A full length cDNA of a vacuolar H⁺PPase gene (named ThVP1) was isolated from the transcriptome cDNA librarys of Tamarix hispida. ThVP1 was 3 022 bp in length, including an open reading frame of 2 298 bp which was predicted to encode a polypeptide of 765 amino acids. The estimated molecular weight and isoelectric points of the putative protein were 80.37 kD and 5.25, respectively. Hydrophobicity analysis and transmembrane domain prediction indicated that the ThVP1 contained 13 potential transmembrane domains with strong hydrophobicity. The amino acids sequence of ThVP1 contains three conservative domains (CS1, CS2 and CS3)，which shows 93% identities in amino acids sequence to vacuolar H⁺PPase genes from Reaumuria trigyna. Phylogenetic analysis indicates that ThVP1 belongs to class I type vacuolar H⁺PPase gene. Quantitative realtime PCR assay revealed that the mRNA level of ThVP1 was significantly upregulated by more than 20 fold higher than that of control under NaCl and PEG treatments in Tamarix hispida, suggesting that ThVP1 might play an important role in salt and drought tolerance of T. hispida.