Abstract: The 3′ end cDNA sequence and amino acid sequence of the FTH (ferritin) gene from Chinese Holstein cattle was cloned and analyzed to provide a theoretical basis for functional studies and its effective utilization. The 3′ end cDNA was cloned from liver tissues by rapid amplification of cDNA ends (RACE), and the bioinformatics method was used to analyze the amino acid sequence. The 3′ end cDNA of the FTH gene was 489 bp and it encoded a peptide of 81 amino acids. Its relative molecular weight was 9.125 3 kD, isoelectric point was 5.19, fat index was 85.56, grand average of hydropathy was -0.342. N-terminal signal peptides and transmembrane domains were not included in this protein. The primary structure of the FTH protein contained four functional domains, and the secondary structure was mainly an α-helix with β-rotation. The results obtained through homologous sequencing indicated that the FTH of Chinese Holstein cattle had a high similarity to that of Bos taurus (99%), and the molecular evolution trees showed that the FTH of Chinese Holstein cattle had very low genetic relationships with other species studied in this research. These results provided clues for evolutionary studies of the FTH gene family, as well as serving as references for further functional analysis and utilization.