China Animal Husbandry and Veterinary Medicine ›› 2021, Vol. 48 ›› Issue (11): 4047-4054.doi: 10.16431/j.cnki.1671-7236.2021.11.014

• Genetics and Breeding • Previous Articles     Next Articles

Cloning and Bioinformatics Analysis of XCL1 Gene CDS in Gushi Chicken

TIAN Huihui1, DING Mengxia2, GUO Yujie1, SU Aru1, SUN Guirong1, TIAN Yadong1, JIANG Ruirui1, HAN Ruili1, KANG Xiangtao1, YAN Fengbin2   

  1. 1. College of Animal Science and Technology, Henan Agricultural University, Zhengzhou 450002, China;
    2. College of Veterinary Medicine, Henan Agricultural University, Zhengzhou 450002, China
  • Received:2021-04-25 Online:2021-11-20 Published:2021-11-01

Abstract: The aim of this study was to clone the CDS region of lymphotactin (XCL1) gene in chicken and explore its biological characteristics. Using the total RNA of thymus tissue in Gushi chicken as the template, the CDS of the gene was amplified by RT-PCR and cloned, and the related bioinformatics analysis was carried out by bioinformatics software. The results showed that XCL1 gene CDS in Gushi chicken was 294 bp in length and encoded 97 amino acids. The homology analysis showed that the homology of XCL1 gene CDS sequence in chicken with Bos taurus, Capra hircus, Ovis aries, Homo sapiens, Mus musculus, Sus scrofa and Rattus norvegicus were 53.7%, 53.0%, 52.9%, 51.8%, 51.1%, 50.9% and 50.4%, respectively. The results of phylogenetic tree showed that chicken was a non mammal, and XCL1 gene was far from mammalian. The molecular formula of the XCL1 encoded protein was C491H822N150O132S6, the theoretical isoelectric point was 10.95, which was a basic protein. The molecular mass was 11.13 ku, the fat coefficient was 102.37, and the instability coefficient was 51.44, which was an unstable protein, and the half-life was 30 h. It had a transmembrane structure (amino acids 5-27) and a signal peptide region (amino acids 1-18), and was a hydrophilic secreted protein. There were 8 potential phosphorylation modification sites and 3 potential glycosylation modification sites in XCL1 protein. The secondary structure of XCL1 protein was composed of alpha helix (35.05%), beta turn (5.15%), extended chain (26.80%) and random coil (32.99%). The tertiary structure prediction was consistent with the secondary structure. Subcellular localization analysis showed that XCL1 protein mainly functions outside the cell;the protein had a conserved SCY domain at amino acid residues 31-88. The protein could form an interaction network with OXT, PTAFR, GPR132 and XCR1. The results of this experiment provided a theoretical reference for further study of XCL1 gene function in chicken.

Key words: Gushi chicken; XCL1 gene; cloning; bioinformatics analysis

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