Abstract: In order to understand the structural characteristics and protein function of α-actin protein ACTA1 gene in Asiatic black bear（Ursus thibetanus）, the α-actin protein ACTA1 gene was amplified by PCR from the total DNA and RNA in the muscle tissue of the Asian black bear, and its gene and sequence were cloned and sequenced. ORF finder software was used to find the ORF of DNA sequence and to infer the amino acid sequence. Gen scan was used to analyze the structural gene sequences. The gene coding sequence and amino acid sequence were compared by DNAMAN Version 6.0 software. The genetic relationship was compared by using MEGA 7.0 software. The functional sites and biochemical characteristics of proteins were predicted and analyzed by using ExPASy software. The results showed that the ORF of ACTA1 gene of Asiatic black bear was 1 134 bp, encoding 377 amino acids. The isoelectric point of ACTA1 protein was 5.24, the molecular weight was 42 ku, with 1 N-glycosylation site, 10 N-myristoylation sites, 5 protein kinase C phosphorylation sites, 2 tyrosine kinase phosphorylation sites, 4 casein kinase II phosphorylation sites, and 1 cAMP-and cGMP-dependent protein kinase phosphorylation site. The homology of ACTA1 gene coding sequence between Asian black bears and Polar bears was the highest, reaching 86.1%. ACTA1 protein was relatively conservative, which had high hydrophilicity and more helix structure, and had binding sites of transmememal helix and polynucleotide. It indicated that ACTA1 gene was highly conserved in evolution, ACTA1 protein had a variety of macro and micro biological functions, and participated in the signal transduction process, which played an important role in growth, development, biological regulation and repair of Asiatic black bear.