alg10 (SPAC56F8.06c; UniProt Q10254) encodes the Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alpha-1,2-glucosyltransferase Alg10, which adds the terminal third glucose, completing Glc3Man9GlcNAc2-PP-Dol. A spontaneous alg10 mutation suppresses the sick phenotype of fission yeast lacking glucosidase I. In the lumenal phase of dolichol-linked oligosaccharide (Glc3Man9GlcNAc2-PP-Dol) assembly on the ER membrane, it adds the next sugar to the growing precursor that oligosaccharyltransferase transfers to nascent glycoproteins. Function is assigned by orthology to the S. cerevisiae ALG enzymes.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005783 endoplasmic reticulum | HDA PMID:16823372 ORFeome cloning and global analysis of protein localization ... | ACCEPT | Summary: ORFeome screen: ER. Supporting Evidence: PMID:16823372 we determined the localization of 4,431 proteins |
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference. Reason: Root organelle row kept. The ER claim holds; the curated UniProt SUBCELLULAR LOCATION (ER membrane, by similarity to S. cerevisiae Alg10, UniProtKB:P50076) and twelve predicted TM helices agree with the HDA ORFeome ER localization (PMID:16823372) of S. pombe Alg10; the IBA stops at the organelle, the ER membrane is captured by separate rows. Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:SCHPO/alg10/alg10-uniprot.txt Multi-pass membrane protein |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: ER membrane: LLO assembly takes place on the ER membrane. Reason: The curated UniProt SUBCELLULAR LOCATION (ER membrane, by similarity to S. cerevisiae Alg10, UniProtKB:P50076) is consistent with twelve predicted transmembrane helices (FT TRANSMEM 7..27 to 408..428). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:SCHPO/alg10/alg10-uniprot.txt Multi-pass membrane protein |
| GO:0005789 endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: ER membrane: LLO assembly takes place on the ER membrane. Reason: The curated UniProt SUBCELLULAR LOCATION (ER membrane, by similarity to S. cerevisiae Alg10, UniProtKB:P50076) is consistent with twelve predicted transmembrane helices (FT TRANSMEM 7..27 to 408..428). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:SCHPO/alg10/alg10-uniprot.txt Multi-pass membrane protein |
| GO:0006487 protein N-linked glycosylation | IBA GO_REF:0000033 | ACCEPT | Summary: LLO assembly is needed for protein N-glycosylation. Reason: The curated UniProt FUNCTION (by similarity to S. cerevisiae Alg10, UniProtKB:P50076) places Alg10 in dolichol-linked oligosaccharide assembly for protein N-glycosylation; in S. pombe, an alg10 mutation alters the lipid-linked oligosaccharide pattern (PMID:30389790). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. PMID:30389790 As the protein encoded by that gene is responsible for the addition of the outermost glucose to the Dol-PP derivative |
| GO:0006488 dolichol-linked oligosaccharide biosynthetic process | EXP PMID:30389790 Abrogation of glucosidase I-mediated glycoprotein deglucosyl... | ACCEPT | Summary: A suppressor mutation in alg10 relieves the gls1 (glucosidase I) defect by preventing addition of the third glucose. Supporting Evidence: PMID:30389790 Our results suggest that a suppression of the mutant phenotype is caused by a simultaneous mutation in the alg10 + gene in the strain that displayed a relieved growth rate. |
| GO:0006488 dolichol-linked oligosaccharide biosynthetic process | IEA GO_REF:0000002 | ACCEPT | Summary: Mapping. Reason: The curated UniProt FUNCTION (by similarity to S. cerevisiae Alg10, UniProtKB:P50076) assigns this LLO-assembly step; S. pombe lipid-linked oligosaccharide analysis of an alg10 mutant (PMID:30389790) shows reduced Glc3Man9GlcNAc2 formation. Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. PMID:30389790 suggesting reduced Alg10p glucosyltransferase activity in the Ξ gls1-H strain. A mutation in the alg10 + gene was indeed observed in this strain. |
| GO:0009101 glycoprotein biosynthetic process | IMP PMID:34851357 A novel fission yeast platform to model N-glycosylation and ... | TOO GENERAL | Summary: Broad parent; platform mutants alter glycoprotein N-glycans, captured more specifically by LLO biosynthesis. Supporting Evidence: PMID:34851357 We constructed a platform of 16 Schizosaccharomyces pombe strains that synthesize all possible theoretical combinations of LLOs containing three to zero glucose (Glc) residues and nine to five mannose (Man) residues. |
| GO:0016757 glycosyltransferase activity | IMP PMID:34851357 A novel fission yeast platform to model N-glycosylation and ... | TOO GENERAL | Summary: Generic glycosyltransferase; the platform deletion defines the specific step. Supporting Evidence: PMID:34851357 We constructed a platform of 16 Schizosaccharomyces pombe strains that synthesize all possible theoretical combinations of LLOs containing three to zero glucose (Glc) residues and nine to five mannose (Man) residues. |
| GO:0098553 lumenal side of endoplasmic reticulum membrane | TAS PMID:9878760 The dolichol pathway of N-linked glycosylation. | ACCEPT | Summary: Lumenal-face LLO assembly steps (after flipping), using Dol-P-Man/Dol-P-Glc donors. Supporting Evidence: PMID:9878760 The oligosaccharide substrate for the N-linked protein glycosylation is assembled at the membrane of the endoplasmic reticulum. |
| GO:0106073 dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT inference. Reason: The curated UniProt FUNCTION (by similarity to S. cerevisiae Alg10, UniProtKB:P50076) describes this terminal alpha-1,2 glucose addition; in S. pombe, an alg10 frameshift strain accumulates Glc2Man9GlcNAc2 LLO, indicating reduced Alg10 glucosyltransferase activity (PMID:30389790, in vivo glycan profiling, not an enzyme assay). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol. PMID:30389790 suggesting reduced Alg10p glucosyltransferase activity in the Ξ gls1-H strain. A mutation in the alg10 + gene was indeed observed in this strain. |
| GO:0106073 dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Mapping. Reason: The curated UniProt FUNCTION (by similarity to S. cerevisiae Alg10, UniProtKB:P50076) describes this terminal alpha-1,2 glucose addition; in S. pombe, an alg10 frameshift strain accumulates Glc2Man9GlcNAc2 LLO, indicating reduced Alg10 glucosyltransferase activity (PMID:30389790, in vivo glycan profiling, not an enzyme assay). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol. PMID:30389790 suggesting reduced Alg10p glucosyltransferase activity in the Ξ gls1-H strain. A mutation in the alg10 + gene was indeed observed in this strain. |
| GO:0106073 dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | IGI PMID:30389790 Abrogation of glucosidase I-mediated glycoprotein deglucosyl... | ACCEPT | Summary: alg10 mutation suppresses glucosidase I loss, consistent with loss of terminal alpha-1,2-glucose addition. Supporting Evidence: PMID:30389790 Our results suggest that a suppression of the mutant phenotype is caused by a simultaneous mutation in the alg10 + gene in the strain that displayed a relieved growth rate. |
| GO:0106073 dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | ISS GO_REF:0000024 | ACCEPT | Summary: Similarity. Reason: The curated UniProt FUNCTION (by similarity to S. cerevisiae Alg10, UniProtKB:P50076) describes this terminal alpha-1,2 glucose addition; in S. pombe, an alg10 frameshift strain accumulates Glc2Man9GlcNAc2 LLO, indicating reduced Alg10 glucosyltransferase activity (PMID:30389790, in vivo glycan profiling, not an enzyme assay). Supporting Evidence: file:SCHPO/alg10/alg10-uniprot.txt adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol. PMID:30389790 suggesting reduced Alg10p glucosyltransferase activity in the Ξ gls1-H strain. A mutation in the alg10 + gene was indeed observed in this strain. |
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