Characteristics Analysis of Bovine HSPA6 Protein and Construction of Protein Interaction Network

In this study, a phylogenetic tree was constructed using bovine heat shock protein A6 (HSPA6) sequences and those of other organisms, and bioinformatic methods were used to analyze the basic physicochemical properties and hydrophilicity of bovine HSPA6 protein. Meanwhile, a protein interaction network was constructed to investigate the structural and functional properties of the protein encoded by the HSPA6 gene. The results showed that bovine HSPA6 protein had high similarity in amino acid sequence with those of sheep, Yangtze finless porpoise and other mammals. The molecular mass of bovine HSPA6 protein was 70570.64 u, the theoretical isoelectric point was 5.66, and it was an acidic hydrophilic protein without transmembrane structure or signal peptide. Bovine HSPA6 protein may have 11 phosphorylation sites with score greater than 0.900 and N-glycosylation sites at the terminal bases, and it was a relatively stable protein with a secondary structure consisting mainly of 40.38% α-helix and 33.65% random coil, containing two major structural domains, the N-terminal nucleotide-binding domain and the C-terminal peptide-binding domain, which played a role in the cytoplasm. The constructed protein network showed that bovine HSPA6 protein mainly interacted with BAG1, DNAJA4, DNAJB1 and DNAJC2, and was involved in the activity of adenylate exchange factors, ATPase activity and chaperone binding, indicating that the HSPA6 protein exerted a potential function in biological processes such as energy metabolism in the bovine organism. These multiple bioinformatic analyses provide a theoretical basis for an in-depth investigation of the mechanism of the effect of bovine HSPA6 protein on meat quality.