China Animal Husbandry and Veterinary Medicine ›› 2020, Vol. 47 ›› Issue (3): 706-713.doi: 10.16431/j.cnki.1671-7236.2020.03.007

• Biotechnology • Previous Articles     Next Articles

Characterization Analysis of HSPA6 Protein in Goat and Construction of Interactive Protein Network

YANG Jiadong, LIU Yueqin, ZHANG Yingjie   

  1. College of Animal Science and Technology, Hebei Agricultural University, Baoding 071001, China
  • Received:2019-09-16 Online:2020-03-20 Published:2020-03-17

Abstract: In order to investigate the structure and functional characteristics of HSPA6 belongs to heat shock protein 70 family in goat,the amino acid composition,physical and chemical properties,hydrophobicity,transmembrane structure,signal peptide,possible phosphorylation modification sites,subcellular localization,secondary structure and tertiary structure of HSPA6 were analyzed using bioinformatic methods.HSP70 protein sequences of various organisms were selected to construct phylogenetic tree,at the same time,the protein interaction network was analyzed.The results showed that HSPA6 in goat had higher homology sequences with mammalian (cattle,pig);the molecular weight of HSPA6 protein in goat was 70.9 ku;The isoelectric point was about 5.78,which indicated it belonged to acidic protein and hydrophilic protein;Without transmembrane structure and signal peptide.There were 10 phosphorylation sites with high scores,which located in N-terminal(nucleotide binding domain,NBD) and C-terminal (peptide binding domain,PBD),and C-terminal contains EEVD motif,which was the conserved motif of HSP70 family proteins located in the cytoplasm,indicating that it was mainly distributed in cytoplasm.The secondary structure of protein was mainly composed of α-helix (41.52%) and random coil (33.75%).The construction of protein interaction network indicated that HSPA6 might interact with HSP70 family members,and might play a role in the formation of complex with HSP40 and HSP90 in cells.Based on the above,this study provided a theoretical basis for further exploring the functional mechanism of HSPA6 in goat in response to environmental stress.

Key words: goat; heat shock protein 70; HSPA6; bioinformatics

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