| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/2000/01/rdf-schema#comment | "A human cDNA encoding a 70.9-kDa type II membrane protein with sequence similarity to class I alpha1,2-mannosidases was isolated. The enzymatic properties of the novel alpha1,2-mannosidase IC were studied by expressing its catalytic domain in Pichia pastoris as a secreted glycoprotein. alpha1,2-Mannosidase IC sequentially hydrolyzes the alpha1,2-linked mannose residues of [(3)H]mannose-labeled Man(9)GlcNAc to form [(3)H]Man(6)GlcNAc and a small amount of [(3)H]Man(5)GlcNAc. The enzyme requires calcium for activity and is inhibited by both 1-deoxymannojirimycin and kifunensine. The order of mannose removal was determined by separating oligosaccharide isomers formed from pyridylaminated Man(9)GlcNAc(2) by high performance liquid chromatography. The terminal alpha1,2-linked mannose residue from the middle branch is the last mannose removed by the enzyme. This residue is the mannose cleaved from Man(9)GlcNAc(2) by the endoplasmic reticulum alpha1, 2-mannosidase I to form Man(8)GlcNAc(2) isomer B. The order of mannose hydrolysis from either pyridylaminated Man(9)GlcNAc(2) or Man(8)GlcNAc(2) isomer B differs from that previously reported for mammalian Golgi alpha1,2-mannosidases IA and IB. The full-length alpha1,2-mannosidase IC was localized to the Golgi of MDBK and MDCK cells by indirect immunofluorescence. Northern blot analysis showed tissue-specific expression of a major transcript of 3.8 kilobase pairs. The expression pattern is different from that of human Golgi alpha1,2-mannosidases IA and IB. Therefore, the human genome contains at least three differentially regulated Golgi alpha1, 2-mannosidase genes encoding enzymes with similar, but not identical specificities."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m004935200"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m004935200"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/author | "Herscovics A."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/author | "Herscovics A."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/author | "Tremblay L.O."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/author | "Tremblay L.O."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/pages | "31655-31660"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/pages | "31655-31660"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/title | "Characterization of a cDNA encoding a novel human Golgi alpha 1,2-mannosidase involved in N-glycan biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/title | "Characterization of a cDNA encoding a novel human Golgi alpha 1,2-mannosidase involved in N-glycan biosynthesis."xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://purl.uniprot.org/core/volume | "275"xsd:string |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10915796 |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10915796 |
| http://purl.uniprot.org/citations/10915796 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10915796 |
| http://purl.uniprot.org/citations/10915796 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10915796 |
| http://purl.uniprot.org/citations/10915796 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/10915796 |