S7S106 · S7S106_GLOTA
- ProteinDol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids458 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc2Man9GlcNAc2-PP-Dol to produce Glc3Man9GlcNAc2-PP-Dol.
Catalytic activity
- a di-trans,poly-cis-dolichyl beta-D-glucosyl phosphate + an alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol = a alpha-D-Glc-(1->2)-alpha-D-Glc-(1->3)-alpha-D-Glc-(1->3)-alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + a di-trans,poly-cis-dolichyl phosphate + H+This reaction proceeds in the forward direction.
a di-trans,poly-cis-dolichyl β-D-glucosyl phosphate RHEA-COMP:19502 + an α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol RHEA-COMP:19522 = a α-D-Glc-(1→2)-α-D-Glc-(1→3)-α-D-Glc-(1→3)-α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→2)-α-D-Man-(1→6)]-α-D-Man-(1→6)]-β-D-Man-(1→4)-β-D-GlcNAc-(1→4)-α-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol RHEA-COMP:19512 + a di-trans,poly-cis-dolichyl phosphate RHEA-COMP:19498 + CHEBI:15378
Pathway
Protein modification; protein glycosylation.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | |
Biological Process | dolichol-linked oligosaccharide biosynthetic process |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Agaricomycetes > Gloeophyllales > Gloeophyllaceae > Gloeophyllum
Accessions
- Primary accessionS7S106
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 79-99 | Helical | ||||
Sequence: MLRLTPMLALVALPIALTHLL | ||||||
Transmembrane | 111-136 | Helical | ||||
Sequence: LLAPTLESVVLSAFPIVWFFGFLYYT | ||||||
Transmembrane | 235-257 | Helical | ||||
Sequence: FIPYGIVVALFGAFVVCNGGIVL | ||||||
Transmembrane | 272-292 | Helical | ||||
Sequence: LYYFLGFVTIFGWPVLVSGPG | ||||||
Transmembrane | 313-331 | Helical | ||||
Sequence: LVTAIVSAVMAVTVYKFTI | ||||||
Transmembrane | 351-375 | Helical | ||||
Sequence: IFMLHPVVPYLLIPGYIACAWAWFL | ||||||
Transmembrane | 382-402 | Helical | ||||
Sequence: TLLQTLLLPVFVLPTLLPTPL | ||||||
Transmembrane | 422-447 | Helical | ||||
Sequence: VPGWGVLLEGAWYAAINAATMWVFLY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-23 | |||||
Sequence: MASPMHHLVFTGICILVLRELNG | ||||||
Chain | PRO_5004544319 | 24-458 | Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alpha-1,2-glucosyltransferase | |||
Sequence: IVTEPYMDEPFHVPQAQAYCRGEFSYWDPKITTPPGLYVVSWVLKKIFLFKCNLQMLRLTPMLALVALPIALTHLLSYHQRVRPPSSLLAPTLESVVLSAFPIVWFFGFLYYTEVPSLLFVVLTVVAASQGKHWLAGLLGLVSCTFRQTNVVWVLYAYASSQLMYLRFRRAAPNGSMPAKLHDPPALEAGPGDLLRSILSAPRVLPDVLPKFIPYGIVVALFGAFVVCNGGIVLGDKSNHIPSFHIPQLYYFLGFVTIFGWPVLVSGPGGLKSLIKEVRYRMFGNLRRSLVTAIVSAVMAVTVYKFTIHHPFLLSDNRHYTFYVWRRIFMLHPVVPYLLIPGYIACAWAWFLRVGRDQTLLQTLLLPVFVLPTLLPTPLLEPRYFLIPYVLLRAQVPDVPGWGVLLEGAWYAAINAATMWVFLYREREGVGRFMW |
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length458
- Mass (Da)51,841
- Last updated2013-10-16 v1
- Checksum086EFEA99D0E9FD6
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KB469296 EMBL· GenBank· DDBJ | EPQ61060.1 EMBL· GenBank· DDBJ | Genomic DNA |