Characterization and Structural Properties of Glycam1 Gene of Some Domestic Animals

Abstract

Nevien M. Sabry, Tarek A. A. Moussa

Glycosylation-dependent cell adhesion molecule 1 (Glycam1) gene is sulfated glycoprotein that appears to mediate the adhesion of leukocyte-endothelial cells. In this study Glycam1 was characterized in Bos taurus, Bubalus bubalis, Ovis aries, Equus caballus and Sus scrofa. Glycam1 gene was amplified from DNA and mRNA samples revealed that different lengths. The coding region of Glycam1 gene is divided into four exons and three introns. Translation the coding region reported the presence of 154 amino acids for both of O. aries and S. scrofa, 153 amino acids in B. bubalis, B. taurus and E. caballus. Glycam1 peptide was unstable, heat stable and the GRAV was negative, so the peptide was hydrophilic. The domain position was 19-154 in O. aries and S. scrofa, 19-153 in B. bubalis and E. caballus and 19-152 in B. taurus. The peptide contained many O-linked glycosylation sits with rich in Ser sites. The helices constitute 69.9-82.4% of the secondary structure of the five animals, where strand units were 15.5-33.3%. The Glycam1 peptide are folded in 2-5 helical unites and 5-7 loops in their mucin domain. The fourth helical peptide in B. bubalis, B. taurus and E. caballus, the third in S. scrofa and the second in O. aries were the longest (115-143, 115-143, 117-137, 116-144 and 116-144, respectively). The Glycam1 gene is characterized by four exons and three introns with very short exon II.