[Objectives]  To clone the cDNA sequence of the Carposina sasakii CSP14 gene, CsasCSP14, determine its expression profiles in different tissues of both sexes, and its molecular docking with host volatiles, and thereby lay a foundation for the future study of the physiological function of this gene. [Methods]  The full-length cDNA sequence of CsasCSP14 was cloned from body tissues of C. sasakii by PCR. The expression levels of CsasCSP14 mRNA in different tissues (antennae, head, thorax, abdomen, legs and wings) were detected by real-time PCR. Modeller software (version-9.19) was used to build a three-dimensional model of CsasCSP14 and Autodock 4.2 was then used to dock this model to 32 apple plant volatiles and 2 sex pheromones. [Results]  The open reading frame (ORF) of the full-length cDNA sequence of CsasCSP14 obtained using real-time PCR was 369 bp long, encoding a protein of 122 aa with an estimated molecular weight 14.13 ku and a pI of 5.20. The encoded protein has a signal peptide, no transmembrane structure, a CSP superfamily domain between residues 18-122 and contains four conserved cysteins and 6 α-helixes. The results of amino acid sequence alignment indicate that CsasCSP14 is homologous to OfurCSP13 with 86% amino acid sequence identify. Furthermore, the results of real-time PCR show that CsasCSP14 transcripts are differentially expressed in the antennae, head, thorax, abdomen, legs and wings of male and female adults. The highest expression of CsasCSP14 was in the antennae of adult males and females. Modeller was used to compare the sequence of CsasCSP14 with those of previously characterized proteins in the Protein Data Bank (PDB). CsasCSP14 shares 65.03% similarity with S. gregaria CSPsg4; the 3D structure of CSPsg4 was used as the template for the 3D structure of CsasCSP14. [Conclusion]  The results of molecular docking simulation indicate that 2-Hexenal, Undecanolactone, Butyl-acetate, Heptanal, 3-Methylbutanal and Farnesene have relatively low binding energies with CsasCSP14. However, the hydrophobic amino acid resides Leu-22, Phe-29, Phe-42 and Ile-46, interact with all CsasCSP14 ligands. These results provide a theoretical basis for further research on the binding of CsasCSP14 to host plant volatiles, and thereby facilitate the development of new methods of controlling C. sasakii.