title: A novel human glycosyltransferase: primary structure and characterization of the gene and transcripts.
abstract: We report the identification and primary structure of a novel human glycosyltransferase, B3GTL (beta3-glycosyltransferase-like). The 498 residue protein consists of a short cytoplasmic N-terminal "tail" (residues 1-4), a single transmembrane domain with type II topology (residues 5-28), a "stem" region (residues 29-260), and a catalytic domain (residues 261-498). The genomes of Anopheles gambiae, Drosophila melanogaster, and Caenorhabditis elegans encode potential orthologs which share 31-39% sequence identity with B3GTL, as well as the following features: a conserved catalytic domain containing a triple aspartate motif (DDD) at its core, a conserved pattern of cysteine residues, a C-terminal KDEL-like motif, and conserved residues and motifs that affiliate this novel group with a family of beta3-glycosyltransferases (GT31 in the CAZY classification). The B3GTL gene lacks canonical TATA and CAAT boxes and contains three functional polyadenylation sites. It is transcribed in a wide range of tissues and in TGF-beta-treated T84 epithelial cells.
authors.affiliation: Paediatric Research Centre, University of Tampere Medical School and Tampere University Hospital, Tampere, Finland. taisto.heinonen@uta.fi
authors.forename: Taisto Y K
authors.initials: TY
authors.lastname: Heinonen
authors.forename: Leena
authors.initials: L
authors.lastname: Pasternack
authors.forename: Katri
authors.initials: K
authors.lastname: Lindfors
authors.forename: Christelle
authors.initials: C
authors.lastname: Breton
authors.forename: Louis N
authors.initials: LN
authors.lastname: Gastinel
authors.forename: Markku
authors.initials: M
authors.lastname: Mäki
authors.forename: Heikki
authors.initials: H
authors.lastname: Kainulainen
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D000818:Animals; D000852:Anopheles / Q000235:genetics; D001483:Base Sequence; D015152:Blotting, Northern; D017173:Caenorhabditis elegans / Q000235:genetics; D020134:Catalytic Domain; D018076:DNA, Complementary / Q000378:metabolism; D004331:Drosophila melanogaster / Q000235:genetics; D005700:Galactosyltransferases; D005964:Glucosyltransferases; D016695:Glycosyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000235:genetics*; D006801:Humans; D008969:Molecular Sequence Data; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D020133:Reverse Transcriptase Polymerase Chain Reaction; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D014018:Tissue Distribution
chemical_list: D018076:DNA, Complementary; D012333:RNA, Messenger; D016695:Glycosyltransferases; C514116:B3GLCT protein, human; D005700:Galactosyltransferases; D005964:Glucosyltransferases