Clustering and Differentiation of glr-3 Gene Function and Its Homologous Proteins

Authors

  • Yue Ma College of Wildlife and Protected Area, Northeast Forestry University, Harbin, 150040, China
  • Tiantian Guo College of Wildlife and Protected Area, Northeast Forestry University, Harbin, 150040, China
  • Yihe Wang College of Wildlife and Protected Area, Northeast Forestry University, Harbin, 150040, China
  • Xinna Li College of Wildlife and Protected Area, Northeast Forestry University, Harbin, 150040, China
  • Jingyu Zhang College of Wildlife and Protected Area, Northeast Forestry University, Harbin, 150040, China

DOI:

https://doi.org/10.30564/jzr.v3i3.3337

Abstract

In order to adapt to the low temperature environment, organisms transmitexcitement to the central system through the thermal sensing system, whichis a classic reflex reaction. The cold receptor GLR-3 perceives cold and produces cold avoidance behavior through peripheral sensory neurons ASER.In order to further understand the gene encoding of the cold sensing glr-3gene and the evolution of its homologous gene group function and proteinfunction, the nucleotide sequence and amino acid sequence of the glr-3gene and its homologous gene in 24 species were obtained and compared.By clustering with the GRIK2 gene sequence of Rana chensinensis, the bioinformatics method was used to predict and sequence analyze the change ofgene, evolution rate, physical and chemical properties of protein, glycosylation sites, phosphorylation sites, secondary structure and tertiary structureof protein. The analysis results show that the glr-3 gene and its homologousgene have obvious positive selection effect. The protein prediction analysisshowed that the glr-3 gene and its homologous genes encoded proteinsin these 25 species were hydrophilic proteins, and the proportion of sidechains of aliphatic amino acids was high. The transmembrane helix waswidespread and there were more N-glycosylation sites and O-glycosylationsites. The protein phosphorylation sites encoded were serine, threonine andtyrosine phosphorylation sites. Secondary structure prediction showed thatthe secondary structure units of the encoded protein were α-helix, β-turn,random coil and extended chain, and the proportion of α-helix was the largest. This study provides useful information on the evolution and function ofthe cold sensing gene glr-3 and its homologous genes.

Keywords:

glr-3 gene; Homology; Low temperature; Maximum likelihood

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Vol. 3 , Iss. 3 (July 2021)

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