Molecular cloning, expression pattern and chromosomal mapping of pig CD9 antigen.

CD9 is a member of the transmembrane-4 superfamily of surface molecules that seems to have a relevant role in cell migration and adhesion, as well as malignant progression. This work describes the isolation of the cDNA coding for the porcine CD9 molecule. Pig CD9 cDNA was isolated from a smooth muscle cDNA library and contains a 678-bp open reading frame with its predicted polypeptide sequence of 226 amino acids. The deduced amino acid sequence conserves the main characteristics of TM4 proteins, including the presence of four transmembrane domains. Like their homologous molecules from other species, pig CD9 has two extracellular regions of a different size with the minor loop bearing two possible glycosylation sites. The pig CD9 gene was localized to chromosome 5q25 by using a somatic cell hybrid panel. Analysis of CD9 expression in different porcine cells and tissues demonstrated that CD9 mRNA is ubiquitously expressed.