7zw1

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7zw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7zw1 OCA], [https://pdbe.org/7zw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7zw1 RCSB], [https://www.ebi.ac.uk/pdbsum/7zw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7zw1 ProSAT]</span></td></tr>

== Disease ==

[https://www.uniprot.org/uniprot/PRPH2_HUMAN PRPH2_HUMAN] Retinitis punctata albescens;Central areolar choroidal dystrophy;Stargardt disease;Multifocal pattern dystrophy simulating fundus flavimaculatus;Butterfly-shaped pigment dystrophy;Adult-onset foveomacular vitelliform dystrophy;Fundus albipunctatus;Cone rod dystrophy;Retinitis pigmentosa. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. Defects in PRPH2 are found in different retinal diseases including cone-rod dystrophy, retinitis pigmentosa, macular degeneration. The mutations underlying autosomal dominant retinitis pigmentosa and severe macular degeneration are largely missense or small in-frame deletions in a large intradiscal loop between the third and fourth transmembrane domains. In contrast, those associated with the milder pattern phenotypes or with digenic RP are scattered more evenly through the gene and are often nonsense mutations. This observation correlates with the hypothesis that the large loop is an important site of interaction between PRPH2 molecules and other protein components in the disk.<ref>PMID:20335603</ref>

== Function ==

[https://www.uniprot.org/uniprot/PRPH2_HUMAN PRPH2_HUMAN] Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure (By similarity). Required for the maintenance of retinal outer nuclear layer thickness (By similarity). Required for the correct development and organization of the photoreceptor inner segment (By similarity).[UniProtKB:P15499]

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== Publication Abstract from PubMed ==

Mammalian peripherin-2 (PRPH2) and rod outer segment membrane protein 1 (ROM1) are retina-specific tetraspanins that partake in the constant renewal of stacked membrane discs of photoreceptor cells that enable vision. Here, we present single-particle cryo-electron microscopy structures of solubilized PRPH2-ROM1 heterodimers and higher-order oligomers. High-risk PRPH2 and ROM1 mutations causing blindness map to the protein-dimer interface. Cysteine bridges connect dimers forming positive-curved oligomers, whereas negative-curved oligomers were observed occasionally. Hexamers and octamers exhibit a secondary micelle that envelopes four carboxyl-terminal helices, supporting a potential role in membrane remodeling. Together, the data indicate multiple structures for PRPH2-ROM1 in creating and maintaining compartmentalization of photoreceptor cells.

Cryo-EM structures of peripherin-2 and ROM1 suggest multiple roles in photoreceptor membrane morphogenesis.,El Mazouni D, Gros P Sci Adv. 2022 Nov 11;8(45):eadd3677. doi: 10.1126/sciadv.add3677. Epub 2022 Nov, 9. PMID:36351012<ref>PMID:36351012</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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