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HighlightsIntroduction of OPN4
OPN4 is a type of photopigment belonging to a larger family of light-sensitive retinal proteins called opsins and encoded by the gene Opn4. In the mammalian retina, there are two additional opsins, both involved in the formation of visual images: rhodopsin and photopsin (types I, II, and III) in the rod and cone photoreceptor cells, respectively. OPN4, like all other animal opsins (e.g. rhodopsin), is a member of the G-protein coupled receptor (GPCR) family. The OPN4 protein has seven alpha helices integrated into the plasma membrane, an N-terminal domain, and a C-terminal domain.
| Basic Information of OPN4 | |
| Protein Name | Melanopsin |
| Gene Name | OPN4 |
| Aliases | Melanopsin, Opsin-4 |
| Organism | Homo sapiens (Human) |
| UniProt ID | Q9UHM6 |
| Transmembrane Times | 7 |
| Length (aa) | 478 |
| Sequence |
MNPPSGPRVPPSPTQEPSCMATPAPPSWWDSSQSSISSLGRLPSISPTAPGTWAAAWVPLPTVD VPDHAHYTLGTVILLVGLTGMLGNLTVIYTFCRSRSLRTPANMFIINLAVSDFLMSFTQAPVFF TSSLYKQWLFGETGCEFYAFCGALFGISSMITLTAIALDRYLVITRPLATFGVASKRRAAFVLL GVWLYALAWSLPPFFGWSAYVPEGLLTSCSWDYMSFTPAVRAYTMLLCCFVFFLPLLIIIYCYI FIFRAIRETGRALQTFGACKGNGESLWQRQRLQSECKMAKIMLLVILLFVLSWAPYSAVALVAF AGYAHVLTPYMSSVPAVIAKASAIHNPIIYAITHPKYRVAIAQHLPCLGVLLGVSRRHSRPYPS YRSTHRSTLTSHTSNLSWISIRRRQESLGSESEVGWTHMEAAAVWGAAQQANGRSLYGQGLEDL EAKAPPRPQGHEAETPGKTKGLIPSQDPRM |
Function of OPN4 Membrane Protein
OPN4 plays an important non-image-forming role in the setting of circadian rhythms as well as other functions. Mutations in the Opn4 gene can lead to clinical disorders, such as seasonal affective disorder (SAD). Studies have shown that 5% of patients with SAD are associated with missense mutations in Opn4 and P10L. Besides, OPN4 serves an important role in the photoentrainment of circadian rhythms in mammals. The discovery of the role of OPN4 in non-image forming vision has led to a growth in optogenetics. Additionally, an OPN4 based receptor has been reported to link to migraine pain.
Fig.1 Structure of OPN4 membrane protein.
Application of OPN4 Membrane Protein in Literature
This article reports that OPN4-knockout mice display reduced photoentrainment. In comparison to wild-type mice that expressed OPN4 normally, deficits in light-induced phase shifts in locomotion activity were noted in melanopsin-null mice (Opn4 -/-).
This article reveals that mice with both outer-retinal degeneration and a deficiency in OPN4 exhibited complete loss of photoentrainment of the circadian oscillator, pupillary light responses, photic suppression of arylalkylamine-N-acetyltransferase transcript, and acute suppression of locomotor activity by light.
Authors show that OPN4 is present in cell bodies, dendrites, and proximal axonal segments of a subset of rat RGCs. Rat RGCs that exhibited intrinsic photosensitivity invariably expressed OPN4. Hence, OPN4 is most likely the visual pigment of phototransducing RGCs that set the circadian clock and initiate other non-image-forming visual functions.
This article reports that the mechanisms that control OPN4 expression in the rat retina. They discover that dopamine (DA) is involved in the regulation of OPN4 mRNA, possibly via dopamine D2 receptors that are located on these ipRGCs.
This article summarizes recent findings related to OPN4 and OPN4 ganglion cells and lists other retinal proteins that might serve as photopigments in the mammalian photoentrainment input pathway.
OPN4 Preparation Options
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-OPN4 antibody development services.
As a forward-looking research institute as well as a leading customer service provider in the field of membrane protein, Creative Biolabs has won good reputation among our worldwide customers for successfully accomplishing numerous challenging projects including generation of many functional membrane proteins. Please feel free to contact us for more information.
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