Q09324 · GCNT1_MOUSE
- ProteinBeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- GeneGcnt1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids428 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Glycosyltransferase that catalyzes the transfer of an N-acetylglucosamine (GlcNAc) moiety in beta1-6 linkage from UDP-GlcNAc onto mucin-type core 1 O-glycan to form the branched mucin-type core 2 O-glycan. The catalysis is metal ion-independent and occurs with inversion of the anomeric configuration of sugar donor (PubMed:12954635, PubMed:22056345, PubMed:9881978).
Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (PubMed:9881978).
Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage-specific embryonic antigen 1 (SSEA-1) determinant (PubMed:7983056).
Can use Galbeta1-3GalNAcalpha1-R and Galbeta1-3GalNAcbeta1-R oligosaccharide derivatives as acceptor substrates (PubMed:7983056).
Selectively involved in synthesis of mucin-type core 2 O-glycans that serve as scaffolds for the display of selectin ligand sialyl Lewis X epitope by myeloid cells, with an impact on homeostasis and recruitment to inflammatory sites (PubMed:9881978).
Can also act on glycolipid substrates. Transfers GlcNAc moiety to GalGb4Cer globosides in a reaction step to the synthesis of stage-specific embryonic antigen 1 (SSEA-1) determinant (PubMed:7983056).
Can use Galbeta1-3GalNAcalpha1-R and Galbeta1-3GalNAcbeta1-R oligosaccharide derivatives as acceptor substrates (PubMed:7983056).
Catalytic activity
- O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-seryl-[protein] + H+ + UDPThis reaction proceeds in the forward direction.
- O3-[beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl]-L-threonyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-{beta-D-galactosyl-(1->3)-[N-acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-L-threonyl-[protein] + H+ + UDPThis reaction proceeds in the forward direction.
- a globoside GalGb4Cer + UDP-N-acetyl-alpha-D-glucosamine = a globoside GlcNAc-(beta1->6)-GalGb4Cer + H+ + UDPThis reaction proceeds in the forward direction.
- a ganglioside GA1 + UDP-N-acetyl-alpha-D-glucosamine = a ganglioside beta-DGlcNAc-(1->6)-GA1 + H+ + UDPThis reaction proceeds in the forward direction.
Activity regulation
Inactivated by thiol-reactive agents. Inhibited by free UDP.
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.1 mM | UDP-N-acetyl-alpha-D-glucosamine | |||||
0.11 mM | Beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R | |||||
0.11 mM | Globoside GalGb4Cer | |||||
0.31 mM | Ganglioside GA1 | |||||
1.25 mM | and Galbeta1-3GalNAcalpha1-R | |||||
0.53 mM | Galbeta1-3GalNAcbeta1-R |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
9.2 μmol/min/mg | toward beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R |
Pathway
Protein modification; protein glycosylation.
Glycolipid biosynthesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 128-130 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: VVH | ||||||
Binding site | 155-157 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: DRK | ||||||
Binding site | 187 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 243 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 250 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 251 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 254 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Active site | 320 | Nucleophile | ||||
Sequence: E | ||||||
Binding site | 320 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 341 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 358 | beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 378 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 401 | UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI) | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Cellular Component | Golgi cisterna | |
Cellular Component | Golgi membrane | |
Cellular Component | trans-Golgi network | |
Molecular Function | beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity | |
Molecular Function | nucleotide binding | |
Biological Process | cell adhesion molecule production | |
Biological Process | glycoprotein biosynthetic process | |
Biological Process | kidney morphogenesis | |
Biological Process | leukocyte tethering or rolling | |
Biological Process | O-glycan processing, core 2 | |
Biological Process | positive regulation of leukocyte tethering or rolling | |
Biological Process | response to insulin | |
Biological Process | tissue morphogenesis |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameBeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ09324
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Single-pass type II membrane protein
Note: Also detected in the trans-Golgi network.
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-9 | Cytoplasmic | ||||
Sequence: MLRNLFRRR | ||||||
Transmembrane | 10-32 | Helical; Signal-anchor for type II membrane protein | ||||
Sequence: LFSCPTKYYFMLLVLSLITFSVL | ||||||
Topological domain | 33-428 | Lumenal | ||||
Sequence: RIHQKPEFFSVRHLELAGDDPYSNVNCTKILQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIVEPLTKEEVGFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKCSTGENNLETEKMPPNKEERWKKRYTVVDGKLTNTGIVKAPPPLKTPLFSGSAYFVVTREYVGYVLENENIQKLMEWAQDTYSPDEFLWATIQRIPEVPGSFPSSNKYDLSDMNAIARFVKWQYFEGHVSNGAPYPPCSGVHVRSVCVFGAGDLSWMLRQHHLFANKFDMDVDPFAIQCLDEHLRHKALENLEH |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deficient mice show normal organogenesis and fertility. The loss of core 2 O-glycans on leukocytes is associated with leukocytosis and impaired neutrophil recruitment at the inflammatory site, while lymphocyte homing to peripheral lymphoid organs is not affected.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 217 | Protects from inactivation caused by air oxidation or thiol-reactive agents. Reduces the affinity for UDP-GlcNAc; when associated with A-378. Abolishes binding to UDP-GlcNAc; when associated with A-401. Loss of catalytic activity; when associated with A-378 and A-401. | ||||
Sequence: C → S | ||||||
Mutagenesis | 378 | Loss of catalytic activity; when associated with S-217 and A-401. Reduces the affinity for UDP-GlcNAc; when associated with S-217. | ||||
Sequence: R → A | ||||||
Mutagenesis | 401 | Loss of catalytic activity; when associated with S-217 and A-378. Abolishes binding to UDP-GlcNAc; when associated with S-217. | ||||
Sequence: K → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 25 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, glycosylation, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000191396 | 1-428 | Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase | |||
Sequence: MLRNLFRRRLFSCPTKYYFMLLVLSLITFSVLRIHQKPEFFSVRHLELAGDDPYSNVNCTKILQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIVEPLTKEEVGFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKCSTGENNLETEKMPPNKEERWKKRYTVVDGKLTNTGIVKAPPPLKTPLFSGSAYFVVTREYVGYVLENENIQKLMEWAQDTYSPDEFLWATIQRIPEVPGSFPSSNKYDLSDMNAIARFVKWQYFEGHVSNGAPYPPCSGVHVRSVCVFGAGDLSWMLRQHHLFANKFDMDVDPFAIQCLDEHLRHKALENLEH | ||||||
Glycosylation | 58 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 59↔413 | |||||
Sequence: CTKILQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIVEPLTKEEVGFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKCSTGENNLETEKMPPNKEERWKKRYTVVDGKLTNTGIVKAPPPLKTPLFSGSAYFVVTREYVGYVLENENIQKLMEWAQDTYSPDEFLWATIQRIPEVPGSFPSSNKYDLSDMNAIARFVKWQYFEGHVSNGAPYPPCSGVHVRSVCVFGAGDLSWMLRQHHLFANKFDMDVDPFAIQC | ||||||
Glycosylation | 95 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Disulfide bond | 100↔172 | |||||
Sequence: CASFIRTRKYIVEPLTKEEVGFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASC | ||||||
Disulfide bond | 151↔199 | |||||
Sequence: CIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNC | ||||||
Disulfide bond | 372↔381 | |||||
Sequence: CSGVHVRSVC |
Post-translational modification
N-glycosylated.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in kidney, liver, stomach, spleen, lung and brain.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 5-9 | Mediates interaction with GOLPH3 and is necessary and sufficient for localization to the Golgi | ||||
Sequence: LFRRR | ||||||
Region | 33-121 | Stem region | ||||
Sequence: RIHQKPEFFSVRHLELAGDDPYSNVNCTKILQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIVEPLTKEEVGF | ||||||
Region | 122-428 | Catalytic | ||||
Sequence: PIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKCSTGENNLETEKMPPNKEERWKKRYTVVDGKLTNTGIVKAPPPLKTPLFSGSAYFVVTREYVGYVLENENIQKLMEWAQDTYSPDEFLWATIQRIPEVPGSFPSSNKYDLSDMNAIARFVKWQYFEGHVSNGAPYPPCSGVHVRSVCVFGAGDLSWMLRQHHLFANKFDMDVDPFAIQCLDEHLRHKALENLEH |
Sequence similarities
Belongs to the glycosyltransferase 14 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length428
- Mass (Da)49,839
- Last updated2011-07-27 v2
- Checksum57E54F07AFFE640B
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 88 | in Ref. 1; AAA60948 and 2; BAA22998/BAA22999 | ||||
Sequence: R → W | ||||||
Sequence conflict | 191 | in Ref. 1; AAA60948 | ||||
Sequence: S → T | ||||||
Sequence conflict | 238 | in Ref. 2; BAA22998/BAA22999 | ||||
Sequence: G → A | ||||||
Sequence conflict | 260 | in Ref. 1; AAA60948 and 2; BAA22998/BAA22999 | ||||
Sequence: T → A | ||||||
Sequence conflict | 362 | in Ref. 1; AAA60948 and 2; BAA22998/BAA22999 | ||||
Sequence: H → D | ||||||
Sequence conflict | 404 | in Ref. 2; BAA22998/BAA22999 | ||||
Sequence: M → I | ||||||
Sequence conflict | 420 | in Ref. 1; AAA60948 and 2; BAA22998/BAA22999 | ||||
Sequence: H → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U19265 EMBL· GenBank· DDBJ | AAA60948.1 EMBL· GenBank· DDBJ | mRNA | ||
D87332 EMBL· GenBank· DDBJ | BAA22998.1 EMBL· GenBank· DDBJ | mRNA | ||
D87333 EMBL· GenBank· DDBJ | BAA22999.1 EMBL· GenBank· DDBJ | mRNA | ||
AK045216 EMBL· GenBank· DDBJ | BAC32265.1 EMBL· GenBank· DDBJ | mRNA |