Visual pigment-like receptor peropsin (RRH), a member of visual pigment-like receptors, is a protein is encoded by the RRH gene in human. It is an important opsin and belongs to the guanine nucleotide-binding protein (G protein)-coupled receptors. Peropsin genes have seven-exons including neuropsin and RGR-opsin genes. The peropsins are one of the four subgroups of the Go/RGR opsins, including Go-opsins, RGR-opsins, peropsins, and neuropsins.
Basic Information of RRH | |
Protein Name | Visual pigment-like receptor peropsin |
Gene Name | RRH |
Aliases | / |
Organism | Homo sapiens (Human) |
UniProt ID | O14718 |
Transmembrane Times | 7 |
Length (aa) | 337 |
Sequence | MLRNNLGNSSDSKNEDGSVFSQTEHNIVATYLIMAGMISIISNIIVLGIFIKYKELRTPTNAIIINLAVTDIGVSSIGYPMSAASDLYGSWKFGYAGCQVYAGLNIFFGMASIGLLTVVAVDRYLTICLPDVGRRMTTNTYIGLILGAWINGLFWALMPIIGWASYAPDPTGATCTINWRKNDRSFVSYTMTVIAINFIVPLTVMFYCYYHVTLSIKHHTTSDCTESLNRDWSDQIDVTKMSVIMICMFLVAWSPYSIVCLWASFGDPKKIPPPMAIIAPLFAKSSTFYNPCIYVVANKKFRRAMLAMFKCQTHQTMPVTSILPMDVSQNPLASGRI |
Visual pigment-like receptor peropsin is one of the G protein-coupled receptors (GPCR). It has been reported that RRH can regulate RPE physiology by detecting light directly or monitoring the concentration of retinoids/other photoreceptor-derived compounds. It also participates in the activity of G-protein coupled receptor signaling pathway, as well as phototransduction, protein-chromophore linkage, and visual perception.
Fig. 1 Gene expression pattern of the RRH gene.
The authors show that these lineages comprise the "classical opsin superfamily" which includes the rod and cone opsins, pinopsin, VA-opsin, parapinopsin and encephalopsin, the RRH and RGR group, and the melanopsin line. Relationship between RRH and RGR suggests that peropsin may function as a retinal isomerase.
This article demonstrates that variants of RRH truncate the last two transmembrane-spanning fragments and the Lys284, except for the disease phenotype. It also concludes that RRH is not a frequent gene in retinitis pigmentosa.
The results show that peropsin exists before the deuterostome-protostome split like other members of the opsin family. Moreover, the spider peropsin and fluorescence from retinal chromophore are found in the same region.
This article indicates that the peropsin gene is not an original cause of RP or some related retinal degenerations.
The article suggests that peropsin can control all-trans-ROL movement from the retina to the RPE and may be in charge of all-trans-ROL storage within the RPE. Peropsin can affect light-dependent regulation of all-trans-ROL uptake between photoreceptors and RPE cells.
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