[Objectives]  To investigate the characteristics of uridine phosphorylase in the silkworm by cloning, prokaryotic expression, bioinformatics analysis, and thereby lay a foundation for elucidating the molecular mechanism of UPase in this economically important species. [Methods]  The CDS of BmUPase1 was cloned using Dazao cDNA and analyzed with bioinformatic software. The gene was then inserted into the prokaryotic expression vector pET28a to create a recombinant plasmid pET28a-BmUPase1, which was then transformed into Escherichia coli BL21 (DE3) to express BmUPase1. Real-time quantitative PCR was performed to profile the expression of the gene in different tissues and growth stages. [Results] Bioinformatics analysis showed that the BmUPase1 gene has an ORF of 1 188 bp and encodes 395 amino acids. BmUPase1 has one conserved domain, and its amino acid sequence identity is most similar to that of Spodoptera litura UPase (85.06 %). qPCR results indicate that the BmUPase1 gene is expressed in all tissues and growth stages, which suggests that it plays an important role in silkworm growth and development. The pET28a-BmUPase1 recombinant vector was successfully expressed in E. coli BL 21, and the expressed protein was of the predicted size. [Conclusion]  The silkworm Uridine phosphorylase gene can be successfully cloned and expressed. The results of this study lay a foundation for further study of the function of this gene in silkworm development.