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Literature summary for 2.4.1.41 extracted from

  • Ten Hagen, K.G.; Bedi, G.S.; Tetaert, D.; Kingsley, P.D.; Hagen, F.K.; Balys, M.M.; Beres, T.M.; Degand, P.; Tabak, L.A.
    Cloning and characterization of a ninth member of the UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase family, ppGaNTase-T9 (2001), J. Biol. Chem., 276, 17395-17404.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene encoding ppGaNTase-T9 from sublingual gland is cloned, characterized, sequenced and expressed transiently in COS7 cells, gene encodes a unique 603-amino acid protein Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Mus musculus 16020
-
membrane ppGaNTase-T9: type II integral membrane protein with a 20-amino acid transmembrane domain, a 9-amino acid cytoplasmic domain and a 94-amino acid stem region Rattus norvegicus 16020
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-N-acetyl-D-galactosamine + polypeptide Rattus norvegicus diversely regulated ppGaNTase family may play a role in the various processes governing development UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide Mus musculus initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide Rattus norvegicus initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-
Rattus norvegicus Q925R7 ppGaNTase-T9
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
Mus musculus
-
brain ppGaNTase-T9, less amount Rattus norvegicus
-
colon
-
Mus musculus
-
colon ppGaNTase-T9 Rattus norvegicus
-
embryo embryonic day 14.5, ppGaNTase-T9 is expressed relatively abundantly compared with ppGaNTase-T7, accumulation in brain Mus musculus
-
heart
-
Mus musculus
-
heart ppGaNTase-T9, less amount Rattus norvegicus
-
lung
-
Mus musculus
-
lung ppGaNTase-T9, less amount Rattus norvegicus
-
ovary
-
Mus musculus
-
ovary ppGaNTase-T9 Rattus norvegicus
-
small intestine
-
Mus musculus
-
small intestine ppGaNTase-T9 Rattus norvegicus
-
spleen
-
Mus musculus
-
spleen ppGaNTase-T9, less amount Rattus norvegicus
-
stomach
-
Mus musculus
-
stomach ppGaNTase-T9, less amount Rattus norvegicus
-
sublingual gland
-
Mus musculus
-
sublingual gland ppGaNTase-T9 Rattus norvegicus
-
testis ppGaNTase-T9 Rattus norvegicus
-
uterine cervix
-
Mus musculus
-
uterine cervix ppGaNTase-T9, less amount Rattus norvegicus
-
uterus
-
Mus musculus
-
uterus ppGaNTase-T9, less amount Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information multiple enzyme isoforms Mus musculus ?
-
?
additional information multiple enzyme isoforms Rattus norvegicus ?
-
?
additional information 9 isoforms, ppGaNTase-T9 contains a 480-amino acid conserved region and shows no activity with non-glycosylated peptides Rattus norvegicus ?
-
?
UDP-N-acetyl-D-galactosamine + GalNAc-glycosylated peptide ppGaNTase-T9: acceptors are di- and triglycosylated MUC5AC and mono-glycosylated EA2, obtained by prior action of ppGaNTase-T1, but not the unmodified peptides, formation of a tetra-glycopeptide species from MUC5AC triglycopeptide substrate, ppGaNTase-T7 forms a hexa-glycopeptide species Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-GalNAc-glucosylated peptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
-
Mus musculus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide transfer of GalNAc to a serine or threonine residue on the acceptor protein Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide diversely regulated ppGaNTase family may play a role in the various processes governing development Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function Mus musculus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?
UDP-N-acetyl-D-galactosamine + polypeptide initiation of mucin-type O-glycosylation by a family of polypeptide GalNAc-transferases, of which each has a unique function Rattus norvegicus UDP + N-acetyl-D-galactosaminyl-polypeptide
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mus musculus
37
-
assay at Rattus norvegicus