Characterization of the human homolog of the rat MRC OX-2 membrane glycoprotein

• Published in: Immunogenetics (New York) 1987-01, Vol.25 (5), p.329-335
• Main Authors: McCaughan, G W, Clark, M J, Barclay, A N
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Antigens, CD; Antigens, Surface - genetics; Base Sequence; DNA Restriction Enzymes; Exons; Genes; Glycoproteins - genetics; Humans; Membrane Proteins - genetics; Rats; Sequence Homology, Nucleic Acid
• ISSN: 0093-7711; 1432-1211
• DOI: 10.1007/bf00404426

The MRC OX-2 antigen is a membrane glycoprotein present on rat thymocytes, neurons, follicular dendritic cells, endothelium, and some smooth muscle. The sequence of 248 amino acids has similarities to Ig domains organized with one V-like domain, one C-like domain, and transmembrane and cytoplasmic regions. Thus it resembles a T-cell receptor chain but shows no sequence divergence. We report the characterization of the human gene for this molecule. Its exon organization is similar to that found for immunoglobulins although the region with similarities to Ig J regions is found within the same exon as the V-like domain. Human MRC OX-2 is expressed at the mRNA level in brain and B-cell lines but not detected in liver or T-cell lines. It does not obviously correspond to any previously defined leukocyte antigen. The sequence homology for the human and rat MRC OX-2 molecules is higher for the Ig-related region (75%) than for many other Ig-related molecules and very high in the transmembrane region (96%), implying a functional role other than simply its anchoring into the membrane.