Abstract: To obtain the cDNA sequence of sweet cherry PaGAST gene and predict the structure and functions of the corresponding protein, PaGAST gene was cloned by electronic cloning technology based on EST sequences from NCBI databases using strawberry FaGAST1 gene sequence as a probe. The bioinformatics methods were utilized to analyze the physical and chemical properties, hydrophobicity and hydrophilicity, signal peptide sequence, transmembrane domain, subcellular localization, functions and other relevant characteristics of the corresponding protein. The results showed that sweet cherry PaGAST gene was 750 bp in length, and its open reading frame was 324 bp long, encoding a polypeptide of 107 amino acids with a signal peptide sequence in the N-terminal and a conserved GASA domain in the C-terminal. Because of high content of hydrophobic amino acid residues among peptide sequences, the PaGAST protein contained a transmembrane helical region, which meant it was a transmembrane protein with 10 presumed protein kinase phosphorylation sites. Subcellular localization analysis showed that the PaGAST protein was very likely to be localized outside the cell membrane. Functional prediction revealed that PaGAST gene had the greatest probability in participation of stress response, signal transduction and immune response. Phylogenetic analysis indicated that sweet cherry PaGAST protein was most closely related to peach. The results above lay a theoretical foundation for the cloning and functional identification of sweet cherry PaGAST gene to some extent.