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Wikipedia article
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. 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.

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

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.

Ciliary
Ciliary opsins are expressed in ciliary photoreceptor cells, and include the vertebrate opsins/encephalopsins, Go and Gs opsin subfamilies. 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. )

Vertebrate visual opsins
Vertebrates typically have four cone opsins (LWS, SWS1, SWS2, and Rh2) inherited from the first vertebrate (and thus predating the first vertebrate), as well as the rod opsin, rhodopsin (Rh1), which emerged after the first vertebrate but before the first Gnathostome (jawed vertebrate). These five opsins emerged through a series of gene duplications beginning with LWS and ending with Rh1. Each one has since evolved into numerous variants and thus constitutes an opsin subtype.

C-type opsins (ciliary)

 * vertebrate visual pigments (LWS/MWS, SWS1, SWS2, Rh2, Rh1)
 * pinopsins
 * parapinopsins
 * vertebrate ancient opsin (VA)
 * parietal opsins
 * OPN3 / encephalopsins (panopsin) / teleost multiple tissue opsins (TMTs)

Cnidops (Cnidarian)

 * Cndiarian Gs-coupled

R-type opsins (Rhabdomeric) / Gq-coupled

 * arthropod visual pigments (M/LWS, SWS)
 * annelid, platyhelminthes and mollusc visual pigments
 * OPN4 / vertebrate melanopsins 1 and 2

Go/RGR (Group 4) Opsins

 * Go-coupled
 * RGR / retinal G-protein coupled receptor
 * peropsins
 * OPN5 / Gi-coupled / neuropsins

Encephalopsins
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.

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

Gs opsins
Gs opsins have only been found in cnidarians.

Rhabdomeric opsins
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. The Gq opsin melanopsin is also expressed in vertebrates, where it is responsible for the maintenance of circadian rhythms. 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).

The identification of the crystal structure of squid rhodopsin 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.

Photoisomerases
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.

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

Cladogram 2
retinal photoisomerases | retinochrome/retinal G protein-coupled receptor (RGR)

R-type

Group 4 (Go-RGR)

C-type

Cnidarian opsin

‘r-type’ group are found in rhabdomeric photoreceptors (as in the eyes of arthropods and cephalopods) ‘c-type’ opsins are found in ciliary photoreceptors (e.g. vertebrate rods and cones) the cnidarian opsins (‘Cnidops’) ‘retinal G-protein coupled receptors’ (RGR), peropsins and neuropsins

(i) the ‘C-type opsins’ (ii) the ‘Cnidops’ (iii) the ‘R-type opsins’ (iv) Group 4 Opsins (Gr4)

4 families
Type II opsins fall phylogenetically into four groups: C-opsins (Ciliary), Cnidops (cnidarian opsins), R-opsins (rhabdomeric), and Go/RGR (also known as RGR/Go or Group 4). Go/RGR is divided into four sub-clades: Go, RGR, peropsins, and neuropsins. C-opsins, R-opsins, and the Go/RGR group are found only in Bilateria.

C-type opsins

group 1.1:
 * vertebrate visual pigments (Rh1, Rh2, SWS1, SWS2, M/LWS)
 * pinopsins (pineal opsins, P-opsins)
 * parapinopsins (pineal, parapineal))
 * vertebrate ancient VA) opsin and parietal opsins

group 1.2:
 * teleost multiple tissue opsins (TMTs)
 * encephalopsins
 * uncharacterized amphioxus and urchin opsins

group 1.3:
 * honeybee ptersopsin
 * uncharacterized insect and Daphnia pulex opsins

group 1.4:
 * uncharacterized Platynereis brain and urchin opsins

Cnidops
 * Ctenophore and cndiarian opsins, including representatives from hydrozoans, anthozoans and cubozoans.

R-type opsins

group 3.1:
 * arthropod visual pigments (M/LWS, SWS)

group 3.2:
 * annelid, platyhelminthes and mollusc visual pigments

group 3.3:
 * vertebrate melanopsins 1 and 2
 * amphioxus sequences

group 3.4
 * uncharacterized tunicate
 * amphioxus and mollusc opsins.

Group 4 Opsins

group 4.1:
 * four separate clades of neuropsins, and amphioxus and urchin opsins

group 4.2:
 * amphioxus, echinoderm and scallop opsins

group 4.3:
 * RGR and uncharacterized mollusc opsins

group 4.4:
 * peropsins
 * amphioxus and hemichordate opsins

Cladogram 4.5
after Portel et al

after Liegertova, et al

after Feuda et al

Cladogram 5
The phylogenetic positions of opsins found in Cnidaria (jellyfish, etc.) and Ctenophora (comb jellies) are disputed. Some scholars. Placopsin, an opsin-like molecule found in Placozoa, is sister clade to the type 2 opsins. Melatonin receptor (MTR) is sister clade to placopsin+type ii opsins.

Fungi
"a rhodopsin in the chytridiomycete Allomyces reticulatus evidently guides phototaxis of its zoospores"

"The fungus Allomyces reticulatus forms swimming zoospores and has been suggested to use rhodopsin-mediated signaling to initiate phototaxis."

A Rhodopsin-Guanylyl Cyclase Gene Fusion Functions in Visual Perception in a Fungus

Wiki Article
There are two groups of protein termed opsins. 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).

type i & type ii opsin list
"Plants originated via a primary endosymbiotic event between a biciliate protozoan host and a cyanobacterium, the ancestor of chloroplasts. Following the origin of chloroplasts, plants diverged into three lineages, glaucophyte algae (Glaucophyta), red algae (Rhodophyta) and green algae+land plants (Viridaeplantae). Of the three lineages, pelagic phototaxis is only present in green plants."

Gáspár Jékely

Evolution of phototaxis

Type II opsins have been found in:

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

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.

Dinoflagellate eye
Hayakawa

Function and Evolutionary Origin of Unicellular Camera-Type Eye Structure