When light enters the eye, it is focused on the retina and detected by rod and cone photoreceptors. The photoreceptors translate the light information into electrical impulses that travel through the synapses with bipolar neurons, then into ganglion cells, and along the optic nerve into the brain. Rods represent 97% of all photoreceptors in the human or mouse retina and are used for night vision. Cones represent the other 3% of all photoreceptors but are used the majority of the time for seeing in daylight, detecting colors, and providing high acuity vision. In order to prevent blindness it is necessary to investigate the molecular mechanisms of how rods and cones are different. One difference is that rods have a synapse in the shape of the spherule but cones have a much larger synapse in the shape of a pedicle which allows these cells to communicate with many more neurons in the retina. In this study, we tested if rod and cone synapses express the same proteins. Since cones are sparse in the wild type (WT) mouse retina we also used a mutant strain called “conefull”. Western blotting and immunohistochemistry (IHC) experiments were performed to detect the following synaptic proteins: RIM1, RIM2, SCAMP, CAST, VAMP2, Complexin 3 and Proton ATPase. By Western blotting, all of these synaptic proteins were found in both WT and conefull retinas. By IHC, all of the synaptic proteins tested in this study were found in the outer synaptic layer in both WT and conefull mice. It is therefore possible that therapies designed to improve photoreceptor synaptic function will work for both rods and cones, i.e. day and night vision.