Q92685 · ALG3_HUMAN
- ProteinDol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
- GeneALG3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids438 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase 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 first dolichyl beta-D-mannosyl phosphate derived mannose in an alpha-1,3 linkage to Man5GlcNAc2-PP-dolichol to produce Man6GlcNAc2-PP-dolichol (PubMed:10581255).
Man6GlcNAc2-PP-dolichol is a substrate for ALG9, the following enzyme in the biosynthetic pathway (PubMed:10581255).
Man6GlcNAc2-PP-dolichol is a substrate for ALG9, the following enzyme in the biosynthetic pathway (PubMed:10581255).
Catalytic activity
- an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[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 beta-D-mannosyl phosphate = an alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-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.
an α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[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:19516 + a di-trans,poly-cis-dolichyl β-D-mannosyl phosphate RHEA-COMP:19501 = an α-D-Man-(1→2)-α-D-Man-(1→2)-α-D-Man-(1→3)-[α-D-Man-(1→3)-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:19517 + 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 | |
Molecular Function | alpha-1,3-mannosyltransferase activity | |
Molecular Function | dol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity | |
Biological Process | dolichol-linked oligosaccharide biosynthetic process | |
Biological Process | protein glycosylation | |
Biological Process | protein N-linked glycosylation |
Keywords
- Molecular function
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameDol-P-Man:Man(5)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase
- 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 accessionQ92685
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 41-61 | Helical | |||
Transmembrane | 95-115 | Helical | |||
Transmembrane | 123-143 | Helical | |||
Transmembrane | 149-169 | Helical | |||
Transmembrane | 172-192 | Helical | |||
Transmembrane | 203-223 | Helical | |||
Transmembrane | 231-251 | Helical | |||
Transmembrane | 289-309 | Helical | |||
Transmembrane | 332-352 | Helical | |||
Transmembrane | 356-376 | Helical | |||
Transmembrane | 407-427 | Helical | |||
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Congenital disorder of glycosylation 1D (CDG1D)
- Note
- DescriptionA form of congenital disorder of glycosylation, a multisystem disorder caused by a defect in glycoprotein biosynthesis and characterized by under-glycosylated serum glycoproteins. Congenital disorders of glycosylation result in a wide variety of clinical features, such as defects in the nervous system development, psychomotor retardation, dysmorphic features, hypotonia, coagulation disorders, and immunodeficiency. The broad spectrum of features reflects the critical role of N-glycoproteins during embryonic development, differentiation, and maintenance of cell functions.
- See alsoMIM:601110
Natural variants in CDG1D
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_010306 | 118 | G>D | in CDG1D; loss of dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; dbSNP:rs28940588 | |
VAR_037806 | 171 | R>Q | in CDG1D; dbSNP:rs119103236 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Natural variant | VAR_037805 | 107 | in dbSNP:rs2233463 | ||
Natural variant | VAR_010306 | 118 | in CDG1D; loss of dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase activity; dbSNP:rs28940588 | ||
Natural variant | VAR_037806 | 171 | in CDG1D; dbSNP:rs119103236 | ||
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 550 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Chain | PRO_0000080566 | 1-438 | UniProt | Dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase | ||
Modified residue (large scale data) | 11 | PRIDE | Phosphoserine | |||
Modified residue | 13 | UniProt | Phosphoserine | |||
Modified residue (large scale data) | 13 | PRIDE | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | Q92685 | ARL13B Q3SXY8 | 3 | EBI-2848814, EBI-11343438 | |
BINARY | Q92685 | CD79A P11912 | 3 | EBI-2848814, EBI-7797864 | |
BINARY | Q92685 | CREB3 O43889 | 4 | EBI-2848814, EBI-625002 | |
BINARY | Q92685 | CREB3 O43889-2 | 4 | EBI-2848814, EBI-625022 | |
BINARY | Q92685 | LRP1 Q07954 | 2 | EBI-2848814, EBI-1046087 | |
BINARY | Q92685 | OSBP P22059 | 2 | EBI-2848814, EBI-2681902 | |
BINARY | Q92685 | OSBPL9 Q96SU4 | 2 | EBI-2848814, EBI-2511368 | |
BINARY | Q92685 | SERP1 Q9Y6X1 | 3 | EBI-2848814, EBI-10329948 | |
BINARY | Q92685 | SSMEM1 Q8WWF3 | 3 | EBI-2848814, EBI-17280858 | |
BINARY | Q92685 | SYPL1 Q16563 | 3 | EBI-2848814, EBI-2800683 | |
BINARY | Q92685 | TMEM52B Q4KMG9 | 3 | EBI-2848814, EBI-18178701 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q92685-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length438
- Mass (Da)50,126
- Last updated1997-02-01 v1
- MD5 ChecksumE0635E13B7CD13BF88E9961EE77131BB
Q92685-2
- Name2
- Differences from canonical
- 1-66: MAAGLRKRGRSGSAAQAEGLCKQWLQRAWQERRLLLREPRYTLLVAACLCLAEVGITFWVIHRVAY → MFPAQAKENAGFSGCGGD
Computationally mapped potential isoform sequences
There are 5 potential isoforms mapped to this entry
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_042738 | 1-66 | in isoform 2 | ||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Y09022 EMBL· GenBank· DDBJ | CAA70220.1 EMBL· GenBank· DDBJ | mRNA | ||
AK289361 EMBL· GenBank· DDBJ | BAF82050.1 EMBL· GenBank· DDBJ | mRNA | ||
AC061705 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC002839 EMBL· GenBank· DDBJ | AAH02839.1 EMBL· GenBank· DDBJ | mRNA | ||
BC004313 EMBL· GenBank· DDBJ | AAH04313.1 EMBL· GenBank· DDBJ | mRNA |