Q09324 · GCNT1_MOUSE

  • Protein
    Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
  • Gene
    Gcnt1
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

Catalytic activity

Activity regulation

Inactivated by thiol-reactive agents. Inhibited by free UDP.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
1.1 mMUDP-N-acetyl-alpha-D-glucosamine
0.11 mMBeta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
0.11 mMGloboside GalGb4Cer
0.31 mMGanglioside GA1
1.25 mMand Galbeta1-3GalNAcalpha1-R
0.53 mMGalbeta1-3GalNAcbeta1-R
Vmax pH TEMPERATURE[C] NOTES EVIDENCE
9.2 μmol/min/mgtoward 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.

TypeIDPosition(s)Description
Binding site128-130UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site155-157UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site187UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site243beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site250beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site251beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site254beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Active site320Nucleophile
Binding site320beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site341beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site358beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl group (UniProtKB | ChEBI) of a glycoprotein (UniProtKB | ChEBI)
Binding site378UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)
Binding site401UDP-N-acetyl-alpha-D-glucosamine (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentextracellular space
Cellular ComponentGolgi cisterna
Cellular ComponentGolgi membrane
Cellular Componenttrans-Golgi network
Molecular Functionbeta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase activity
Molecular Functionnucleotide binding
Biological Processcell adhesion molecule production
Biological Processglycoprotein biosynthetic process
Biological Processkidney morphogenesis
Biological Processleukocyte tethering or rolling
Biological ProcessO-glycan processing, core 2
Biological Processpositive regulation of leukocyte tethering or rolling
Biological Processresponse to insulin
Biological Processtissue morphogenesis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
  • EC number
  • Alternative names
    • Core 2 beta-1,6-N-acetylglucosaminyltransferase
      (C2GlcNAcT
      )
    • Core 2-branching enzyme
    • Core2-GlcNAc-transferase (C2GNT)
    • Leukocyte type core 2 beta-1,6-N-acetylglucosaminyltransferase
      (C2GnT-L
      )

Gene names

    • Name
      Gcnt1

Organism names

  • Taxonomic identifier
  • Strains
    • DBA/2J
    • BALB/cJ
    • C57BL/6J
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    Q09324
  • Secondary accessions
    • O35981
    • Q8BRB2

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus membrane
; Single-pass type II membrane protein
Note: Also detected in the trans-Golgi network.

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-9Cytoplasmic
Transmembrane10-32Helical; Signal-anchor for type II membrane protein
Topological domain33-428Lumenal

Keywords

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.

TypeIDPosition(s)Description
Mutagenesis217Protects 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.
Mutagenesis378Loss of catalytic activity; when associated with S-217 and A-401. Reduces the affinity for UDP-GlcNAc; when associated with S-217.
Mutagenesis401Loss of catalytic activity; when associated with S-217 and A-378. Abolishes binding to UDP-GlcNAc; when associated with S-217.

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.

Go to variant viewer

PTM/Processing

Features

Showing features for chain, glycosylation, disulfide bond.

TypeIDPosition(s)Description
ChainPRO_00001913961-428Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
Glycosylation58N-linked (GlcNAc...) asparagine
Disulfide bond59↔413
Glycosylation95N-linked (GlcNAc...) asparagine
Disulfide bond100↔172
Disulfide bond151↔199
Disulfide bond372↔381

Post-translational modification

N-glycosylated.

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in kidney, liver, stomach, spleen, lung and brain.

Gene expression databases

Interaction

Subunit

Interacts with GOLPH3; may control GCNT1 retention in the Golgi.

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region.

TypeIDPosition(s)Description
Region5-9Mediates interaction with GOLPH3 and is necessary and sufficient for localization to the Golgi
Region33-121Stem region
Region122-428Catalytic

Sequence similarities

Belongs to the glycosyltransferase 14 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    49,839
  • Last updated
    2011-07-27 v2
  • Checksum
    57E54F07AFFE640B
MLRNLFRRRLFSCPTKYYFMLLVLSLITFSVLRIHQKPEFFSVRHLELAGDDPYSNVNCTKILQGDPEEIQKVKLEILTVQFKKRPRRTPHDYINMTRDCASFIRTRKYIVEPLTKEEVGFPIAYSIVVHHKIEMLDRLLRAIYMPQNFYCIHVDRKAEESFLAAVQGIASCFDNVFVASQLESVVYASWSRVKADLNCMKDLYRMNANWKYLINLCGMDFPIKTNLEIVRKLKCSTGENNLETEKMPPNKEERWKKRYTVVDGKLTNTGIVKAPPPLKTPLFSGSAYFVVTREYVGYVLENENIQKLMEWAQDTYSPDEFLWATIQRIPEVPGSFPSSNKYDLSDMNAIARFVKWQYFEGHVSNGAPYPPCSGVHVRSVCVFGAGDLSWMLRQHHLFANKFDMDVDPFAIQCLDEHLRHKALENLEH

Features

Showing features for sequence conflict.

TypeIDPosition(s)Description
Sequence conflict88in Ref. 1; AAA60948 and 2; BAA22998/BAA22999
Sequence conflict191in Ref. 1; AAA60948
Sequence conflict238in Ref. 2; BAA22998/BAA22999
Sequence conflict260in Ref. 1; AAA60948 and 2; BAA22998/BAA22999
Sequence conflict362in Ref. 1; AAA60948 and 2; BAA22998/BAA22999
Sequence conflict404in Ref. 2; BAA22998/BAA22999
Sequence conflict420in Ref. 1; AAA60948 and 2; BAA22998/BAA22999

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

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