Abstract: Transmembrane protein 68（TP68）is protein with unknown structure and function. In the present study，the coding cDNA sequence of mouse TP68 was cloned by reverse transcription PCR and analyzed by bioinformatical tools in detail. The results showed that the full length coding cDNA of mouse TP68 was 990 bp，which encoded 329 amino acids. Protein domain analysis indicated that mouse TP68 had a classical glycerophospholipid acyltransferase domain and two transmembrane domains，which may be an endoplasmic reticulum-anchored protein. Moreover，TP68 had classic substrate binding sites，catalytic active sites and spatial conformation of glycerophospholipid acyltransferases by sequence alignment and the 3-D modeling. These results for the first time identify the encoding cDNA sequence of mouse TP68 and provide the basis to further study its structure and function.