melanopsin no relation color vision
Animal opsins are G-protein-coupled receptors and a group of proteins made light-sensitive via a chromophore, typically retinal. When bound to retinal, opsins become Retinylidene proteins, but are usually still called opsins regardless. Most prominently, they are found in photoreceptor cells of the retina. Five classical groups of opsins are involved in vision, mediating the conversion of a photon of light into an electrochemical signal, the first step in the visual transduction cascade. Another opsin found in the mammalian retina, melanopsin, is involved in circadian rhythms and pupillary reflex but not in vision. Humans have in total nine opsins. Beside vision and light perception, opsins may also sense temperature, sound, or chemicals.Vertebrate visual opsins
Vertebrate visual opsins are a subclass of ciliary opsins that express in the vertebrate retina and mediate vision. They are further subdivided into:Parietopsins
The first parietopsin was found in the photoreceptor cells of the lizard parietal eye. The lizard parietopsin is green-sensitive (λmax = 522 nm), and despite it is a c-opsin, like the vertebrate visual opsins, it does not induce hyperpolarization via a Gt-protein, but induces depolarization via a Go-protein.Encephalopsin or Panopsin
The panopsins are found in many tissues (skin, brain, testes, heart, liver, kidney, skeletal muscle, lung, pancreas and retina). They were originally found in the human and mouse brain and thus called encephalopsin.The first invertebrate panopsin was found in the ciliary photoreceptor cells of the annelid Platynereis dumerilii and is called c(iliary)-opsin. This c-opsin is UV-sensitive (λmax = 383 nm) and can be tuned by 125 nm at a single amino-acid (range λmax = 377 - 502 nm). Thus, not unsurprisingly, a second but cyan sensitive c-opsin (λmax = 490 nm) exists in Platynereis dumerilii. The first c-opsin mediates in the larva UV induced gravitaxis. The gravitaxis forms with phototaxis a ratio-chromatic depth-gauge. In different depths, the light in water is composed of different wavelengths: First the red (> 600 nm) and the UV and violet (< 420 nm) wavelengths disappear. The higher the depth the narrower the spectrum so that only cyan light (480 nm) is left. Thus, the larvae can determine their depth by color. The color unlike brightness stays almost constant independent of time of day or the weather, for instance if it is cloudy.Panopsins are also expressed in the brains of some insects. The panopsins of mosquito and pufferfish absorb maximally at 500 nm and 460 nm, respectively. Both activate in vitro Gi and Go proteins.The panopsins are sister to the TMT-opsins.Rhabdomeric opsins
Rhabdomeric opsins (rhabopsins, r-opsins) are also known as Gq-opsins, because they couple to a Gq-protein. Rhabopsins are used by molluscs and arthropods. Arthropods appear to attain colour vision in a similar fashion to the vertebrates, by using three (or more) distinct groups of opsins, distinct both in terms of phylogeny and spectral sensitivity.  The rhabopsin melanopsin is also expressed in vertebrates, where it regulates circadian rhythms and mediates the pupillary reflex.Unlike cilopsins, rhabopsins are associated with canonical transient receptor potential ion channels; these lead to the electric potential difference across a cell membrane being eradicated (i.e. depolarization).The identification of the crystal structure of squid rhodopsin is likely to further our understanding of its function in this group.
Arthropods use different opsins in their different eye types, but at least in Limulus the opsins expressed in the lateral and the compound eyes are 99% identical and presumably diverged recently.Melanopsin
Melanopsin (OPN4) is involved in circadian rhythms, the pupillary reflex, and color correction in high-brightness situations. Phylogenetically, it is a member of the rhabdomeric opsins (rhabopsins, r-opsins) and functionally and structurally a rhabopsin, but does not occur in rhabdomeres.
no relation