Aim To elucidate the role of the motifs in the cytoplasmic domain of scavenger receptor A (SR-A). Methods A SR-A DNA mutant (SR-AΔ_ 1-27) was constructed by truncating the 1 to 27 amino acid residues of the N-terminal cytoplasmic domain. SR-A and SR-A_ Δ1-27 were transfected into CHO cells by Lipofectamine 2000. Western blot, laser confocal microscopy, flow cytometry and cell adhesion assay were used additionally. Results Compared with SR-A, expression of the SR-A_ Δ1-27 was increased and amount of cell-associated Dil-labeled ac-LDL in SR-A_ Δ1-27 expressing cells were almost reduced 80%. SR-A_ Δ1-27 was able to assemble in the plasma membrane and cytoplasm. SR-A_ Δ1-27 could bind its lipoprotein ligands but decline to internalize the bound ligands greatly. Incited by Ac-LDL, SR-A_ Δ1-27 located not only in membrane and plasma, but also in the nuclear. The SR-A_ Δ1-27 display decreased adhesion. Conclusion The 1 to 27 amino acid residues of the N-terminal cytoplasmic domain mediate SR-A expresssion and location, lipid uptake and cell adhesion