Q5I7T1 · AG10B_HUMAN
- ProteinDol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase
- GeneALG10B
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids473 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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 | |
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | lumenal side of endoplasmic reticulum membrane | |
Cellular Component | plasma membrane | |
Molecular Function | dolichyl pyrophosphate Glc2Man9GlcNAc2 alpha-1,2-glucosyltransferase activity | |
Biological Process | dolichol-linked oligosaccharide biosynthetic process | |
Biological Process | protein N-linked glycosylation |
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
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ5I7T1
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Note: Also detected at the plasma membrane.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-6 | Cytoplasmic | ||||
Sequence: MAQLEG | ||||||
Transmembrane | 7-27 | Helical | ||||
Sequence: YCFSAALSCTFLVSCLLFSAF | ||||||
Topological domain | 28-64 | Extracellular | ||||
Sequence: SRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITT | ||||||
Transmembrane | 65-85 | Helical | ||||
Sequence: LPGLYLVSVGVVKPAIWIFAW | ||||||
Topological domain | 86-97 | Cytoplasmic | ||||
Sequence: SEHVVCSIGMLR | ||||||
Transmembrane | 98-118 | Helical | ||||
Sequence: FVNLLFSVGNFYLLYLLFHKV | ||||||
Topological domain | 119-126 | Extracellular | ||||
Sequence: QPRNKAAS | ||||||
Transmembrane | 127-147 | Helical | ||||
Sequence: SIQRVLSTLTLAVFPTLYFFN | ||||||
Topological domain | 148-150 | Cytoplasmic | ||||
Sequence: FLY | ||||||
Transmembrane | 151-171 | Helical | ||||
Sequence: YTEAGSMFFTLFAYLMCLYGN | ||||||
Topological domain | 172-175 | Extracellular | ||||
Sequence: HKTS | ||||||
Transmembrane | 176-196 | Helical | ||||
Sequence: AFLGFCGFMFRQTNIIWAVFC | ||||||
Topological domain | 197-256 | Cytoplasmic | ||||
Sequence: AGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLFCLTWP | ||||||
Transmembrane | 257-277 | Helical | ||||
Sequence: YILLGFLFCAFVVVNGGIVIG | ||||||
Topological domain | 278-283 | Extracellular | ||||
Sequence: DRSSHE | ||||||
Transmembrane | 284-304 | Helical | ||||
Sequence: ACLHFPQLFYFFSFTLFFSFP | ||||||
Topological domain | 305-317 | Cytoplasmic | ||||
Sequence: HLLSPSKIKTFLS | ||||||
Transmembrane | 318-338 | Helical | ||||
Sequence: LVWKHGILFLVVTLVSVFLVW | ||||||
Topological domain | 339-365 | Extracellular | ||||
Sequence: KFTYAHKYLLADNRHYTFYVWKRVFQR | ||||||
Transmembrane | 366-386 | Helical | ||||
Sequence: YAILKYLLVPAYIFAGWSIAD | ||||||
Topological domain | 387-392 | Cytoplasmic | ||||
Sequence: SLKSKP | ||||||
Transmembrane | 393-413 | Helical | ||||
Sequence: IFWNLMFFICLFIVIVPQKLL | ||||||
Topological domain | 414-436 | Extracellular | ||||
Sequence: EFRYFILPYVIYRLNITLPPTSR | ||||||
Transmembrane | 437-457 | Helical | ||||
Sequence: LVCELSCYAIVNFITFYIFLN | ||||||
Topological domain | 458-473 | Cytoplasmic | ||||
Sequence: KTFQWPNSQDIQRFMW |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_089086 | 33 | found in a patient with ventricular fibrillation and QT prolongation; uncertain significance; dbSNP:rs188043534 | |||
Sequence: E → D | ||||||
Natural variant | VAR_048217 | 84 | in dbSNP:rs6582584 | |||
Sequence: A → G | ||||||
Natural variant | VAR_061002 | 383 | in dbSNP:rs57963306 | |||
Sequence: S → N | ||||||
Natural variant | VAR_023753 | 446 | in dbSNP:rs61730283 | |||
Sequence: I → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 613 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000215448 | 1-473 | Dol-P-Glc:Glc2Man9GlcNAc2-PP-Dol alpha-1,2-glucosyltransferase | |||
Sequence: MAQLEGYCFSAALSCTFLVSCLLFSAFSRALREPYMDEIFHLPQAQRYCEGHFSLSQWDPMITTLPGLYLVSVGVVKPAIWIFAWSEHVVCSIGMLRFVNLLFSVGNFYLLYLLFHKVQPRNKAASSIQRVLSTLTLAVFPTLYFFNFLYYTEAGSMFFTLFAYLMCLYGNHKTSAFLGFCGFMFRQTNIIWAVFCAGNVIAQKLTEAWKTELQKKEDRLPPIKGPFAEFRKILQFLLAYSMSFKNLSMLFCLTWPYILLGFLFCAFVVVNGGIVIGDRSSHEACLHFPQLFYFFSFTLFFSFPHLLSPSKIKTFLSLVWKHGILFLVVTLVSVFLVWKFTYAHKYLLADNRHYTFYVWKRVFQRYAILKYLLVPAYIFAGWSIADSLKSKPIFWNLMFFICLFIVIVPQKLLEFRYFILPYVIYRLNITLPPTSRLVCELSCYAIVNFITFYIFLNKTFQWPNSQDIQRFMW |
Proteomic databases
PTM databases
Expression
Tissue specificity
Highly expressed in heart, placenta, liver, kidney and pancreas. Weakly expressed in lung, skeletal muscle and brain.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with KCNH1; may regulate KCNH1, possibly by regulating its N-glycosylation. Interacts with KCNH2; may reduce KCNH2 sensitivity to classic proarrhythmic drug blockade, possibly by regulating its N-glycosylation.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q5I7T1 | CD79A P11912 | 3 | EBI-18075734, EBI-7797864 | |
BINARY | Q5I7T1 | SHISAL1 Q3SXP7 | 3 | EBI-18075734, EBI-18037857 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)55,448
- Last updated2010-05-18 v2
- Checksum47D0CF7B6C84B8EC
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY845858 EMBL· GenBank· DDBJ | AAW31756.1 EMBL· GenBank· DDBJ | mRNA | ||
AC117372 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471111 EMBL· GenBank· DDBJ | EAW57795.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC137413 EMBL· GenBank· DDBJ | AAI37414.1 EMBL· GenBank· DDBJ | mRNA | ||
BC137414 EMBL· GenBank· DDBJ | AAI37415.1 EMBL· GenBank· DDBJ | mRNA |