A0A7J7RNB4 · A0A7J7RNB4_RHIFE
- ProteinGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids347 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo-orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity: stearoyl-sphingomyelin was the most effective, followed by palmitoyl-sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group.
Catalytic activity
- 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP + H+
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 104-106 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 135 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 178 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 183 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 208-210 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Binding site | 210 | Mn2+ (UniProtKB | ChEBI) | |||
Site | 241 | Interaction with galactose moiety of substrate glycoprotein | |||
Active site | 297 | Proton donor/acceptor | |||
Binding site | 324-326 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | |||
Site | 334 | Interaction with galactose moiety of substrate glycoprotein | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | Golgi membrane | |
Molecular Function | galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity | |
Molecular Function | metal ion binding | |
Biological Process | carbohydrate metabolic process | |
Biological Process | chondroitin sulfate proteoglycan biosynthetic process | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Chiroptera > Yinpterochiroptera > Rhinolophoidea > Rhinolophidae > Rhinolophinae > Rhinolophus
Accessions
- Primary accessionA0A7J7RNB4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Transmembrane | 20-38 | Helical | |||
Keywords
- Cellular component
PTM/Processing
Features
Showing features for glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Glycosylation | 316 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
Interaction
Subunit
Homodimer. Interacts with SAR1A.
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Region | 48-67 | Disordered | |||
Compositional bias | 50-67 | Basic and acidic residues | |||
Sequence similarities
Belongs to the glycosyltransferase 43 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length347
- Mass (Da)39,769
- Last updated2021-04-07 v1
- Checksum90654C663AC48029
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 50-67 | Basic and acidic residues | |||
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JACAGC010000025 EMBL· GenBank· DDBJ | KAF6277652.1 EMBL· GenBank· DDBJ | Genomic DNA |