alg1 (SPAC23C4.14; UniProt O13933) encodes the GDP-Man-dependent chitobiosyldiphosphodolichol beta-1,4-mannosyltransferase Alg1, which adds the first (beta-linked) mannose. In the cytoplasmic 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:0000030 mannosyltransferase activity | IBA GO_REF:0000033 | TOO GENERAL | Summary: Generic mannosyltransferase; the specific activity is annotated. Reason: True but uninformative. The curated reaction (transfer of mannose from GDP-mannose to GlcNAc(2)-PP-dolichol, by similarity to S. cerevisiae ALG1, P16661) and the PANTHER subfamily assignment support the specific GO:0004578 chitobiosyldiphosphodolichol beta-mannosyltransferase activity, asserted elsewhere in this review, which entails mannosyltransferase activity. No S. pombe enzyme assay. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt dolichol + GDP-alpha-D-mannose = a beta-D-Man-(1->4)-beta-D-GlcNAc- file:SCHPO/alg1/alg1-uniprot.txt PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1. |
| GO:0000030 mannosyltransferase activity | IEA GO_REF:0000002 | TOO GENERAL | Summary: Generic mannosyltransferase; the specific activity is annotated. Reason: True but uninformative. The curated reaction (transfer of mannose from GDP-mannose to GlcNAc(2)-PP-dolichol, by similarity to S. cerevisiae ALG1, P16661) and the PANTHER subfamily assignment support the specific GO:0004578 chitobiosyldiphosphodolichol beta-mannosyltransferase activity, asserted elsewhere in this review, which entails mannosyltransferase activity. No S. pombe enzyme assay. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt dolichol + GDP-alpha-D-mannose = a beta-D-Man-(1->4)-beta-D-GlcNAc- file:SCHPO/alg1/alg1-uniprot.txt PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1. |
| GO:0004578 chitobiosyldiphosphodolichol beta-mannosyltransferase activity | IEA GO_REF:0000120 | ACCEPT | Summary: beta-1,4-mannosyltransferase (first mannose) activity (mapping/similarity). Reason: UniProt's curated catalytic activity (GDP-Man + GlcNAc2-PP-Dol -> Man-beta1,4-GlcNAc2-PP-Dol, EC 2.4.1.142) is assigned by similarity to S. cerevisiae ALG1 (UniProtKB:P16661); PANTHER subfamily membership (PTHR13036:SF0) supports the specific activity. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt dolichol + GDP-alpha-D-mannose = a beta-D-Man-(1->4)-beta-D-GlcNAc- file:SCHPO/alg1/alg1-uniprot.txt DR PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1. |
| GO:0004578 chitobiosyldiphosphodolichol beta-mannosyltransferase activity | ISS GO_REF:0000024 | ACCEPT | Summary: beta-1,4-mannosyltransferase (first mannose) activity (mapping/similarity). Reason: UniProt's curated catalytic activity (GDP-Man + GlcNAc2-PP-Dol -> Man-beta1,4-GlcNAc2-PP-Dol, EC 2.4.1.142) is assigned by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), the ISS source; PANTHER subfamily membership (PTHR13036:SF0) supports the specific activity. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt dolichol + GDP-alpha-D-mannose = a beta-D-Man-(1->4)-beta-D-GlcNAc- file:SCHPO/alg1/alg1-uniprot.txt DR PANTHER; PTHR13036:SF0; CHITOBIOSYLDIPHOSPHODOLICHOL BETA-MANNOSYLTRANSFERASE; 1. |
| 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: UniProt's curated subcellular location (ER membrane, single-pass) is by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), matching the ER placement of the PAINT node; an independent S. pombe ORFeome screen (PMID:16823372, separate HDA row) also places it in the ER. Root ER term kept beside the ER-membrane rows (organelle policy). Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane |
| GO:0005789 endoplasmic reticulum membrane | IEA GO_REF:0000044 | ACCEPT | Summary: ER membrane: LLO assembly takes place on the ER membrane. Reason: UniProt's curated subcellular location (ER membrane, single-pass, N-terminal helical TRANSMEM) is by similarity to S. cerevisiae ALG1 (UniProtKB:P16661). Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:SCHPO/alg1/alg1-uniprot.txt TRANSMEM 1..19 |
| GO:0005789 endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: ER membrane: LLO assembly takes place on the ER membrane. Reason: UniProt's curated subcellular location (ER membrane, single-pass, N-terminal helical TRANSMEM) is by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), the ISS source. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt SUBCELLULAR LOCATION: Endoplasmic reticulum membrane file:SCHPO/alg1/alg1-uniprot.txt TRANSMEM 1..19 |
| GO:0006488 dolichol-linked oligosaccharide biosynthetic process | IC GO_REF:0000111 | ACCEPT | Summary: Dolichol-linked oligosaccharide (LLO) biosynthesis. Reason: UniProt's curated FUNCTION, by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), places alg1 in assembly of the lipid-linked (dolichol-PP) precursor oligosaccharide; the curator IC follows from the beta-mannosyltransferase activity, the first mannose addition to GlcNAc2-PP-Dol. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation file:SCHPO/alg1/alg1-uniprot.txt dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER |
| GO:0006488 dolichol-linked oligosaccharide biosynthetic process | ISS GO_REF:0000024 | ACCEPT | Summary: Dolichol-linked oligosaccharide (LLO) biosynthesis. Reason: UniProt's curated FUNCTION, by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), places alg1 in assembly of the lipid-linked (dolichol-PP) precursor oligosaccharide. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation file:SCHPO/alg1/alg1-uniprot.txt dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER |
| GO:0009101 glycoprotein biosynthetic process | IBA GO_REF:0000033 | TOO GENERAL | Summary: Glycoprotein biosynthesis, true but entailed by the accepted dolichol-linked oligosaccharide biosynthesis rows. Reason: By similarity to S. cerevisiae ALG1 (P16661), UniProt's FUNCTION and PATHWAY lines place the protein in formation of the lipid-linked precursor oligosaccharide for N-glycosylation, within protein glycosylation. GO:0006488 dolichol-linked oligosaccharide biosynthetic process, asserted on this gene, is part_of protein N-linked glycosylation and so entails this broad term through the is_a/part_of closure (checked with oaklib), as on alg2 and alg12. No S. pombe experiment. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt Participates in the formation of the lipid-linked precursor oligosaccharide for N-glycosylation. file:SCHPO/alg1/alg1-uniprot.txt PATHWAY: Protein modification; protein glycosylation. |
| GO:0098554 cytoplasmic side of endoplasmic reticulum membrane | ISS GO_REF:0000024 | ACCEPT | Summary: Cytoplasmic-face step (similarity). Reason: UniProt's curated FUNCTION, by similarity to S. cerevisiae ALG1 (UniProtKB:P16661), places the GlcNAc(2)-Man(5)-PP-Dol assembly steps on the cytoplasmic surface of the ER, and the topology features (by similarity to P16661) put the catalytic domain (117..424) on the cytoplasmic side. Supporting Evidence: file:SCHPO/alg1/alg1-uniprot.txt dolichol-pyrophosphate-GlcNAc(2)-Man(5) intermediate on the cytoplasmic surface of the ER file:SCHPO/alg1/alg1-uniprot.txt TOPO_DOM 117..424 |
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