrast to known Golgi glycosyltransferases, is not a single-pass membrane protein but contains three transmembrane domains, including a tandem transmembrane domain insertion into its glycosyltransferase-A fold as indicated by comparative modeling. Mutational analysis reveals a catalytic site, a DXD-like motif for UDP-GalNAc donor binding, and several residues potentially involved in acceptor binding. We suggest that a juxtamembrane region of PGAP4 accommodates various GPI-anchored proteins, presenting their acceptor residue toward the catalytic center. In summary, we present insights into the structure of PGAP4 and elucidate the initial step of GPI-GalNAc biosynthesis."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-017-02799-0"xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.org/dc/terms/identifier | "doi:10.1038/s41467-017-02799-0"xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Fujita M."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Fujita M."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Nakamura S."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Nakamura S."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Murakami Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Murakami Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Maeda Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Maeda Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Saito K."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Saito K."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Takada Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Takada Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Kinoshita T."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Kinoshita T."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Yamaguchi Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Yamaguchi Y."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Mishra S.K."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Mishra S.K."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Hirata T."xsd:string |
http://purl.uniprot.org/citations/29374258 | http://purl.uniprot.org/core/author | "Hirata T."xsd:string |