Genomic Analysis of Intrinsically Disordered Proteins in the Genus Camelus

Int J Mol Sci. 2020 Jun 3;21(11):4010. doi: 10.3390/ijms21114010.

Abstract

Intrinsically disordered proteins/regions (IDPs/IDRs) fail to fold completely into 3D structures, but have major roles in determining protein function. While natively disordered proteins/regions have been found to fulfill a wide variety of primary cellular roles, the functions of many disordered proteins in numerous species remain to be uncovered. Here, we perform the first large-scale study of IDPs/IDRs in the genus Camelus, one of the most important mammalians in Asia and North Africa, in order to explore the biological roles of these proteins. The study includes the prediction of disordered proteins/regions in Camelus species and in humans using multiple state-of-the-art prediction tools. Additionally, we provide a comparative analysis of Camelus and Homo sapiens IDPs/IDRs for the sake of highlighting the distinctive use of disorder in each genus. Our findings indicate that the human proteome is more disordered than the Camelus proteome. Gene Ontology analysis also revealed that Camelus IDPs are enriched in glutathione catabolism and lactose biosynthesis.

Keywords: Camelus; GO; disorder prediction; disoredered proteins.

Publication types

  • Comparative Study

MeSH terms

  • Animals
  • Camelus*
  • Computational Biology
  • Genome
  • Genomics*
  • Humans
  • Intrinsically Disordered Proteins / chemistry
  • Intrinsically Disordered Proteins / genetics*
  • Protein Conformation
  • Proteome / metabolism
  • Proteomics
  • Species Specificity

Substances

  • Intrinsically Disordered Proteins
  • Proteome