Abstract: In order to clone the coding region of myosin light chain 1（MYL1） gene and analyze it bioinformatics.Specific primers were designed according to the mRNA sequence of boar MYL1 gene published on GenBank in NCBI website（registration number: NM₂14374.2）. PCR was performed on the encoding region of Tibetan pig MYL1 gene using cDNA reverse transcription of total RNA extracted from Longissimus dorsi tissue as template.Target purpose gene was sequenced, and Tibetan pig MYL1 gene coding sequence homology, protein structure and function（amino acids, the general physical and chemical properties, hydrophobicity and secondary structure and tertiary structure, phosphorylation sites, transmembrane helical structure and subcellular localization signal peptide and protein interactions） was analyzed by using bioinformatics analysis software.The results showed that the full length of MYL1 gene sequence was 453 bp.The Tibetan pig had the closest genetic relationship with wild boar and the farthest with zebrafish.The nucleotide sequences of MYL1 gene of Tibetan pig were 100%, 92.1%, 91.4%, 91.2%, 91.2%, 90.5%, 90.3%, 89.2%, 80.6% and 68.2%, similar to those of wild boar, ox, Homo sapiens, horse, sheep, dog, cave rabbit, house rat, chicken and zebrafish, respectively.There were 19 kinds of amino acids in the coding region of Tibetan pig MYL1 gene, which was composed of 150 amino acids.The molecular weight of Tibetan pig MYL1 protein was 16 657.86 u, the molecular formula is C₇₂₈H₁₁₅₃N₁₉₃O₂₃₅S₉, the fat coefficient was 79.33, the theoretical isoelectric point pI was 4.63, the instability coefficient is 37.81, and the total number of negatively charged amino acid residues（Asp + Glu） was 26.The total number of positively charged amino acid residues（Arg + Lys） was 15, and the theoretical half-life was 30 h.MYL1 protein was a hydrophilic protein.The proportion of α helix was the largest（58.67%）, followed by random curl（24.67%）, β rotation（8.67%） and extended chain（8.00%）.The predicted results of tertiary structure and secondary structure agree well.There were 16 phosphorylation sites in amino acid sequence, including eight serine phosphorylation sites, six threonine phosphorylation sites and two tyrosine phosphorylation sites.It had no transmembrane helix structure and was a non-transmembrane protein; no signal peptide, non-secretory protein; mainly located in the cytoplasm（47.8%）, in the nucleus about 26.1%, in the cytoskeleton about 8.3%, in the endoplasmic reticulum, golgi apparatus, secretory system vesicles, vacuoles about 4.3%.There was an interaction network relationship with TNNC2 protein, MYH1 protein, MYH3 protein, MYH7 protein, and the correlation coefficient with TNNC2 protein was 0.999, the correlation coefficient with myosin heavy chain family MYH1 protein, MYH3 protein, MYH7 protein was 0.979, 0.975 and 0.971, respectively.The correlation coefficient between MYBPC1 protein and TPM1 protein was 0.969.The correlation coefficient between MYL1 protein and TPM2 protein and TNNI3 protein was 0.965.These results suggest that MYL1 gene of Tibetan pigs may have strong biological functions.