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Information on EC 2.4.1.122 - N-acetylgalactosaminide beta-1,3-galactosyltransferase and Organism(s) Mus musculus and UniProt Accession Q9JJ06

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IUBMB Comments
The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
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Mus musculus
UNIPROT: Q9JJ06
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
galactosyltransferase, c1galt1, t-synthase, beta-galactosyltransferase, c1galt, core 1 synthase, dc1galt1, core 1 beta3-gal-t, ce-t-synthase, core 1 beta3-gal-transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
T-synthase
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core 1 beta1,3-galactosyltransferase
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galactosyltransferase, uridine diphosphogalactose-mucin beta-(1-3)-
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T-synthase
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uridine diphosphogalactose-mucin beta-(1-3)-galactosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
UDP-alpha-D-galactose:N-acetyl-alpha-D-galactosaminyl-R beta-1,3-galactosyltransferase (configuration-inverting)
The eukaryotic enzyme can act on non-reducing O-serine-linked N-acetylgalactosamine residues in mucin glycoproteins, forming the T-antigen. The bacterial enzyme, found in some pathogenic strains, is involved in biosynthesis of the O-antigen repeating unit.
CAS REGISTRY NUMBER
COMMENTARY hide
97089-61-7
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + N-acetyl-alpha-D-galactosaminyl-R
UDP + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-galactose + N-acetyl-alpha-D-galactosaminyl-R
UDP + beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-galactosaminyl-R
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
the double mutant (DM) mouse generates oocytes lacking complex N- and O-glycans due to oocyte-specific deletion of core 1 beta1,3-galactosyltransferase (C1galt1) and N-acetylglucosaminyltransferase I (Mgat1) and has modified cumulus expansion. Oocyte-specific ablation of C1galt1 and Mgat1 may affect bone morphogenetic protein 15 synthesis or bioactivity, thereby reducing SMAD1/5/8 phosphorylation and hyaluronan production. The genotype of the DM mouse is oocyte-specific. Cumulus-oocyte complexes (COCs) from mice with oocyte-specific deletions of C1galt1 and Mgat1 have abnormal cumulus matrix that is resistant to hyaluronidase treatment
physiological function
T-synthase is required for the generation of complex O-glycans. The O-glycosylation has been implicated in receptor signalling and cell-matrix interactions
malfunction
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oocyte-specific deletion at the primary follicle stage of T-synthase leads to a sustained increase in fertility mutant females ovulated 30-50% more eggs and has a sustained increase in litter size compared to controls, ovarian weights and follicle numbers are greater in mutants, but follicular apoptosis is not decreased, the number of follicles entering the growing pool is unaltered, but 3-week mutants ovulate fewer eggs, suggesting that increased fertility results from prolonged follicle development, T-synthase mutant ovaries also contain numerous multiple-oocyte follicles that appeared to form by adjacent, predominantly preantral, follicles joining
physiological function
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T-synthase generates core 1-derived O-glycans
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
C1GLT_MOUSE
363
1
42304
Swiss-Prot
Secretory Pathway (Reliability: 1)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination
generation of mutant mice, oocyte-specific deletion of T-synthase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ju, T.; Brewer, K.; D'Souza, A.; Cummings, R.D.; Canfield, W.M.
Cloning and expression of human core 1 beta1,3-galactosyltransferase
J. Biol. Chem.
277
178-186
2002
Caenorhabditis elegans (Q18515), Caenorhabditis elegans, Rattus norvegicus (Q9JJ05), Mus musculus (Q9JJ06), Mus musculus, Homo sapiens (Q9NS00), Homo sapiens
Manually annotated by BRENDA team
Williams, S.A.; Stanley, P.
Mouse fertility is enhanced by oocyte-specific loss of core 1-derived O-glycans
FASEB J.
22
2273-2284
2008
Mus musculus
Manually annotated by BRENDA team
Lo, B.K.M.; Archibong-Omon, A.; Ploutarchou, P.; Day, A.J.; Milner, C.M.; Williams, S.A.
Oocyte-specific ablation of N- and O-glycans alters cumulus cell signalling and extracellular matrix composition
Reprod. Fertil. Dev.
31
529-537
2019
Mus musculus (Q9JJ06), Mus musculus
Manually annotated by BRENDA team