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The sequence of rat leukosialin (W3/13 antigen) reveals a molecule with O‐linked glycosylation of one third of its extracellular amino acids.
Author(s) -
Killeen N.,
Barclay A. N.,
Willis A. C.,
Williams A. F.
Publication year - 1987
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1987.tb02747.x
Subject(s) - biology , glycosylation , sequence (biology) , extracellular , peptide sequence , n linked glycosylation , antigen , biochemistry , genetics , microbiology and biotechnology , glycan , glycoprotein , gene
Leukosialin is one of the major glycoproteins of thymocytes and T lymphocytes and is notable for a very high content of O‐linked carbohydrate structures. The full protein sequence for rat leukosialin as translated from cDNA clones is now reported. The molecule contains 371 amino acids with 224 residues outside the cell, one transmembrane sequence and 124 cytoplasmic residues. Data from the peptide sequence and carbohydrate composition suggest that one in three of the extracellular amino acids may be O‐glycosylated with no N‐linked glycosylation sites. The cDNA sequence contained a CpG rich region in the 3′ coding sequence and a large 3′ non‐coding region which included tandem repeats of the sequence GGAT.