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Information on EC 2.4.1.41 - polypeptide N-acetylgalactosaminyltransferase and Organism(s) Sus scrofa and UniProt Accession Q29121
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EC Tree
2.4.1.41 polypeptide N-acetylgalactosaminyltransferaseIUBMB Comments
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
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Word Map
- 2.4.1.41
-
o-glycosylation
-
mucin-type
- mucin
- glycosyltransferase
- o-glycans
-
o-linked
- threonine
- gangliosides
- lectin
- calcinosis
- oligosaccharide
- metastasis
- calcification
-
hyperphosphatemic
- gm2
-
galactosyltransferase
- glycolipids
-
1,25-dihydroxyvitamin
-
phosphaturic
- gd1a
-
sialyltransferase
-
submaxillary
-
angptl3
-
mucin-like
- klotho
- hyperostosis
- muc5ac
-
factor-23
- apomucin
- analysis
- drug development
-
lutropin
-
asn-linked
- molecular biology
-
periarticular
- medicine
-
o-glycoproteins
- iga1
- villosa
The taxonomic range for the selected organisms is: Sus scrofa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
=
+
+
=
+
Synonyms
galnt3, n-acetylgalactosaminyltransferase, galnt2, galnac-t3, galnac-t, galnt14, galnac-transferase, galnac transferase, galnac-t2, galnac-t1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
acetylgalactosaminyltransferase, uridine diphosphoacetylgalactosamine-glycoprotein
-
-
-
-
GalNAc-transferase
-
-
-
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glycoprotein acetylgalactosaminyltransferase
-
-
-
-
polypeptide-N-acetylgalactosamine transferase
-
-
-
-
ppGalNAc-T
-
-
-
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ppGaNTase
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-
-
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protein-UDP acetylgalactosaminyltransferase
-
-
-
-
UDP-acetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
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-
-
-
UDP-acetylgalactosamine:peptide-N-galactosaminyltransferase
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-
-
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UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase
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-
-
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UDP-N-acetylgalactosamine-glycoprotein N-acetylgalactosaminyltransferase
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-
-
-
UDP-N-acetylgalactosamine-protein N-acetylgalactosaminyltransferase
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-
-
-
UDP-N-acetylgalactosamine:kappa-casein polypeptide N-acetylgalactosaminyltransferase
-
-
-
-
UDP-N-acetylgalactosamine:polypeptide N-acetylgalactosaminyltransferase
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-
-
-
UDP-N-acetylgalactosamine:protein N-acetylgalactosaminyl transferase
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-
-
-
uridine diphosphoacetylgalactosamine-glycoprotein acetylgalactosaminyltransferase
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-
-
-
UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyl-transferase
Requires both Mn2+ and Ca2+. The glycosyl residue is transferred to threonine or serine hydroxy groups on the polypeptide core of submaxillary mucin, kappa-casein, apofetuin and some other acceptors of high molecular mass.
CAS REGISTRY NUMBER
COMMENTARY
9075-15-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-alpha-D-galactosamine + deglycosylated human trachea mucin
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + deglycosylated swine trachea mucin
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Gln-Ala-Ala-Gly-Thr-Ser-Gly-Ala-Gly-Pro-Gly
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Ala-Ala-Ser-Ala-Ala-Pro-Leu-Arg
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Ala-Ser-Ser-Ser-Ala-Pro-Leu-Arg
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Pro-Pro-Asp-Val-Val-Ser-Val-Val-Pro-Leu-Arg
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Val-Leu-Gly-Thr-Thr-Ala-Val
?
-
-
-
-
?
UDP-N-acetyl-alpha-D-galactosamine + Val-Lys-Thr-Glu-Ala-Thr-Thr-Phe-Ile
?
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + HIV-V3 peptide
UDP + N-acetyl-D-galactosaminyl-HIV-V3 peptide
-
submaxillary gland enzyme, low activity
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
UDP-N-acetyl-D-galactosamine + myelin basic protein
UDP + N-acetyl-D-galactosaminyl-myelin basic protein
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
deglycosylated bovine submaxillary mucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
porcine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
ovine apomucin
-
-
?
UDP-N-acetyl-D-galactosamine + apomucin
UDP + N-acetyl-D-galactosaminyl-apomucin
-
deglycosylated Cowper's gland, swine and human trachea mucins
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
-
only Ser acceptor sites, with a very low activity
-
-
?
UDP-N-acetyl-D-galactosamine + human chorionic gonadotropin-beta peptide
UDP + N-acetyl-D-galactosaminyl-human chorionic gonadotropin-beta peptide
-
submaxillary gland enzyme
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
L-threonine specifically O-glycosylated in alpha-configuration, Thr-Pro-Pro-Pro-sequence requires a peptide length of five or more for significant acceptor activity
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
only UDP-GalNAc serves as sugar donor
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: synthetic polypeptides with sequences identical or similar to those found in porcine mucin or human erythropoietin, acceptor substrate specificity is dependent on the amino acid sequence adjacent to serine and threonine residues, but it is more sensitive to the sequence adjacent to serine than to threonine
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: bovine submaxillary mucin core protein, myelin basic protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
O-glycosylation of the polypeptide, acceptor: porcine stomach mucin
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: ovine and porcine apomucin, porcine mucin-like synthetic peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
O-glycosylating enzyme, acceptors: synthetic peptides in which the Thr-Pro-Pro-Pro sequence is varied
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptor: SIV3 peptide
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
transfer of GalNAc to a serine or threonine residue on the acceptor protein
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: deglycosylated Cowper's gland, swine and human trachea mucins, tryptic peptides prepared from them, best substrates are fragments of incompletely deglycosylated mucin polypeptide chains
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
specifically transfers N-acetylgalactosamine from UDP-GalNAc to the hydroxyl group of threonine, no transferase activity towards serine-containing peptides, amino acid sequence adjacent to glycosylated Thr residues may influence the rate of glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
acceptors: human mucin Muc1 and Muc2 peptides, human chorionic gonadotropin-beta peptide, HIV-V3 peptides
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
first step in biosynthesis of O-linked oligosaccharides in submaxillary gland
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
key role in overall control of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
additional information
?
-
-
different substrate specificities before and after Muc2 affinity chromatography of enzyme
-
-
?
additional information
?
-
-
not: UDP-glucuronate, UDP-xylose, GDP-mannose, GDP-fucose, intact mucins, desialylated mucins, glycolipid acceptors, including globoside and ceramide hexosides, no transfer of GalNAc to terminal sugar residues in oligosaccharide chains
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
-
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
catalyzes the first step in biosynthesis of O-linked oligosaccharides in many glycoproteins
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
first step in biosynthesis of O-linked oligosaccharides in submaxillary gland
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
key role in overall control of O-glycosylation
-
-
?
UDP-N-acetyl-D-galactosamine + polypeptide
UDP + N-acetyl-D-galactosaminyl-polypeptide
-
primary step in the production of mucin-type O-linked oligosaccharide groups in glycoproteins
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
-
no reactivation of metal-free enzyme by Mg2+, Zn2+ and Ca2+
Mn2+
-
metal-free enzyme is inactive, Mn2+ is the best activator, maximal activity at 5 mM, half-maximal activity at 0.4 mM MnCl2, 20 and 100 mM result in 10% and 80% inhibition
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
-
Mn2+ is the best activator, maximal activity at 5 mM, 20 and 100 mM result in 10% and 80% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
Km: 1.01 mg/ml: ovine apomucin, 2.54 mg/ml: porcine apomucin
-
additional information
additional information
-
Km: 0.83 mg/ml: deglycosylated Cowper's gland mucin, 1.12 mg/ml: deglycosylated human trachea mucin, 0.94 mg/ml: deglycosylated swine trachea mucin, values for several tryptic peptides derived from them
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 9.5
-
pH 4.5: no activity, pH 6.8: gradual decrease of activity below, pH 9.5: 16% of activity maximum
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
cis-Golgi apparatus and smooth-membraned vesicular structures in close topological relation with it
additional information
-
not in rough endoplasmic reticulum, its translational elements, smooth-membraned structures related to it and the trans Golgi apparatus, mucn droplets and the plasma membrane
-
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GALT1_PIG
559
1
64119
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
8 h, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 5% w/v glycerol, 40% loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 60% w/v glycerol, 1 year, stable
-
4°C, 20 mM imidazole-HCl, pH 7.2, 0.1% Triton X-100, 5 mM MnCl2, 25% w/v glycerol, 1 month, 10% loss of activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
affinity chromatography on deglycosylated Cowper's gland mucin bound to Sepharose, 12500fold
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Wang, Y.; Agrwal, N.; Eckhardt, A.E.; Stevens, R.D.; Hill, R.L.
The acceptor substrate specificity of porcine submaxillary UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase is dependent on the amino acid sequences adjacent to serine and threonine residues
J. Biol. Chem.
268
22979-22983
1993
Sus scrofa
Wang, Y.; Abernethy, J.L.; Eckhardt, A.E.; Hill, R.L.
Purification and characterization of a UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase specific for glycosylation of threonine residues
J. Biol. Chem.
267
12709-12716
1992
Sus scrofa
Hatanaka, K.; Slama, J.T.; Elbein, A.D.
Synthesis of a new inhibitor of the UDP-GalNAc:polypeptide galactosaminyl transferase
Biochem. Biophys. Res. Commun.
175
668-672
1991
Sus scrofa
Cottrell, J.M.; Hall, R.L.; Sturton, R.G.; Kent, P.W.
Polypeptide N-acetylgalactosaminyltransferase activity in tracheal epithelial microsomes
Biochem. J.
283
299-305
1992
Sus scrofa
Mendicino, J.; Sangadala, S.
Purification and characterization of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase from swine trachea epithelium
Mol. Cell. Biochem.
185
135-145
1998
Sus scrofa
Soerensen, T.; White, T.; Wandall, H.H.; Kristensen, A.K.; Roepstorff, P.; Clausen, H.
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase. Identification and separation of two distinct transferase activities
J. Biol. Chem.
270
24166-24173
1995
Homo sapiens, Ovis sp., Rattus norvegicus, Sus scrofa
Roth, J.; Wang, Y.; Eckhardt, A.E.; Hill, R.L.
Subcellular localization of the UDP-N-acetyl-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase-mediated O-glycosylation reaction in the submaxillary gland
Proc. Natl. Acad. Sci. USA
91
8935-8939
1994
Bos taurus, Sus scrofa
Yoshida, A.; Hara, T.; Ikenaga, H.; Takeuchi, M.
Cloning and expression of a porcine UDP-GalNAc:polypeptide N-acetylgalactosaminyl transferase
Glycoconj. J.
12
824-828
1995
Sus scrofa (Q29121)
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