PubMed:10521544 JSONTXT

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":438,"end":445},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":599,"end":606},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":993,"end":1000},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlyCosmos600-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":438,"end":445},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":599,"end":606},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":993,"end":1000},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlyCosmos600-CLO","denotations":[{"id":"T1","span":{"begin":1361,"end":1366},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":438,"end":445},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":599,"end":606},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":993,"end":1000},"obj":"Glycan_Motif"}],"attributes":[{"id":"A1","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A2","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"},{"id":"A3","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

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{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":438,"end":445},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":599,"end":606},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":993,"end":1000},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":873,"end":897},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC297"},{"id":"_T2","span":{"begin":873,"end":901},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC776"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

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The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T2","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T3","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T4","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T5","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/O60476"},{"id":"T6","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T7","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T8","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T9","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T10","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/Q9UKM7"},{"id":"T11","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T12","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T13","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T14","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T15","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/Q9BZQ6"},{"id":"T16","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T17","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T18","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T19","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T20","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/Q5SRI9"},{"id":"T21","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T22","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T23","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T24","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T25","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/Q9NR34"},{"id":"T26","span":{"begin":43,"end":64},"obj":"http://www.uniprot.org/uniprot/P33908"},{"id":"T27","span":{"begin":713,"end":734},"obj":"http://www.uniprot.org/uniprot/P33908"},{"id":"T28","span":{"begin":781,"end":802},"obj":"http://www.uniprot.org/uniprot/P33908"},{"id":"T29","span":{"begin":846,"end":867},"obj":"http://www.uniprot.org/uniprot/P33908"},{"id":"T30","span":{"begin":1185,"end":1206},"obj":"http://www.uniprot.org/uniprot/P33908"},{"id":"T31","span":{"begin":824,"end":851},"obj":"http://www.uniprot.org/uniprot/Q96HE7"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"FSU-PRGE","denotations":[{"id":"T1","span":{"begin":43,"end":64},"obj":"protein"},{"id":"T2","span":{"begin":275,"end":305},"obj":"protein"},{"id":"T3","span":{"begin":713,"end":734},"obj":"protein"},{"id":"T4","span":{"begin":781,"end":802},"obj":"protein"},{"id":"T5","span":{"begin":846,"end":867},"obj":"protein"},{"id":"T6","span":{"begin":947,"end":969},"obj":"protein"},{"id":"T7","span":{"begin":1185,"end":1206},"obj":"protein"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":241,"end":260},"obj":"http://purl.bioontology.org/ontology/STY/T087"},{"id":"T2","span":{"begin":381,"end":387},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/1365831"},{"id":"T3","span":{"begin":873,"end":886},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4895"},{"id":"T4","span":{"begin":873,"end":886},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4930"},{"id":"T5","span":{"begin":873,"end":886},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/36034"},{"id":"T6","span":{"begin":873,"end":886},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/4891"},{"id":"T7","span":{"begin":1100,"end":1107},"obj":"http://purl.bioontology.org/ontology/STY/T024"},{"id":"T8","span":{"begin":1361,"end":1366},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":43,"end":64},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T2","span":{"begin":43,"end":64},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T3","span":{"begin":713,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T4","span":{"begin":713,"end":734},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T5","span":{"begin":781,"end":802},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T6","span":{"begin":781,"end":802},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T7","span":{"begin":846,"end":867},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T8","span":{"begin":846,"end":867},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T9","span":{"begin":283,"end":305},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T10","span":{"begin":283,"end":305},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T11","span":{"begin":947,"end":969},"obj":"http://purl.obolibrary.org/obo/GO_0004559"},{"id":"T12","span":{"begin":947,"end":969},"obj":"http://purl.obolibrary.org/obo/GO_0004571"},{"id":"T13","span":{"begin":119,"end":140},"obj":"http://purl.obolibrary.org/obo/GO_0006487"},{"id":"T14","span":{"begin":121,"end":140},"obj":"http://purl.obolibrary.org/obo/GO_0000271"},{"id":"T15","span":{"begin":128,"end":140},"obj":"http://purl.obolibrary.org/obo/GO_0009058"},{"id":"T16","span":{"begin":361,"end":369},"obj":"http://purl.obolibrary.org/obo/GO_0046903"},{"id":"T17","span":{"begin":361,"end":377},"obj":"http://purl.obolibrary.org/obo/GO_0009306"},{"id":"T18","span":{"begin":632,"end":647},"obj":"http://purl.obolibrary.org/obo/GO_0003824"},{"id":"T19","span":{"begin":1152,"end":1162},"obj":"http://purl.obolibrary.org/obo/GO_0006351"},{"id":"T20","span":{"begin":1361,"end":1379},"obj":"http://purl.obolibrary.org/obo/GO_0098657"},{"id":"T21","span":{"begin":1400,"end":1429},"obj":"http://purl.obolibrary.org/obo/GO_0006516"},{"id":"T22","span":{"begin":1418,"end":1429},"obj":"http://purl.obolibrary.org/obo/GO_0009056"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":207,"end":215},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T2","span":{"begin":824,"end":845},"obj":"http://purl.obolibrary.org/obo/GO_0005783"},{"id":"T3","span":{"begin":941,"end":946},"obj":"http://purl.obolibrary.org/obo/GO_0005794"},{"id":"T4","span":{"begin":1361,"end":1366},"obj":"http://purl.obolibrary.org/obo/GO_0005623"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"UBERON-AE","denotations":[{"id":"T1","span":{"begin":576,"end":579},"obj":"http://purl.obolibrary.org/obo/UBERON_0001460"},{"id":"T2","span":{"begin":1100,"end":1107},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":37,"end":42},"obj":"http://edamontology.org/topic_2815"},{"id":"T2","span":{"begin":177,"end":182},"obj":"http://edamontology.org/topic_2815"},{"id":"T3","span":{"begin":183,"end":187},"obj":"http://edamontology.org/topic_3512"},{"id":"T4","span":{"begin":207,"end":223},"obj":"http://edamontology.org/topic_0820"},{"id":"T5","span":{"begin":216,"end":223},"obj":"http://edamontology.org/topic_0078"},{"id":"T6","span":{"begin":241,"end":251},"obj":"http://edamontology.org/topic_0154"},{"id":"T7","span":{"begin":252,"end":260},"obj":"http://edamontology.org/topic_0080"},{"id":"T8","span":{"begin":252,"end":260},"obj":"http://edamontology.org/topic_3168"},{"id":"T9","span":{"begin":370,"end":377},"obj":"http://edamontology.org/topic_0078"},{"id":"T10","span":{"begin":479,"end":482},"obj":"http://edamontology.org/topic_0593"},{"id":"T11","span":{"begin":580,"end":588},"obj":"http://edamontology.org/topic_0749"},{"id":"T12","span":{"begin":707,"end":712},"obj":"http://edamontology.org/topic_2815"},{"id":"T13","span":{"begin":775,"end":780},"obj":"http://edamontology.org/topic_2815"},{"id":"T14","span":{"begin":824,"end":845},"obj":"http://edamontology.org/topic_0616"},{"id":"T15","span":{"begin":1094,"end":1099},"obj":"http://edamontology.org/topic_2815"},{"id":"T16","span":{"begin":1152,"end":1162},"obj":"http://edamontology.org/topic_3308"},{"id":"T17","span":{"begin":1152,"end":1162},"obj":"http://edamontology.org/topic_0110"},{"id":"T18","span":{"begin":1152,"end":1162},"obj":"http://edamontology.org/topic_0203"},{"id":"T19","span":{"begin":1152,"end":1162},"obj":"http://edamontology.org/topic_3512"},{"id":"T20","span":{"begin":1355,"end":1360},"obj":"http://edamontology.org/topic_2817"},{"id":"T21","span":{"begin":1355,"end":1360},"obj":"http://edamontology.org/topic_0782"},{"id":"T22","span":{"begin":1383,"end":1389},"obj":"http://edamontology.org/topic_0154"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

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and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"glycosmos-test-glycan-structure","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":438,"end":445},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":599,"end":606},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":993,"end":1000},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"glycosmos-test-structure-v1","denotations":[{"id":"PD-GlycanStructures-B_T1","span":{"begin":438,"end":445},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T2","span":{"begin":599,"end":606},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"},{"id":"PD-GlycanStructures-B_T3","span":{"begin":993,"end":1000},"obj":"http://rdf.glyconavi.org/CarTNa/CarTNa218/trivialname"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlyCosmos600-GlycoProteins","denotations":[{"id":"PD-GlycoProteins-B_T1","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T2","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T3","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T4","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T5","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T6","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T7","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000585"},{"id":"PD-GlycoProteins-B_T8","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T9","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T10","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T11","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T12","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T13","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T14","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000648"},{"id":"PD-GlycoProteins-B_T15","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T16","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T17","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T18","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T19","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T20","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T21","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0000773"},{"id":"PD-GlycoProteins-B_T22","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T23","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T24","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T25","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T26","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T27","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T28","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001141"},{"id":"PD-GlycoProteins-B_T29","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T30","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T31","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T32","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T33","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T34","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T35","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0001144"},{"id":"PD-GlycoProteins-B_T36","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T37","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T38","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T39","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T40","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T41","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T42","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002027"},{"id":"PD-GlycoProteins-B_T43","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T44","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T45","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T46","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T47","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T48","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T49","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0002028"},{"id":"PD-GlycoProteins-B_T50","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T51","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T52","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T53","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T54","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T55","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T56","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0004660"},{"id":"PD-GlycoProteins-B_T57","span":{"begin":43,"end":64},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T58","span":{"begin":283,"end":305},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T59","span":{"begin":713,"end":734},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T60","span":{"begin":781,"end":802},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T61","span":{"begin":846,"end":867},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T62","span":{"begin":947,"end":969},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"},{"id":"PD-GlycoProteins-B_T63","span":{"begin":1185,"end":1206},"obj":"https://acgg.asia/db/gpdb/id/GPDB0005222"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":119,"end":127},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"},{"id":"T2","span":{"begin":1034,"end":1042},"obj":"http://rdf.glycoinfo.org/glycan/G00027MO"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"GlyTouCan-IUPAC","denotations":[{"id":"GlycanIUPAC_T1","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G41652MJ\""},{"id":"GlycanIUPAC_T2","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G20761YC\""},{"id":"GlycanIUPAC_T3","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G19807HM\""},{"id":"GlycanIUPAC_T4","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G20351TE\""},{"id":"GlycanIUPAC_T5","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G71957MR\""},{"id":"GlycanIUPAC_T6","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G59040AE\""},{"id":"GlycanIUPAC_T7","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G14987PW\""},{"id":"GlycanIUPAC_T8","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G95064PC\""},{"id":"GlycanIUPAC_T9","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G39143AQ\""},{"id":"GlycanIUPAC_T10","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G65149OO\""},{"id":"GlycanIUPAC_T11","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G02766SY\""},{"id":"GlycanIUPAC_T12","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G26019KJ\""},{"id":"GlycanIUPAC_T13","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G36429CZ\""},{"id":"GlycanIUPAC_T14","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G89633TP\""},{"id":"GlycanIUPAC_T15","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G28494FO\""},{"id":"GlycanIUPAC_T16","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G06219CP\""},{"id":"GlycanIUPAC_T17","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G44237SM\""},{"id":"GlycanIUPAC_T18","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G57948RL\""},{"id":"GlycanIUPAC_T19","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G64016DN\""},{"id":"GlycanIUPAC_T20","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G14536PC\""},{"id":"GlycanIUPAC_T21","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G14356FW\""},{"id":"GlycanIUPAC_T22","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G34565UO\""},{"id":"GlycanIUPAC_T23","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G67124MW\""},{"id":"GlycanIUPAC_T24","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G71457ZU\""},{"id":"GlycanIUPAC_T25","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G55228VZ\""},{"id":"GlycanIUPAC_T26","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G31034MJ\""},{"id":"GlycanIUPAC_T27","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G25776IP\""},{"id":"GlycanIUPAC_T28","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G64442BV\""},{"id":"GlycanIUPAC_T29","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G57018LE\""},{"id":"GlycanIUPAC_T30","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G61761GX\""},{"id":"GlycanIUPAC_T31","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G76318UX\""},{"id":"GlycanIUPAC_T32","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G61906ER\""},{"id":"GlycanIUPAC_T33","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G68723GR\""},{"id":"GlycanIUPAC_T34","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G19540LE\""},{"id":"GlycanIUPAC_T35","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G74944PO\""},{"id":"GlycanIUPAC_T36","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G89489ZJ\""},{"id":"GlycanIUPAC_T37","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G04434YU\""},{"id":"GlycanIUPAC_T38","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G21450PB\""},{"id":"GlycanIUPAC_T39","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G93629QY\""},{"id":"GlycanIUPAC_T40","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G02603TR\""},{"id":"GlycanIUPAC_T41","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G40280JP\""},{"id":"GlycanIUPAC_T42","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G95259IC\""},{"id":"GlycanIUPAC_T43","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G26900FE\""},{"id":"GlycanIUPAC_T44","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G21346KK\""},{"id":"GlycanIUPAC_T45","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G62509FF\""},{"id":"GlycanIUPAC_T46","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G83932AK\""},{"id":"GlycanIUPAC_T47","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G96978IB\""},{"id":"GlycanIUPAC_T48","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G34275DN\""},{"id":"GlycanIUPAC_T49","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G07071JF\""},{"id":"GlycanIUPAC_T50","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G80639QD\""},{"id":"GlycanIUPAC_T51","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G99460PJ\""},{"id":"GlycanIUPAC_T52","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G22024BZ\""},{"id":"GlycanIUPAC_T53","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G74097ZY\""},{"id":"GlycanIUPAC_T54","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G84439YP\""},{"id":"GlycanIUPAC_T55","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G52207WQ\""},{"id":"GlycanIUPAC_T56","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G90695MS\""},{"id":"GlycanIUPAC_T57","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G50398QX\""},{"id":"GlycanIUPAC_T58","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G12166ZT\""},{"id":"GlycanIUPAC_T59","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G48368BR\""},{"id":"GlycanIUPAC_T60","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G57407RW\""},{"id":"GlycanIUPAC_T61","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G00386TY\""},{"id":"GlycanIUPAC_T62","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G18723JK\""},{"id":"GlycanIUPAC_T63","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G93757OR\""},{"id":"GlycanIUPAC_T64","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G29006SI\""},{"id":"GlycanIUPAC_T65","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G03099OQ\""},{"id":"GlycanIUPAC_T66","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G53739OW\""},{"id":"GlycanIUPAC_T67","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G70440ZO\""},{"id":"GlycanIUPAC_T68","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G29951RR\""},{"id":"GlycanIUPAC_T69","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G58402TI\""},{"id":"GlycanIUPAC_T70","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G39875TP\""},{"id":"GlycanIUPAC_T71","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G83439QV\""},{"id":"GlycanIUPAC_T72","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G41762RC\""},{"id":"GlycanIUPAC_T73","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G91604UI\""},{"id":"GlycanIUPAC_T74","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G88447WE\""},{"id":"GlycanIUPAC_T75","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G93634BS\""},{"id":"GlycanIUPAC_T76","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G02587BH\""},{"id":"GlycanIUPAC_T77","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G43511MX\""},{"id":"GlycanIUPAC_T78","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G64958DH\""},{"id":"GlycanIUPAC_T79","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G30384TR\""},{"id":"GlycanIUPAC_T80","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G15624EX\""},{"id":"GlycanIUPAC_T81","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G22706ST\""},{"id":"GlycanIUPAC_T82","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G57408PI\""},{"id":"GlycanIUPAC_T83","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G86403XX\""},{"id":"GlycanIUPAC_T84","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G78043YB\""},{"id":"GlycanIUPAC_T85","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G18952JK\""},{"id":"GlycanIUPAC_T86","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G49020ND\""},{"id":"GlycanIUPAC_T87","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G63590YW\""},{"id":"GlycanIUPAC_T88","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G22793KS\""},{"id":"GlycanIUPAC_T89","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G64134SS\""},{"id":"GlycanIUPAC_T90","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G17338HY\""},{"id":"GlycanIUPAC_T91","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G99745XF\""},{"id":"GlycanIUPAC_T92","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G27782HN\""},{"id":"GlycanIUPAC_T93","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G57496DC\""},{"id":"GlycanIUPAC_T94","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G93169WB\""},{"id":"GlycanIUPAC_T95","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G05518TD\""},{"id":"GlycanIUPAC_T96","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G62603DN\""},{"id":"GlycanIUPAC_T97","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G59574FS\""},{"id":"GlycanIUPAC_T98","span":{"begin":1090,"end":1093},"obj":"\"http://rdf.glycoinfo.org/glycan/G47567WC\""}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"performance-test","denotations":[{"id":"PD-UBERON-AE-B_T1","span":{"begin":576,"end":579},"obj":"http://purl.obolibrary.org/obo/UBERON_0001460"},{"id":"PD-UBERON-AE-B_T2","span":{"begin":1100,"end":1107},"obj":"http://purl.obolibrary.org/obo/UBERON_0000479"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":37,"end":42},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":177,"end":182},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":381,"end":396},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":707,"end":712},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":775,"end":780},"obj":"OrganismTaxon"},{"id":"T6","span":{"begin":873,"end":897},"obj":"OrganismTaxon"},{"id":"T7","span":{"begin":1094,"end":1099},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"9606"},{"id":"A2","pred":"db_id","subj":"T2","obj":"9606"},{"id":"A3","pred":"db_id","subj":"T3","obj":"4922"},{"id":"A4","pred":"db_id","subj":"T4","obj":"9606"},{"id":"A5","pred":"db_id","subj":"T5","obj":"9606"},{"id":"A6","pred":"db_id","subj":"T6","obj":"4932"},{"id":"A7","pred":"db_id","subj":"T7","obj":"9606"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":207,"end":215},"obj":"Body_part"},{"id":"T4","span":{"begin":576,"end":579},"obj":"Body_part"},{"id":"T6","span":{"begin":836,"end":845},"obj":"Body_part"},{"id":"T7","span":{"begin":941,"end":946},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"A2","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A3","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A4","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0001460"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0003822"},{"id":"A6","pred":"uberon_id","subj":"T6","obj":"http://purl.obolibrary.org/obo/UBERON_0007361"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/GO_0005794"}],"text":"Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis.\nWe report the isolation of a novel human cDNA encoding a type II membrane protein of 79.5 kDa with amino acid sequence similarity to Class I alpha 1,2-mannosidases. The catalytic domain of the enzyme was expressed as a secreted protein in Pichia pastoris. The recombinant enzyme removes a single mannose residue from Man9GlcNAc and [1H]-NMR analysis indicates that the only product is Man8GlcNAc isomer B, the form lacking the middle-arm terminal alpha 1,2-mannose. Calcium is required for enzyme activity and both 1-deoxymannojirimycin and kifunensine inhibit the human alpha 1,2-mannosidase. The properties and specificity of this human alpha 1,2-mannosidase are identical to the endoplasmic reticulum alpha 1,2-mannosidase from Saccharomyces cerevisiae and differ from those of previously cloned Golgi alpha 1,2-mannosidases that remove up to four mannose residues from Man9GlcNAc2 during N-glycan maturation. Northern blot analysis showed that all human tissues examined express variable amounts of a 3 kb transcript. This highly specific alpha 1,2-mannosidase is likely to be involved in glycoprotein quality control since there is increasing evidence that trimming of Man9GlcNAc2 to Man8GlcNAc2 isomer B in yeast cells is important to target misfolded glycoproteins for degradation."}