We previously found that the dopamine D 3 receptor can be split at the third cytoplasmic loop into two fragments (D 3 t r u n k and D 3 t a i l ), and that the mixture of the two fragments retains the binding and functional activity of the wild type receptor. The dopamine D 3 receptor gene gives rise to several inactive receptor splice variants, one of which is the D 3 n f . Since this gene variant very closely resembles our D 3 t r u n k fragment, in this study we investigated if the transfection of D 3 n f with D 3 t a i l could result in the rescue of a functional dopamine receptor. Our experiments showed that D 3 t a i l can indeed rescue the activity of D 3 n f , and that the pharmacological profile of this split D 3 n f /D 3 t a i l receptor is identical to that of the wild type D 3 receptor.