Animals depend on light from their external environment to provide information for physiological functions such as vision, photoentrainment of circadian and circannual rhythms, photoperiodism, and background adaptation. Animals have a variety of photoreceptor cells that perform these functions, not only in the retina but also in other tissues, including brain tissue. In these cells, opsins function as universal photoreceptive proteins responsible for both visual and nonvisual photoreception. All opsins identified thus far bind either 11-cis or all-trans retinal as a chromophore and are classified into several groups based on their amino acid sequences. Opn5 forms an independent group that has diversified among vertebrate species. Most mammals only have one Opn5 gene, Opn5m, while nonmammalian vertebrates have two additional Opn5 subtypes, Opn5L1 and Opn5L2. Among these subtypes, Opn5m and Opn5L2 are UV-sensitive pigments in the dark. UV irradiation converts them into the visible light-sensitive active state, which converts back to the dark state by visible light irradiation. Opn5m and Opn5L2 therefore behave as bistable pigments. By contrast, Opn5L1 exclusively binds all-trans retinal to form the active state in the dark. Opn5L1 is converted to the resting state by light irradiation and subsequently reverts to the active state by a thermal process. Thus, Opn5L1 is categorized as a unique reverse photoreceptor whose activity is regulated by its photocyclic reaction. In this review, I introduce the diversity of molecular properties that have been described for vertebrate Opn5 subtypes and their physiological relevance.
Keywords: Opn5; Photoreceptive protein; Retinal; Rhodopsin.