Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope.

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Citation

Mitsumoto Y, Oka S, Sakuma H, Inazawa J, Kawasaki T

Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope.

Genomics. 2000 Apr 15;65(2):166-73.

PubMed ID
10783264 [ View in PubMed
]
Abstract

The HNK-1 carbohydrate is expressed on various cell adhesion molecules in the nervous system and is suggested to play a role in cell-cell and cell-substrate interactions. Here we describe the isolation of a cDNA encoding human glucuronyltransferase (GlcAT-P), which is a key enzyme in the biosynthesis of the HNK-1 carbohydrate. The primary structure deduced from the cDNA sequence predicted a type II transmembrane protein of 334 amino acids. Human GlcAT-P was 98.2% identical with rat GlcAT-P in amino acid sequence, the exception being the length of the cytoplasmic tail. Northern blot analysis indicated that human GlcAT-P is expressed mainly in the brain. There is a single copy of the human GlcAT-P gene (HGMW-approved symbol B3GAT1), and it was mapped to chromosome 11q25.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1Q9P2W7Details