PubMed:10406849 JSON TXT

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Glycan-Motif

{"project":"Glycan-Motif","denotations":[{"id":"T1","span":{"begin":60,"end":67},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":673,"end":680},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":798,"end":805},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":1324,"end":1331},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlyCosmos6-Glycan-Motif-Image

{"project":"GlyCosmos6-Glycan-Motif-Image","denotations":[{"id":"T1","span":{"begin":60,"end":67},"obj":"Glycan_Motif"},{"id":"T2","span":{"begin":673,"end":680},"obj":"Glycan_Motif"},{"id":"T3","span":{"begin":798,"end":805},"obj":"Glycan_Motif"},{"id":"T4","span":{"begin":1324,"end":1331},"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"},{"id":"A4","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/0.10.0/png/binary/G70323CJ"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlyCosmos6-Glycan-Motif-Structure

{"project":"GlyCosmos6-Glycan-Motif-Structure","denotations":[{"id":"T1","span":{"begin":60,"end":67},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T2","span":{"begin":673,"end":680},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T3","span":{"begin":798,"end":805},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"},{"id":"T4","span":{"begin":1324,"end":1331},"obj":"https://glytoucan.org/Structures/Glycans/G70323CJ"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":315,"end":321},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlycoBiology-FMA

uniprot-human

{"project":"uniprot-human","denotations":[{"id":"T1","span":{"begin":37,"end":42},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T2","span":{"begin":184,"end":189},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T3","span":{"begin":472,"end":477},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T4","span":{"begin":519,"end":524},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T5","span":{"begin":618,"end":623},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T6","span":{"begin":651,"end":656},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T7","span":{"begin":1236,"end":1241},"obj":"http://www.uniprot.org/uniprot/Q12907"},{"id":"T8","span":{"begin":409,"end":417},"obj":"http://www.uniprot.org/uniprot/Q9UQG6"},{"id":"T9","span":{"begin":584,"end":595},"obj":"http://www.uniprot.org/uniprot/Q99484"},{"id":"T10","span":{"begin":1078,"end":1091},"obj":"http://www.uniprot.org/uniprot/Q9UNY3"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":37,"end":42},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T2","span":{"begin":184,"end":189},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T3","span":{"begin":472,"end":477},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T4","span":{"begin":519,"end":524},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T5","span":{"begin":618,"end":623},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T6","span":{"begin":651,"end":656},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T7","span":{"begin":1236,"end":1241},"obj":"http://www.uniprot.org/uniprot/Q9DBH5"},{"id":"T8","span":{"begin":315,"end":321},"obj":"http://www.uniprot.org/uniprot/P28352"},{"id":"T9","span":{"begin":409,"end":417},"obj":"http://www.uniprot.org/uniprot/Q9D0F3"},{"id":"T10","span":{"begin":584,"end":595},"obj":"http://www.uniprot.org/uniprot/P38649"},{"id":"T11","span":{"begin":716,"end":719},"obj":"http://www.uniprot.org/uniprot/A2APV2"},{"id":"T12","span":{"begin":958,"end":961},"obj":"http://www.uniprot.org/uniprot/A2APV2"},{"id":"T13","span":{"begin":1049,"end":1052},"obj":"http://www.uniprot.org/uniprot/A2APV2"},{"id":"T14","span":{"begin":1367,"end":1370},"obj":"http://www.uniprot.org/uniprot/A2APV2"},{"id":"T15","span":{"begin":984,"end":987},"obj":"http://www.uniprot.org/uniprot/Q61024"},{"id":"T16","span":{"begin":1078,"end":1091},"obj":"http://www.uniprot.org/uniprot/O08710"},{"id":"T17","span":{"begin":1129,"end":1133},"obj":"http://www.uniprot.org/uniprot/P17717"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlycoBiology-NCBITAXON

{"project":"GlycoBiology-NCBITAXON","denotations":[{"id":"T1","span":{"begin":0,"end":9},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/246680"},{"id":"T2","span":{"begin":129,"end":134},"obj":"http://purl.bioontology.org/ontology/STY/T025"},{"id":"T3","span":{"begin":147,"end":156},"obj":"http://purl.bioontology.org/ontology/NCBITAXON/246680"},{"id":"T4","span":{"begin":230,"end":235},"obj":"http://purl.bioontology.org/ontology/STY/T025"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":136,"end":418},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":419,"end":632},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":633,"end":768},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":769,"end":896},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":897,"end":977},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":978,"end":983},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":984,"end":1015},"obj":"Sentence"},{"id":"TextSentencer_T9","span":{"begin":1016,"end":1207},"obj":"Sentence"},{"id":"TextSentencer_T10","span":{"begin":1208,"end":1374},"obj":"Sentence"},{"id":"TextSentencer_T11","span":{"begin":1375,"end":1385},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"T2","span":{"begin":136,"end":418},"obj":"Sentence"},{"id":"T3","span":{"begin":419,"end":632},"obj":"Sentence"},{"id":"T4","span":{"begin":633,"end":768},"obj":"Sentence"},{"id":"T5","span":{"begin":769,"end":977},"obj":"Sentence"},{"id":"T6","span":{"begin":978,"end":1207},"obj":"Sentence"},{"id":"T7","span":{"begin":1208,"end":1374},"obj":"Sentence"},{"id":"T8","span":{"begin":1375,"end":1385},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"T2","span":{"begin":136,"end":418},"obj":"Sentence"},{"id":"T3","span":{"begin":419,"end":632},"obj":"Sentence"},{"id":"T4","span":{"begin":633,"end":768},"obj":"Sentence"},{"id":"T5","span":{"begin":769,"end":896},"obj":"Sentence"},{"id":"T6","span":{"begin":897,"end":977},"obj":"Sentence"},{"id":"T7","span":{"begin":978,"end":983},"obj":"Sentence"},{"id":"T8","span":{"begin":984,"end":1015},"obj":"Sentence"},{"id":"T9","span":{"begin":1016,"end":1207},"obj":"Sentence"},{"id":"T10","span":{"begin":1208,"end":1374},"obj":"Sentence"},{"id":"T11","span":{"begin":1375,"end":1385},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":103,"end":111},"obj":"http://purl.obolibrary.org/obo/GO_0097502"},{"id":"T2","span":{"begin":838,"end":840},"obj":"http://purl.obolibrary.org/obo/GO_0033968"},{"id":"T3","span":{"begin":929,"end":954},"obj":"http://purl.obolibrary.org/obo/GO_0051100"},{"id":"T4","span":{"begin":980,"end":982},"obj":"http://purl.obolibrary.org/obo/GO_0003987"},{"id":"T5","span":{"begin":980,"end":982},"obj":"http://purl.obolibrary.org/obo/GO_0043884"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GO-MF

{"project":"GO-MF","denotations":[{"id":"T1","span":{"begin":483,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0030246"},{"id":"T2","span":{"begin":496,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T3","span":{"begin":773,"end":780},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T4","span":{"begin":947,"end":954},"obj":"http://purl.obolibrary.org/obo/GO_0070026"},{"id":"T5","span":{"begin":496,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T6","span":{"begin":773,"end":780},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T7","span":{"begin":947,"end":954},"obj":"http://purl.obolibrary.org/obo/GO_0003680"},{"id":"T8","span":{"begin":496,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T9","span":{"begin":773,"end":780},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T10","span":{"begin":947,"end":954},"obj":"http://purl.obolibrary.org/obo/GO_0017091"},{"id":"T11","span":{"begin":496,"end":503},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T12","span":{"begin":773,"end":780},"obj":"http://purl.obolibrary.org/obo/GO_0005488"},{"id":"T13","span":{"begin":947,"end":954},"obj":"http://purl.obolibrary.org/obo/GO_0005488"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":10,"end":27},"obj":"http://purl.obolibrary.org/obo/GO_0016021"},{"id":"T2","span":{"begin":157,"end":174},"obj":"http://purl.obolibrary.org/obo/GO_0016021"},{"id":"T3","span":{"begin":10,"end":35},"obj":"http://purl.obolibrary.org/obo/GO_0097631"},{"id":"T4","span":{"begin":157,"end":182},"obj":"http://purl.obolibrary.org/obo/GO_0097631"},{"id":"T5","span":{"begin":10,"end":35},"obj":"http://purl.obolibrary.org/obo/GO_0030173"},{"id":"T6","span":{"begin":157,"end":182},"obj":"http://purl.obolibrary.org/obo/GO_0030173"},{"id":"T7","span":{"begin":10,"end":35},"obj":"http://purl.obolibrary.org/obo/GO_0030176"},{"id":"T8","span":{"begin":157,"end":182},"obj":"http://purl.obolibrary.org/obo/GO_0030176"},{"id":"T9","span":{"begin":19,"end":27},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T10","span":{"begin":166,"end":174},"obj":"http://purl.obolibrary.org/obo/GO_0016020"},{"id":"T11","span":{"begin":129,"end":134},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T12","span":{"begin":230,"end":235},"obj":"http://purl.obolibrary.org/obo/GO_0005623"},{"id":"T13","span":{"begin":409,"end":414},"obj":"http://purl.obolibrary.org/obo/GO_0005793"},{"id":"T14","span":{"begin":1258,"end":1271},"obj":"http://purl.obolibrary.org/obo/GO_0005622"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

EDAM-topics

{"project":"EDAM-topics","denotations":[{"id":"T1","span":{"begin":19,"end":35},"obj":"http://edamontology.org/topic_0820"},{"id":"T2","span":{"begin":28,"end":35},"obj":"http://edamontology.org/topic_0078"},{"id":"T3","span":{"begin":166,"end":182},"obj":"http://edamontology.org/topic_0820"},{"id":"T4","span":{"begin":175,"end":182},"obj":"http://edamontology.org/topic_0078"},{"id":"T5","span":{"begin":329,"end":337},"obj":"http://edamontology.org/topic_0078"},{"id":"T6","span":{"begin":391,"end":396},"obj":"http://edamontology.org/topic_0780"},{"id":"T7","span":{"begin":483,"end":495},"obj":"http://edamontology.org/topic_0152"},{"id":"T8","span":{"begin":557,"end":564},"obj":"http://edamontology.org/topic_0078"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

EDAM-DFO

{"project":"EDAM-DFO","denotations":[{"id":"T1","span":{"begin":28,"end":35},"obj":"http://edamontology.org/format_1208"},{"id":"T2","span":{"begin":28,"end":35},"obj":"http://edamontology.org/data_1467"},{"id":"T3","span":{"begin":112,"end":120},"obj":"http://edamontology.org/data_1756"},{"id":"T4","span":{"begin":175,"end":182},"obj":"http://edamontology.org/data_1467"},{"id":"T5","span":{"begin":175,"end":182},"obj":"http://edamontology.org/format_1208"},{"id":"T6","span":{"begin":329,"end":337},"obj":"http://edamontology.org/format_1208"},{"id":"T7","span":{"begin":329,"end":337},"obj":"http://edamontology.org/data_1467"},{"id":"T8","span":{"begin":437,"end":448},"obj":"http://edamontology.org/data_2576"},{"id":"T9","span":{"begin":437,"end":448},"obj":"http://edamontology.org/data_0977"},{"id":"T10","span":{"begin":440,"end":448},"obj":"http://edamontology.org/data_2611"},{"id":"T11","span":{"begin":440,"end":448},"obj":"http://edamontology.org/data_0842"},{"id":"T12","span":{"begin":557,"end":564},"obj":"http://edamontology.org/data_1467"},{"id":"T13","span":{"begin":557,"end":564},"obj":"http://edamontology.org/format_1208"},{"id":"T14","span":{"begin":720,"end":728},"obj":"http://edamontology.org/data_1756"},{"id":"T15","span":{"begin":873,"end":875},"obj":"http://edamontology.org/format_1997"},{"id":"T16","span":{"begin":901,"end":914},"obj":"http://edamontology.org/data_2140"},{"id":"T17","span":{"begin":1242,"end":1251},"obj":"http://edamontology.org/operation_0004"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

NGLY1-deficiency

{"project":"NGLY1-deficiency","denotations":[{"id":"PD-NGLY1-deficiency-B_T1","span":{"begin":967,"end":973},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T2","span":{"begin":1058,"end":1064},"obj":"chem:24139"},{"id":"PD-NGLY1-deficiency-B_T3","span":{"begin":1375,"end":1381},"obj":"chem:24139"}],"namespaces":[{"prefix":"hgnc","uri":"https://www.genenames.org/data/gene-symbol-report/#!/hgnc_id/HGNC:"},{"prefix":"omim","uri":"https://www.omim.org/entry/"},{"prefix":"chem","uri":"https://pubchem.ncbi.nlm.nih.gov/compound/"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":315,"end":321},"obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlycoBiology-Motifs

{"project":"GlycoBiology-Motifs","denotations":[{"id":"T1","span":{"begin":55,"end":67},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"},{"id":"T2","span":{"begin":668,"end":680},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"},{"id":"T3","span":{"begin":793,"end":805},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"},{"id":"T4","span":{"begin":1319,"end":1331},"obj":"http://rdf.glycoinfo.org/glycan/G00028MO"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

Lectin

{"project":"Lectin","denotations":[{"id":"Lectin_T1","span":{"begin":716,"end":719},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T2","span":{"begin":958,"end":961},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T3","span":{"begin":1049,"end":1052},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T4","span":{"begin":1367,"end":1370},"obj":"https://acgg.asia/db/lfdb/LfDB0217"},{"id":"Lectin_T5","span":{"begin":838,"end":840},"obj":"https://acgg.asia/db/lfdb/LfDB0227"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

GlyTouCan-IUPAC

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":315,"end":321},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000484"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

Lectin-Jamboree

{"project":"Lectin-Jamboree","denotations":[{"id":"T1","span":{"begin":397,"end":404},"obj":"lectin"},{"id":"T2","span":{"begin":1272,"end":1278},"obj":"lectin"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

Lectin-Jamboree-Sentence

{"project":"Lectin-Jamboree-Sentence","blocks":[{"id":"T1","span":{"begin":0,"end":135},"obj":"Sentence"},{"id":"T2","span":{"begin":136,"end":418},"obj":"Sentence"},{"id":"T3","span":{"begin":419,"end":632},"obj":"Sentence"},{"id":"T4","span":{"begin":633,"end":768},"obj":"Sentence"},{"id":"T5","span":{"begin":769,"end":977},"obj":"Sentence"},{"id":"T6","span":{"begin":978,"end":1207},"obj":"Sentence"},{"id":"T7","span":{"begin":1208,"end":1374},"obj":"Sentence"},{"id":"T8","span":{"begin":1375,"end":1385},"obj":"Sentence"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}

Anatomy-UBERON

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":19,"end":27},"obj":"Body_part"},{"id":"T4","span":{"begin":166,"end":174},"obj":"Body_part"},{"id":"T7","span":{"begin":1258,"end":1271},"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/GO_0016020"},{"id":"A5","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000094"},{"id":"A6","pred":"uberon_id","subj":"T4","obj":"http://purl.obolibrary.org/obo/UBERON_0000158"},{"id":"A7","pred":"uberon_id","subj":"T7","obj":"http://purl.obolibrary.org/obo/GO_0005622"}],"text":"Vesicular-integral membrane protein, VIP36, recognizes high-mannose type glycans containing alpha1--\u003e2 mannosyl residues in MDCK cells.\nThe 36 kDa vesicular-integral membrane protein, VIP36, has been originally isolated from MDCK cells as a component of glycolipid-enriched detergent-insoluble complexes containing apical marker proteins, and its luminal domain shows homology to leguminous plant lectins and ERGIC-53. As the first step to identify the functional role of VIP36, the carbohydrate binding specificity of VIP36 was investigated using a fusion protein of glutathione- S -transferase and luminal domain of VIP36 (Vip36). It was found that VIP36 recognizes high-mannose type glycans containing alpha1--\u003e2 Man residues and alpha-amino substituted asparagine. The binding of Vip36 to high-mannose type glycans was independent of Ca(2+)and theoptimal condition was pH 6.0 at 37 degrees C. The concentration at which half inhibition of the binding by Man(7-9).GlcNAc(2). N Ac. Asn occurred was 1.0 x 10(-9)M. The association constant between Man(7-9).GlcNAc(2)in porcine thyroglobulin and immobilized Vip36 was 2.1 x 10(8)M(-1)as determined by means of a biosensor based on surface plasmon resonance. These results indicate that VIP36 functions as an intracellular lectin recognizing glycoproteins which possess high-mannose type glycans, (Manalpha1--\u003e2)(2-4).Man(5). GlcNAc(2)."}