Q9JHE4 · G3ST1_MOUSE
- ProteinGalactosylceramide sulfotransferase
- GeneGal3st1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids423 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Catalyzes the transfer of a sulfate group to position 3 of non-reducing beta-galactosyl residues in glycerolipids and sphingolipids, therefore participates in the biosynthesis of sulfoglycolipids (PubMed:11917099).
Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (PubMed:11917099).
Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro) (By similarity).
Catalyzes the synthesis of galactosylceramide sulfate (sulfatide), a major lipid component of the myelin sheath and of monogalactosylalkylacylglycerol sulfate (seminolipid), present in spermatocytes (PubMed:11917099).
Seems to prefer beta-glycosides at the non-reducing termini of sugar chains attached to a lipid moiety. Also acts on lactosylceramide, galactosyl 1-alkyl-2-sn-glycerol and galactosyl diacylglycerol (in vitro) (By similarity).
Catalytic activity
- 3'-phosphoadenylyl sulfate + a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine = adenosine 3',5'-bisphosphate + H+ + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enineThis reaction proceeds in the forward direction.
- 3'-phosphoadenylyl sulfate + beta-D-Gal-(1<->1')-Cer = 1-(3-O-sulfo-beta-D-galactosyl)-ceramide + adenosine 3',5'-bisphosphate + H+This reaction proceeds in the forward direction.
- 3'-phosphoadenylyl sulfate + a 1,2-diacyl-3-O-(beta-D-galactosyl)-sn-glycerol = 1,2-diacyl-3-(3-O-sulfo-beta-D-galactosyl)-sn-glycerol + adenosine 3',5'-bisphosphate + H+This reaction proceeds in the forward direction.
- 3'-phosphoadenylyl sulfate + a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) = adenosine 3',5'-bisphosphate + beta-D-3-sulfogalactosyl-(1->4)-beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine + H+This reaction proceeds in the forward direction.
Pathway
Lipid metabolism; sphingolipid metabolism.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | Golgi membrane | |
Cellular Component | membrane | |
Molecular Function | galactosylceramide sulfotransferase activity | |
Biological Process | galactosylceramide biosynthetic process | |
Biological Process | galactosylceramide metabolic process | |
Biological Process | glycerolipid metabolic process | |
Biological Process | glycolipid biosynthetic process | |
Biological Process | myelination | |
Biological Process | spermatogenesis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameGalactosylceramide sulfotransferase
- EC number
- Short namesGalCer sulfotransferase
- 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 accessionQ9JHE4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-12 | Cytoplasmic | ||||
Sequence: MTLLPKKPCKSK | ||||||
Transmembrane | 13-35 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: AKGLLLGALFTSFLLLLYSYVVP | ||||||
Topological domain | 36-423 | Lumenal | ||||
Sequence: PLYPNMAFTTSEAAAPCSPIPNEPVAATPANGSAGGCQPRRDIVFMKTHKTASSTLLNILFRFGQKHELKFAFPNGRNDFHYPSYFARSLVQDYRPGACFNIICNHMRFHYEEVRGLVRPGATFITVIRDPARLFESSFHYFGSVVPLTWKLSSRDKLAEFLQDPDRYYDPSSYNAHYLRNLLFFDLGYDSSLDPASPRVQEHILEVERRFHLVLLQEYFDESLVLLRELLCWDLEDVLYFKLNARRDSPVPRLSGELYRRATAWNLLDVRLYRHFNASFWRKVEAFGRERMAREVAELRQANEHMRHICIDGGQAVGAEAIQDSAMQPWQPLGIKSILGYNLKKSIGPQHEQLCRRMLTPEIQYLSDLGANLWVTKLWKFLRDFLRW |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mice homozygous for a null mutation of the CST gene born healthy and display hindlimb weakness from week 6 of age and subsequently show a prenounced tremor and progressive ataxia. Myelin vacuolation is observed in the cerebellar white matter, diencephalon, brainstem and spinal anterior column. Male mice were infertile due to a blocked spermatogenesis.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 19 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000085202 | 1-423 | Galactosylceramide sulfotransferase | |||
Sequence: MTLLPKKPCKSKAKGLLLGALFTSFLLLLYSYVVPPLYPNMAFTTSEAAAPCSPIPNEPVAATPANGSAGGCQPRRDIVFMKTHKTASSTLLNILFRFGQKHELKFAFPNGRNDFHYPSYFARSLVQDYRPGACFNIICNHMRFHYEEVRGLVRPGATFITVIRDPARLFESSFHYFGSVVPLTWKLSSRDKLAEFLQDPDRYYDPSSYNAHYLRNLLFFDLGYDSSLDPASPRVQEHILEVERRFHLVLLQEYFDESLVLLRELLCWDLEDVLYFKLNARRDSPVPRLSGELYRRATAWNLLDVRLYRHFNASFWRKVEAFGRERMAREVAELRQANEHMRHICIDGGQAVGAEAIQDSAMQPWQPLGIKSILGYNLKKSIGPQHEQLCRRMLTPEIQYLSDLGANLWVTKLWKFLRDFLRW | ||||||
Glycosylation | 66 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 312 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in brain, testis, kidney, stomach, small intestine, liver, and lung. Not detected in heart, skeletal muscle, and spleen.
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length423
- Mass (Da)48,968
- Last updated2002-07-26 v2
- ChecksumFD54A1A71F4AEE46
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 18 | in Ref. 2; BAB25160 | ||||
Sequence: L → P | ||||||
Sequence conflict | 263 | in Ref. 2; BAB25160 | ||||
Sequence: R → Q | ||||||
Sequence conflict | 271 | in Ref. 2; BAB25160 | ||||
Sequence: E → K | ||||||
Sequence conflict | 358 | in Ref. 1; BAA93009/BAA93008 | ||||
Sequence: Q → R | ||||||
Sequence conflict | 392 | in Ref. 2; BAB25160 | ||||
Sequence: R → G | ||||||
Sequence conflict | 398 | in Ref. 1; BAA93009/BAA93008 | ||||
Sequence: I → T |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AB032940 EMBL· GenBank· DDBJ | BAA93009.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AB032939 EMBL· GenBank· DDBJ | BAA93008.1 EMBL· GenBank· DDBJ | mRNA | ||
AK007645 EMBL· GenBank· DDBJ | BAB25160.1 EMBL· GenBank· DDBJ | mRNA | ||
BC026806 EMBL· GenBank· DDBJ | AAH26806.1 EMBL· GenBank· DDBJ | mRNA |