›› 2013, Vol. 40 ›› Issue (8): 20-25.

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Bioinformatics Analysis of Porcine Oviduct-specific Glycoprotein Structure and Function

LIU Chun-ying1, LI Fang-zheng2   

  1. 1. Life Science Department, Qingdao Agricultural University, Qingdao 266109, China;
    2. College of Animal Science and Technology, Qingdao Agricultural University, Qingdao 266109, China
  • Received:2013-03-29 Online:2013-08-20 Published:2013-08-16

Abstract: Lasergene,Protscale,SOPMA,Mega and ScanProsite were used to study the structure, conservation and phylogeny of porcine oviduct-specific glycoprotein (OGP). The results showed that the full length of porcine OGP contained a complete open read coding of 1581 bp, which encoded 527 amino acids. The porcine OGP had obvious signal peptide and it was a secretion protein, it was no obvious hydrophobic region. The secondary structures were mainly composed of α-helix and random coli. Phylogenetic tree analysis of the amino acids sequences showed that the porcine OGP displayed nearest relationship with the sheep OGP, and lower homology with those of bovine. The OGP was a member of glycosyl hydrolase 18 family (GH18). The GH18 domain structure of OGP had high differences between bovine and porcine.

Key words: porcine; oviduct-specific glycoprotein (OGP); bioinformatics

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