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

Authors

  • Yue Ma Email 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
Received: 7 June 2021 | Published Online: 3 August 2021

Abstract

In order to adapt to the low temperature environment, organisms transmit
excitement to the central system through the thermal sensing system, which
is a classic reflex reaction. The cold receptor GLR-3 perceives cold and pro
duces cold avoidance behavior through peripheral sensory neurons ASER.
In order to further understand the gene encoding of the cold sensing glr-3
gene and the evolution of its homologous gene group function and protein
function, the nucleotide sequence and amino acid sequence of the glr-3
gene and its homologous gene in 24 species were obtained and compared.
By clustering with the GRIK2 gene sequence of Rana chensinensis, the bio
informatics method was used to predict and sequence analyze the change of
gene, evolution rate, physical and chemical properties of protein, glycosyla
tion sites, phosphorylation sites, secondary structure and tertiary structure
of protein. The analysis results show that the glr-3 gene and its homologous
gene have obvious positive selection effect. The protein prediction analysis
showed that the glr-3 gene and its homologous genes encoded proteins
in these 25 species were hydrophilic proteins, and the proportion of side
chains of aliphatic amino acids was high. The transmembrane helix was
widespread and there were more N-glycosylation sites and O-glycosylation
sites. The protein phosphorylation sites encoded were serine, threonine and
tyrosine phosphorylation sites. Secondary structure prediction showed that
the 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 larg
est. This study provides useful information on the evolution and function of
the cold sensing gene glr-3 and its homologous genes.

Keywords:

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

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2021 Vol.3 No.3

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Copyright © 2021 Yue Ma, Tiantian Guo, Yihe Wang, Xinna Li, Jingyu Zhang

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