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Symbol report for GALNT1

HGNC data for GALNT1

Approved symbol
GALNT1
Approved name

polypeptide N-acetylgalactosaminyltransferase 1

Locus type
gene with protein product
HGNC ID
HGNC:4123
Symbol status
Approved
Previous names
UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1)
Alias symbols
GalNAc-T1
Alias names
protein-UDP acetylgalactosaminyltransferase 1
polypeptide GalNAc transferase 1
Chromosomal location
18q12.2
Bos taurus
GALNT1 VGNC:29222 VGNC
Canis familiaris
GALNT1 VGNC:41084 VGNC
Equus caballus
GALNT1 VGNC:18222 VGNC
Felis catus
GALNT1 VGNC:62442 VGNC
Macaca mulatta
GALNT1 VGNC:72871 VGNC
Mus musculus
Galnt1 MGI:894693 Curated
Pan troglodytes
GALNT1 VGNC:14784 VGNC
Rattus norvegicus
Galnt1 RGD:620358
Sus scrofa
GALNT1 VGNC:97062 VGNC
Identification of two cysteine residues involved in the binding of UDP-GalNAc to UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 1 (GalNAc-T1).
Tenno M et al. Eur J Biochem 2002 Sep;269(17)4308-4316
Tenno M, Toba S, Kézdy FJ, Elhammer AP, Kurosaka A.
Eur J Biochem 2002 Sep;269(17)4308-4316
Abstract: Biosynthesis of mucin-type O-glycans is initiated by a family of UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferases, which contain several conserved cysteine residues among the isozymes. We found that a cysteine-specific reagent, p-chloromercuriphenylsulfonic acid (PCMPS), irreversibly inhibited one of the isozymes (GalNAc-T1). Presence of either UDP-GalNAc or UDP during PCMPS treatment protected GalNAc-T1 from inactivation, to the same extent. This suggests that GalNAc-T1 contains free cysteine residues interacting with the UDP moiety of the sugar donor. For the functional analysis of the cysteine residues, several conserved cysteine residues in GalNAc-T1 were mutated individually to alanine. All of the mutations except one resulted in complete inactivation or a drastic decrease in the activity, of the enzyme. We identified only Cys212 and Cys214, among the conserved cysteine residues in GalNAc-T1, as free cysteine residues, by cysteine-specific labeling of GalNAc-T1. To investigate the role of these two cysteine residues, we generated cysteine to serine mutants (C212S and C214S). The serine mutants were more active than the corresponding alanine mutants (C212A and C214A). Kinetic analysis demonstrated that the affinity of the serine-mutants for UDP-GalNAc was decreased, as compared to the wild type enzyme. The affinity for the acceptor apomucin, on the other hand, was essentially unaffected. The functional importance of the introduced serine residues was further demonstrated by the inhibition of all serine mutant enzymes with diisopropyl fluorophosphate. In addition, the serine mutants were more resistant to modification by PCMPS. Our results indicate that Cys212 and Cys214 are sites of PCMPS modification, and that these cysteine residues are involved in the interaction with the UDP moiety of UDP-GalNAc.
Purification and cDNA cloning of a human UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase.
White T et al. J Biol Chem 1995 Oct;270(41)24156-24165
White T, Bennett EP, Takio K, Sørensen T, Bonding N, Clausen H.
J Biol Chem 1995 Oct;270(41)24156-24165
Abstract: A UDP-GalNAc:polypeptide N-acetylgalactosaminyl-transferase (GalNAc-transferase) from human placenta was purified to apparent homogeneity using a synthetic acceptor peptide as affinity ligand. The purified GalNAc-transferase migrated as a single band with an approximate molecular weight of 52,000 by reducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Based on a partial amino acid sequence, the cDNA encoding the transferase was cloned and sequenced from a cDNA library of a human cancer cell line. The cDNA sequence has a 571-amino acid coding region indicating a protein of 64.7 kDa with a type II domain structure. The deduced protein sequence showed significant similarity to a recently cloned bovine polypeptide GalNAc-transferase (Homa, F.L., Hollanders, T., Lehman, D.J., Thomsen, D.R., and Elhammer, A.P. (1993) J. Biol. Chem. 268, 12609-12616). A polymerase chain reaction construct was expressed in insect cells using a baculovirus vector. Northern analysis of eight human tissues differed clearly from that of the bovine GalNAc-transferase. Polymerase chain reaction cloning and sequencing of the human version of the bovine transferase are presented, and 98% similarity at the amino acid level was found. The data suggest that the purified human GalNAc-transferase is a novel member of a family of polypeptide GalNAc-transferases, and a nomenclature GalNAc-T1 and GalNAc-T2 is introduced to distinguish the members.