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Three-dimensional structure of bovine rhodopsin. The seven transmembrane domains are shown in varying colors. The chromophore is shown in red.

Opsins are a group of light-sensitive proteins 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 image-forming.

Opsin classification[edit]

Opsins can be classified in any of several ways, including function (vision, phototaxis, photoperiodism, etc.), type of chromophore (retinal, flavine, bilin), molecular structure (tertiary, quaternary), signal output (phosphorylation, reduction, oxidation), etc.[1]

There are two groups of protein termed opsins.[2][3] type I opsins are employed by prokaryotes and - as the protein component of channelrhodopsins - by some algae, whereas animals use type II opsins. No opsins have been found outside these groups (for instance in plants, fungi, or placozoans).[2]

At one time it was thought that type I and type II were related because of structural and functional similarities. With the advent of genetic sequencing it became apparent that sequence identity was no greater than could be accounted for by random chance. However, in recent years new methods have been developed specific to deep phylogeny. As a result, several studies have found evidence of a possible phylogenetic relationship. [4] [5] [6]

Type I opsins[edit]

Like type II opsins, type I opsins have a seven transmembrane domain structure similar to that found in eukaryotic G-protein coupled receptors.

Type I opsins (also known as microbial opsins) are found in all three domains of life: Archaea, Bacteria, and Eukaryota. In Eukaryota, type I opsins are found mainly in unicellular organisms such as green algae, and in fungi. In most complex multicellular eukaryotes, type I opsins have been replaced with other light-sensitive molecules such as cryptochrome and phytochrome in plants, and type II opins in Metazoa (animals).[7]

Microbial opsins are often known by the rhodopsin form of the molecule, i.e., rhodopsin (in the broad sense) = opsin + chromophore. Among the many kinds of microbial opsins are the proton pumps bacteriorhodopsin (BR) and xanthorhodopsin (xR), the chloride pump halorhodopsin (HR) the photosensors sensory rhodopsin I (SRI) and sensory rhodopsin II (SRII), as well as proteorhodopsin (PR), Neurospora opsin I (NOPI), Chlamydomonas sensory rhodopsins A (CSRA), Chlamydomonas sensory rhodopsins B (CSRB), channelrhodopsin (ChR), archaerhodopsin (Arch), xanthorhodopsin, and archaerhodopsin.[8]

Several type I opsins, such as proteo- and bacteriorhodopsin, are used by various bacterial groups to harvest energy from light to carry out metabolic processes using a non-chlorophyll-based pathway. Beside that, halorhodopsins of Halobacteria and channelrhodopsins of some algae, e.g. Volvox, serve them as light-gated ion channels, amongst others also for phototactic purposes. Sensory rhodopsins exist in Halobacteria that induce a phototactic response by interacting with transducer membrane-embedded proteins that have no relation to G proteins.[9]

Type II opsins[edit]

Type II opsins (or animal opsins) are seven-transmembrane proteins (35–55 kDa) belonging to the G protein-coupled receptor (GPCR) superfamily.[10]

Based on the phylogeny of their sequences, type II opsins can be grouped into six families; these families are very distinct, with under 20% of their sequences shared with any other subfamily. The families consist of the vertebrate opsins/encephalopsins; Go opsins; Gs opsins; invertebrate Gq opsins; the photoisomerases (RGR) and neuropsins.[11]These subfamilies can be grouped according to their expression; the first three are found in ciliary-type photoreceptor cells; Gq opsins in rhabdomeric-type photoreceptor cells; and the latter two are found elsewhere but based on their shared intron positions can be bundled together into the photoisomerases.[11]

Ciliary opsins[edit]

Ciliary opsins are expressed in ciliary photoreceptor cells, and include the vertebrate opsins/encephalopsins, Go and Gs opsin subfamilies.[11] They convert light signals to nerve impulses via cyclic nucleotide gated ion channels, which work by increasing the charge differential across the cell membrane (i.e. hyperpolarization.[2])

Vertebrate opsins[edit]

Vertebrate opsins can be further subdivided into rod opsins and four types of cone opsin, based on differential spatial expression, spectral sensitivity, and evolutionary history.[11] Rod opsins (rhodopsins, usually denoted Rh), are used in night vision, are thermally stable, and are found in the rod photoreceptor cells. Cone opsins, employed in color vision, are less-stable opsins located in the cone photoreceptor cells. Cone opsins are further subdivided according to their absorption maxima (λmax), the wavelength at which the highest light absorption is observed. Evolutionary relationships, deduced using the amino acid sequence of the opsins, are also frequently used to categorize cone opsins into their respective group. Both methods predict four general cone opsin groups in addition to rhodopsin.[12]

Humans have the following set of photoreceptor proteins responsible for vision:

  • Rhodopsin (Rh1, OPN2, RHO) – expressed in rod cells, used in night vision
  • Three cone opsins (also known as photopsins) – expressed in cone cells, used in color vision
    • Long Wavelength Sensitive (OPN1LW) Opsin – λmax of 560 nm, in the yellow-green region of the electromagnetic spectrum.[13] May be called the "red opsin", "L opsin" or "LWS opsin." Note that despite its common name as the "red" opsin, this opsin's peak sensitivity is not in the red region of the spectrum. However, it is more sensitive to red than the other two human opsins.[14] This receptor also has a secondary response in the violet high frequencies[15][16]
    • Middle Wavelength Sensitive (OPN1MW) Opsin – λmax of 530 nm, in the green region of the electromagnetic spectrum.[13] May be called the "green opsin", "M opsin" or "MWS opsin."
    • Short Wavelength Sensitive (OPN1SW) Opsin – λmax of 430 nm, in the blue region of the electromagnetic spectrum.[13] May be called the "blue opsin", "S opsin" or "SWS opsin."


This type of opsin is expressed throughout the mammalian heart

It is also expressed in ciliary photoreceptor cells in annelids, and in the brains of some insects.[11]

Go opsins[edit]

Go opsins are absent from higher vertebrates[17] and ecdysozoans.[18] They are found in the ciliary photoreceptor cells of the scallop eye[19] and the basal chordate amphioxus.[20] In Platynereis dumerilii however, a Go opsin is expressed in the rhabdomeric photoreceptor cells of the eyes.[21]

Gs opsins[edit]

Gs opsins have only been found in cnidarians.[11]

Rhabdomeric opsins[edit]

Arthropods and molluscs use Gq opsins. Arthropods appear to attain colour vision in a similar fashion to the vertebrates, by the use of three (or more) distinct groups of opsin, distinct both in terms of phylogeny and spectral sensitivity.[11] The Gq opsin melanopsin is also expressed in vertebrates, where it is responsible for the maintenance of circadian rhythms.[11]

Unlike ciliary opsins, these 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).[2]

The identification of the crystal structure of squid rhodopsin[22] is likely to further our understanding of its function in this group.

Arthropods do use different opsins in their different eye types, but at least in Limulus the opsins expressed in lateral and in compound eyes are 99% identical and presumably diverged recently.[23]


This class of opsins are not coupled to a G-protein, and thus serve to traffic retinal around in response to light, rather than directly in signal-induction.[11]


These opsins are found in nervous tissue in mammals, and despite some genetic similarities to photoisomerases, their function has not yet been identified.[11]

Name Gene Notes
Melanopsin OPN4 best studied novel opsin involved in circadian rhythms and pupillary reflex
Pineal Opsin (Pinopsin)[24] wide range of expression in the brain, most notably in the pineal region
Vertebrate Ancient (VA) opsin[25] has three isoforms VA short (VAS), VA medium (VAM), and VA long (VAL). It is expressed in the inner retina, within the horizontal and amacrine cells, as well as the pineal organ and habenular region of the brain
Parapinopsin (PP) Opsin [26]
Extraretinal (or extra-ocular) Rhodopsin-Like Opsins (Exo-Rh)[27] Rhodopsin-like protein expressed in the pineal region
Encephalopsin or Panopsin OPN3 originally found in human and mice tissue with a very wide range of expression (brain, testes, heart, liver, kidney, skeletal muscle, lung, pancreas and retina)
Teleost Multiple Tissue (TMT) Opsin[28] Teleost fish opsin with a wide range of expression
Peropsin or "Retinal pigment epithelium-derived rhodopsin homolog" RRH expressed in the retinal pigment epithelium (RPE) cells
Retinal G protein coupled receptor RGR expressed in the retinal pigment epithelium (RPE) and Müller cells
Neuropsin OPN5

Structure and function[edit]

Opsin proteins covalently bind to a vitamin A-based retinaldehyde chromophore through a Schiff base linkage to a lysine residue in the seventh transmembrane alpha helix. In vertebrates, the chromophore is either 11-cis-retinal (A1) or 11-cis-3,4-didehydroretinal (A2) and is found in the retinal binding pocket of the opsin. The absorption of a photon of light results in the photoisomerization of the chromophore from the 11-cis to an all-trans conformation. The photoisomerization induces a conformational change in the opsin protein, causing the activation of the phototransduction cascade. The opsin remains insensitive to light in the trans form. It is regenerated by the replacement of the all-trans retinal by a newly synthesized 11-cis-retinal provided from the retinal epithelial cells. Opsins are functional while bound to either chromophore, with A2-bound opsin λmax being at a longer wavelength than A1-bound opsin.

Opsins contain seven transmembrane α-helical domains connected by three extra-cellular and three cytoplasmic loops. Many amino acid residues, termed functionally conserved residues, are highly conserved between all opsin groups, indicative of important functional roles. All residue positions discussed henceforth are relative to the 348 amino acid bovine rhodopsin crystallized by Palczewski et al.[29] Lys296 is conserved in all known opsins and serves as the site for the Schiff base linkage with the chromophore. Cys138 and Cys110 form a highly conserved disulfide bridge. Glu113 serves as the counterion, stabilizing the protonation of the Schiff linkage between Lys296 and the chromophore. The Glu134-Arg135-Tyr136 is another highly conserved motif, involved in the propagation of the transduction signal once a photon has been absorbed.

Certain amino acid residues, termed spectral tuning sites, have a strong effect on λmax values. Using site-directed mutagenesis, it is possible to selectively mutate these residues and investigate the resulting changes in light absorption properties of the opsin. It is important to differentiate spectral tuning sites, residues that affect the wavelength at which the opsin absorbs light, from functionally conserved sites, residues important for the proper functioning of the opsin. They are not mutually exclusive, but, for practical reasons, it is easier to investigate spectral tuning sites that do not affect opsin functionality. For a comprehensive review of spectral tuning sites see Yokoyama[30] and Deeb.[31] The impact of spectral tuning sites on λmax differs between different opsin groups and between opsin groups of different species.

See also[edit]

External links[edit]


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  3. ^ Fernald, R. D. (2006). "Casting a genetic light on the evolution of eyes" (PDF). Science 313 (5795): 1914–1918. Bibcode:2006Sci...313.1914F. doi:10.1126/science.1127889. PMID 17008522. 
  4. ^ Shen, Libing; Chen, Chao; Zheng, Hongxiang; Jin, Li (2013). "The Evolutionary Relationship between Microbial Rhodopsins and Metazoan Rhodopsins". The Scientific World Journal 2013: 1–10. doi:10.1155/2013/435651. ISSN 1537-744X. 
  5. ^ Devine, E. L.; Oprian, D. D.; Theobald, D. L. (2013). "Relocating the active-site lysine in rhodopsin and implications for evolution of retinylidene proteins". Proceedings of the National Academy of Sciences 110 (33): 13351–13355. doi:10.1073/pnas.1306826110. ISSN 0027-8424. 
  6. ^ Zhang, Zaichao; Wu, Jiayan; Xiao, Jingfa; Zhang, Zhewen; Zhao, Yongbing; Jin, Zhong; Li, Rujiao (2014). "Systematic study on G-protein couple receptor prototypes: did they really evolve from prokaryotic genes?". IET Systems Biology 8 (4): 154–161. doi:10.1049/iet-syb.2013.0037. ISSN 1751-8849. 
  7. ^ Yoshizawa, S.; Kumagai, Y.; Kim, H.; Ogura, Y.; Hayashi, T.; Iwasaki, W.; DeLong, E. F.; Kogure, K. (2014). "Functional characterization of flavobacteria rhodopsins reveals a unique class of light-driven chloride pump in bacteria". Proceedings of the National Academy of Sciences 111 (18): 6732–6737. doi:10.1073/pnas.1403051111. ISSN 0027-8424. 
  8. ^ Grote, Mathias; Engelhard, Martin; Hegemann, Peter (2014). "Of ion pumps, sensors and channels — Perspectives on microbial rhodopsins between science and history". Biochimica et Biophysica Acta (BBA) - Bioenergetics 1837 (5): 533–545. doi:10.1016/j.bbabio.2013.08.006. ISSN 0005-2728. 
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  13. ^ a b c (http://faculty.oxy.edu/clint/physio/article/Themachineryofcolourvision.pdf)
  14. ^ http://faculty.oxy.edu/clint/physio/article/Themachineryofcolourvision.pdf
  15. ^ Mathpages http://www.mathpages.com/home/kmath579/kmath579.htm
  16. ^ .University of California excerpts from "Theory of Color"
  17. ^ Porter, Megan L.; Blasic, Joseph R.; Bok, Michael J.; Cameron, Evan G.; Pringle, Thomas; Cronin, Thomas W.; Robinson, Phyllis R. (19 October 2011). "Shedding new light on opsin evolution". Proceedings of the Royal Society B. doi:10.1098/rspb.2011.1819. PMID 22012981. Retrieved 9 November 2011. 
  18. ^ Hering, Lars; Mayer, Georg (4 September 2014). "Analysis of the Opsin Repertoire in the Tardigrade Hypsibius dujardini Provides Insights into the Evolution of Opsin Genes in Panarthropoda". Genome Biology and Evolution 6 (9): 2380–2391. doi:10.1093/gbe/evu193. PMID 25193307. Retrieved 15 September 2015. 
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