Q9P2W7 · B3GA1_HUMAN
- ProteinGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
- GeneB3GAT1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids334 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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] + H+ + UDP
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site, site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 91-93 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: PTY | ||||||
Binding site | 122 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 165 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 170 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 195-197 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: DDD | ||||||
Binding site | 197 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 228 | Interaction with galactose moiety of substrate glycoprotein | ||||
Sequence: E | ||||||
Active site | 284 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 311-313 | UDP-alpha-D-glucuronate (UniProtKB | ChEBI) | ||||
Sequence: HTR | ||||||
Site | 321 | Interaction with galactose moiety of substrate glycoprotein | ||||
Sequence: N |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Cellular Component | extracellular region | |
Cellular Component | Golgi membrane | |
Cellular Component | intracellular membrane-bounded organelle | |
Cellular Component | 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 | glycosaminoglycan biosynthetic process | |
Biological Process | protein glycosylation | |
Biological Process | visual learning |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGalactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
- 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 accessionQ9P2W7
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Isoform 1
Golgi apparatus membrane ; Single-pass type II membrane protein
Isoform 2
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-6 | Cytoplasmic | ||||
Sequence: MPKRRD | ||||||
Transmembrane | 7-27 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: ILAIVLIVLPWTLLITVWHQS | ||||||
Topological domain | 28-334 | Lumenal | ||||
Sequence: TLAPLLAVHKDEGSDPRRETPPGADPREYCTSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI |
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_044538 | 131 | in dbSNP:rs35434644 | |||
Sequence: A → T |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 443 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000195167 | 1-334 | Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 | |||
Sequence: MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSDRDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVVEDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRETFPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVGWKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPKAANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI | ||||||
Modified residue | 103 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 108 | Phosphothreonine | ||||
Sequence: T | ||||||
Glycosylation | 140 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 184 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 303 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
The soluble form derives from the membrane form by proteolytic processing.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Homodimer. Interacts with SAR1A.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9P2W7 | CMTM7 Q96FZ5 | 3 | EBI-3918235, EBI-2807956 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 3-5 | Essential for transport from endoplasmic reticulum to Golgi apparatus and interaction with SAR1A | ||||
Sequence: KRR | ||||||
Region | 37-56 | Disordered | ||||
Sequence: KDEGSDPRRETPPGADPREY | ||||||
Region | 245-254 | Interaction with galactose moiety of substrate glycoprotein | ||||
Sequence: FDPHRPFAID |
Sequence similarities
Belongs to the glycosyltransferase 43 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9P2W7-1
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
- SynonymssGlcAT-P
- Length334
- Mass (Da)38,256
- Last updated2008-07-22 v2
- Checksum0DF42399D19701B3
Q9P2W7-2
- Name2
- SynonymslGlcAT-P
- Differences from canonical
- 1-1: M → MGNEEPWVQPALEM
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_058538 | 1 | in isoform 2 | |||
Sequence: M → MGNEEPWVQPALEM | ||||||
Sequence conflict | 240 | in Ref. 1; BAA96077 | ||||
Sequence: G → R | ||||||
Sequence conflict | 267 | in Ref. 2; BAH13084 | ||||
Sequence: Q → K | ||||||
Sequence conflict | 306 | in Ref. 2; BAH13084 | ||||
Sequence: K → R |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB029396 EMBL· GenBank· DDBJ | BAA96077.1 EMBL· GenBank· DDBJ | mRNA | ||
AK299637 EMBL· GenBank· DDBJ | BAH13084.1 EMBL· GenBank· DDBJ | mRNA | ||
CR457098 EMBL· GenBank· DDBJ | CAG33379.1 EMBL· GenBank· DDBJ | mRNA | ||
BC010466 EMBL· GenBank· DDBJ | AAH10466.1 EMBL· GenBank· DDBJ | mRNA |