English

Abstract

Pulmonary vascular remodeling (PVR) is the main characteristic lesion of ascites syndrome (AS) in broilers. JAZF1 plays an important role in PVR, but there is no study on its protein function and structure. In this study, the physical and chemical properties, hydrophilicity/hydrophobicity and transmembrane domain, phosphorylation site and glycosylation site, subcellular localization and signal peptide, secondary and tertiary structure, antigen peptide and conserved domain and phylogenetic relationship of JAZF1 protein were predicted online by bioinformatics tools. The results showed that the number of amino acids of JAZF1 was 243aa, the theoretical isoelectric point was 8.63, the instability index was 58.1, and the average coefficient of hydrophilicity was -0.674. It was found to be a hydrophilic protein having 35 phosphorylation sites and a N-glycosylation site with no transmembrane domain. The protein is expressed in the nucleus, there is no signal peptide distribution in the whole sequence and the secondary structure is mainly composed of random coil and α- helix. There were 7 B cell epitopes, 7 conserved domains and compared with other birds, JAZF1 is 95.61% similar. In summary, from the analysis we came to conclude that the amino acid sequence 64-80aa, 91-108aa, 136-151aa and 179-187aa can be selected as antigen sites and among which 136-151aa may be the best. This study lays a good foundation for follow-up experiments, which then provides powerful conditions for pathological detection of pulmonary vascular remodeling and gene drug therapy of ascites syndrome in broilers.