May play a role in rpe physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.
Combining with an extracellular signal and transmitting the signal across the membrane by activating an associated G-protein; promotes the exchange of GDP for GTP on the alpha subunit of a heterotrimeric G-protein complex.
The function of absorbing and responding to incidental electromagnetic radiation, particularly visible light. The response may involve a change in conformation.
A series of molecular signals that proceeds with an activated receptor promoting the exchange of GDP for GTP on the alpha-subunit of an associated heterotrimeric G-protein complex. The GTP-bound activated alpha-G-protein then dissociates from the beta- and gamma-subunits to further transmit the signal within the cell. The pathway begins with receptor-ligand interaction, or for basal GPCR signaling the pathway begins with the receptor activating its G protein in the absence of an agonist, and ends with regulation of a downstream cellular process, e.g. transcription.
Proc. Natl. Acad. Sci. U.S.A. 94, 9893-9898 (1997)[PubMed:9275222]
A visual pigment-like protein, referred to as peropsin, has been identified by large-scale sequencing of cDNAs derived from human ocular tissues. The corresponding mRNA was found only in the eye, where it is localized to the retinal pigment epithelium (RPE). Peropsin immunoreactivity, visualized by light and electron microscopy, localizes the protein to the apical face of the RPE, and most prominently to the microvilli that surround the photoreceptor outer segments. These observations suggest that peropsin may play a role in RPE physiology either by detecting light directly or by monitoring the concentration of retinoids or other photoreceptor-derived compounds.
The series of events required for an organism to receive a visual stimulus, convert it to a molecular signal, and recognize and characterize the signal. Visual stimuli are detected in the form of photons and are processed to form an image.
IEAInterPro 2 GO
Pathways
According to Reactome, this protein belongs to the following pathway:
Protein involved in sensory transduction, the process by which a cell converts an extracellular signal, such as light, taste, sound, touch or smell, into electric signals.
Receptors which transduce extracellular signals across the cell membrane. At the external side they receive a ligand (a photon in case of opsins), and at the cytosolic side they activate a guanine nucleotide-binding (G) protein. These receptors are hydrophobic proteins that cross the membrane seven times.
Protein involved in the convertion of light directly into a signal. These proteins are classified in a limited number of families based on the chemical structure of the light-absorbing chromophores involved, and also on protein sequence similarities to discriminate the many photoreceptor proteins that bind a flavin derivative. Accordingly, the most important families are the rhodopsins, the phytochromes, the xanthopsins, the cryptochromes, the phototropins and the BLUF proteins.
Protein found in the retina or, in the case of bacteriorhodopsin, in the purple membrane of halobacteria, and which acts as a photoreceptor and which binds a retinal chromophore.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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