O88419 · B4GT6_RAT
- ProteinBeta-1,4-galactosyltransferase 6
- GeneB4galt6
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids382 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer) (PubMed:9593693).
LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity).
LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity).
Catalytic activity
- a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + UDP-alpha-D-galactose = a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + H+ + UDPThis reaction proceeds in the forward direction.
Cofactor
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Activity regulation
Inhibited by EDTA.
pH Dependence
Optimum pH is 7.2.
Pathway
Protein modification; protein glycosylation.
Sphingolipid metabolism.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 163-167 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: PFRNR | ||||||
Binding site | 202-204 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: FNR | ||||||
Binding site | 229-230 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: VD | ||||||
Binding site | 230 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 258 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 290 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 292-295 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: GEDD | ||||||
Binding site | 323 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 323-324 | UDP-alpha-D-galactose (UniProtKB | ChEBI) | ||||
Sequence: HH | ||||||
Binding site | 334 | N-acetyl-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi apparatus | |
Cellular Component | Golgi cisterna membrane | |
Molecular Function | galactosyltransferase activity | |
Molecular Function | metal ion binding | |
Molecular Function | UDP-galactose:glucosylceramide beta-1,4-galactosyltransferase activity | |
Biological Process | carbohydrate metabolic process | |
Biological Process | central nervous system myelination | |
Biological Process | central nervous system neuron axonogenesis | |
Biological Process | ganglioside biosynthetic process via lactosylceramide | |
Biological Process | glycosphingolipid biosynthetic process | |
Biological Process | glycosylation | |
Biological Process | lactosylceramide biosynthetic process | |
Biological Process | neuron maturation | |
Biological Process | protein glycosylation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameBeta-1,4-galactosyltransferase 6
- EC number
- Short namesBeta-1,4-GalTase 6; Beta4Gal-T6; b4Gal-T6
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Rattus
Accessions
- Primary accessionO88419
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 | 1-15 | Cytoplasmic | ||||
Sequence: MSALKRMMRVSNRSL | ||||||
Transmembrane | 16-35 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: IAFIFFFSLSTSCLYFIYVA | ||||||
Topological domain | 36-382 | Lumenal | ||||
Sequence: PGIANTYLFMVQARGIMLRENVKTIGHMIRLYTNKNTTLNGTDYPEGNNTSDYLVQTTTYLPQNFTYSPHLPCPEKLPYMRGFLSVNVSEISFDEVHQLFSKDSEIEPGGHWRPQDCKPRWKVAVLIPFRNRHEHLPIFFLHLIPMLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDRAWDCVIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVHYSGYNVTRPEGDLGKYTSIPHHHRGEVQFLGRYKLLRYSKERQFIDGLNNLLYTPKILVDRLYTNISVNLMPELAPVEDY |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080549 | 1-382 | Beta-1,4-galactosyltransferase 6 | |||
Sequence: MSALKRMMRVSNRSLIAFIFFFSLSTSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTIGHMIRLYTNKNTTLNGTDYPEGNNTSDYLVQTTTYLPQNFTYSPHLPCPEKLPYMRGFLSVNVSEISFDEVHQLFSKDSEIEPGGHWRPQDCKPRWKVAVLIPFRNRHEHLPIFFLHLIPMLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDRAWDCVIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVHYSGYNVTRPEGDLGKYTSIPHHHRGEVQFLGRYKLLRYSKERQFIDGLNNLLYTPKILVDRLYTNISVNLMPELAPVEDY | ||||||
Glycosylation | 71 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 75 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 83 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 84 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 99 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 108↔152 | |||||
Sequence: CPEKLPYMRGFLSVNVSEISFDEVHQLFSKDSEIEPGGHWRPQDC | ||||||
Glycosylation | 122 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 223↔242 | |||||
Sequence: CVIFHDVDHLPENDRNYYGC | ||||||
Glycosylation | 307 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 367 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Highest expression in brain with lower levels found in lungs, heart, skeletal muscle and kidney. Lowest expression in testis, liver and spleen.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length382
- Mass (Da)44,778
- Last updated1998-11-01 v1
- Checksum37C2A32B32D10D51
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A0A0MXX9 | A0A0A0MXX9_RAT | B4galt6 | 357 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF048687 EMBL· GenBank· DDBJ | AAC24515.1 EMBL· GenBank· DDBJ | mRNA |