Q91YY2 · B4GT3_MOUSE
- ProteinBeta-1,4-galactosyltransferase 3
- GeneB4galt3
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids395 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Catalytic activity
- an N-acetyl-beta-D-glucosaminyl derivative + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-N-acetyl-beta-D-glucosaminyl derivative + H+ + UDPThis reaction proceeds in the forward direction.
- beta-D-glucosylceramide + UDP-alpha-D-galactose = a beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H+ + UDPThis reaction proceeds in the forward direction.
- a neolactoside IV3-beta-GlcNAc-nLc4Cer + UDP-alpha-D-galactose = beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-beta-D-Glc-(1<->1')-Cer + H+ + UDPThis reaction proceeds in the forward direction.
Cofactor
Pathway
Protein modification; protein glycosylation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 132-136 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: PHRAR | ||||||
Binding site | 171-173 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: FNR | ||||||
Binding site | 198-199 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: VD | ||||||
Binding site | 199 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 228 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 260 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 262-265 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GEDD | ||||||
Binding site | 293 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 293-295 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: HRG | ||||||
Binding site | 305 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cisterna membrane | |
Molecular Function | beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity | |
Molecular Function | galactosyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | N-acetyllactosamine synthase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | galactosylceramide biosynthetic process | |
Biological Process | glycosylation | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-1,4-galactosyltransferase 3
- EC number
- Short namesBeta-1,4-GalTase 3; Beta4Gal-T3; b4Gal-T3
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ91YY2
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus, Golgi stack membrane ; Single-pass type II membrane protein
Note: Trans cisternae of Golgi stack.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-10 | Cytoplasmic | ||||
Sequence: MLRRLLERPC | ||||||
Transmembrane | 11-31 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: TLALLVGSQLAVMMYLSLGGF | ||||||
Topological domain | 32-395 | Lumenal | ||||
Sequence: RSLSALFGRDPGPTFDYSHPHDVYSNLSHLPAAPGAAGAPPAQALPYCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080538 | 1-395 | Beta-1,4-galactosyltransferase 3 | |||
Sequence: MLRRLLERPCTLALLVGSQLAVMMYLSLGGFRSLSALFGRDPGPTFDYSHPHDVYSNLSHLPAAPGAAGAPPAQALPYCPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGCEPRSRTAIIVPHRAREHHLRLLLYHLHPFLQRQQLAYGIYVIHQAGNGTFNRAKLLNVGVREALRDEEWDCLFLHDVDLLPENDHNLYVCDPRGPRHVAVAMNKFGYSLPYPQYFGGVSALTPDQYLKMNGFPNEYWGWGGEDDDIATRVRLAGMKISRPPTSVGHYKMVKHRGDKGNEENPHRFDLLVRTQNSWTQDGMNSLTYRLLARELGPLYTNITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH | ||||||
Glycosylation | 57 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 79↔121 | |||||
Sequence: CPERSPFLVGPVSVSFSPVPSLAEIVERNPRVESGGRYRPAGC | ||||||
Glycosylation | 168 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 192↔211 | |||||
Sequence: CLFLHDVDLLPENDHNLYVC | ||||||
Glycosylation | 339 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 387 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 340-395 | Disordered | ||||
Sequence: ITADIGTDPRGPRSPSGPRYPPGSSQAFRQEMLQRRPPARPGPLPTANHTAPRGSH |
Sequence similarities
Belongs to the glycosyltransferase 7 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length395
- Mass (Da)44,084
- Last updated2001-12-01 v1
- Checksum16401B033EEB4B21
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A6YXE7 | A0A0A6YXE7_MOUSE | B4galt3 | 173 | ||
A0A0A6YXS2 | A0A0A6YXS2_MOUSE | B4galt3 | 13 | ||
D3YUU0 | D3YUU0_MOUSE | B4galt3 | 65 | ||
D3YVA5 | D3YVA5_MOUSE | B4galt3 | 139 |
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 353 | in Ref. 1; AAF22221 | ||||
Sequence: S → A |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF142671 EMBL· GenBank· DDBJ | AAF22221.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013619 EMBL· GenBank· DDBJ | AAH13619.1 EMBL· GenBank· DDBJ | mRNA |