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Sequence and Mapping of Galectin-5, a β-Galactoside-binding Lectin, Found in Rat Erythrocytes (∗)

A monomeric rat β-galactoside-binding lectin previously purified from extracts of rat lung has been localized to erythrocytes, and the cDNA encoding it has been isolated from a rat reticulocyte cDNA library. The deduced amino acid sequence of the cDNA predicts a protein with a Mr of 16,199, with no...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-03, Vol.270 (10), p.5032-5038
Main Authors: Gitt, Michael A., Wiser, Mark F., Leffler, Hakon, Herrmann, Joerg, Xia, Yu-Rong, Massa, Stephen M., Cooper, Douglas N.W., Lusis, Aldons J., Barondes, Samuel H.
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Language:English
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Summary:A monomeric rat β-galactoside-binding lectin previously purified from extracts of rat lung has been localized to erythrocytes, and the cDNA encoding it has been isolated from a rat reticulocyte cDNA library. The deduced amino acid sequence of the cDNA predicts a protein with a Mr of 16,199, with no evidence of a signal peptide. The deduced sequence is identical to the sequences of seven proteolytic peptides derived from the purified lectin. Peptide analysis by mass spectrometry indicates that the N-terminal methionine is cleaved and that serine 2 is acetylated. The lectin shares all the strictly conserved amino acid residues of other members of the mammalian galectin family and is designated galectin-5 (GenBankTM accession number L36862). Galectin-5 is a weak agglutinin of rat erythrocytes, despite its monomeric structure. The gene encoding galectin-5 (LGALS5) has been mapped in mouse to chromosome 11, ∼50 centimorgans from the centromere and 1.8 ± 1.8 centimorgans from the polymorphic marker D11Mit34n, a region syntenic with human chromosome 17q11.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.10.5032