The outer segment (OS) of rod photoreceptors consist of a highly modified primary cilium containing phototransduction machinery necessary for light detection. The delivery and organization of the phototransduction components within and along the cilium into the series of stacked, highly organized disks is critical for cell function and viability. How disks are formed within the cilium remains an area of active investigation. We have found nuclear distribution protein C (nudC), a key component of mitosis and cytokinesis during development, to be present in the inner segment region of these postmitotic cells in several species, including mouse, tree shrew, monkey, and frog. Further, we found nudC interacts with rhodopsin and the small GTPase rab11a. Here, we show through transgenic tadpole studies that nudC is integral to rod cell disk formation and photoreceptor protein localization. Finally, we demonstrate that short hairpin RNA knockdown of nudC in tadpole rod photoreceptors, which leads to the inability of rod cells to maintain their OS, is rescued through coexpression of murine nudC.-Boitet, E. R., Reish, N. J., Hubbard, M. G., Gross, A. K. NudC regulates photoreceptor disk morphogenesis and rhodopsin localization.