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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1985 Jun;82(11):3819–3823. doi: 10.1073/pnas.82.11.3819

Isolation and characterization of mouse Thy-1 genomic clones.

H C Chang, T Seki, T Moriuchi, J Silver
PMCID: PMC397879  PMID: 2582427

Abstract

The mouse Thy-1.2 gene was isolated from a C57Bl/6 cosmid library and its nucleotide sequence was determined from an 8-kilobase-long EcoRI fragment. The predicted amino acid sequence indicates that the mouse Thy-1 molecule contains a 19 amino acid leader peptide and the 112 amino acids reported previously from protein sequence analysis, plus 31 extra amino acids at the carboxyl terminus. These 31 amino acids contain a stretch of 20 amino acids, at positions 124-143, which is highly hydrophobic. RNA transfer blot analysis of RNA from mouse tissues indicates that the sequence coding for these 31 amino acids is present on poly(A)-containing RNA of brain and thymus tissues. This hydrophobic segment very likely provides the basis for integration of Thy-1 within the plasma membrane. The entire coding sequence of Thy-1 is distributed among three exons, encoding amino acid residues -19 to 8, -7 to 106, and 107 to 143, respectively. Comparison of the mouse and rat Thy-1 genes shows that both have a similar gene organization and encode a highly conserved transmembrane segment.

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Selected References

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