Retinoschisin

Retinoschisin 1
Identifiers
Symbols	RS1 ; RS; XLRS1
External IDs	OMIM: 300839 MGI: 1336189 HomoloGene: 279 GeneCards: RS1 Gene
Gene ontology Molecular function • phosphatidylserine binding • phosphatidylinositol-4,5-bisphosphate binding • phosphatidylinositol-3,4,5-trisphosphate binding • phosphatidylinositol-5-phosphate binding • phosphatidylinositol-3-phosphate binding • phosphatidylinositol-3,4-bisphosphate binding • phosphatidylinositol-4-phosphate binding • phosphatidylinositol-3,5-bisphosphate binding Cellular component • extracellular space • extrinsic component of plasma membrane Biological process • cell adhesion • multicellular organismal development • visual perception • retina layer formation • adaptation of rhodopsin mediated signaling Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	6247	20147
Ensembl	ENSG00000102104	ENSMUSG00000031293
UniProt	O15537	Q9Z1L4
RefSeq (mRNA)	NM_000330	NM_011302
RefSeq (protein)	NP_000321	NP_035432
Location (UCSC)	Chr X: 18.64 – 18.67 Mb	Chr X: 160.77 – 160.8 Mb
PubMed search

Retinoschisin also known as X-linked juvenile retinoschisis protein is a protein that in humans is encoded by the RS1 gene.^[1][2][3]

Function and Cell Biology

Retinoschisin is an extracellular protein that plays a crucial role in the cellular organization of the retina. This protein is assembled and secreted from photoreceptors and bipolar cells as a homo-oligomeric protein complex. ^[3] Monomeric retinoschisin contains 224 amino acids with a leader sequence that is cleaved off upon preparation in the cell for secretion. ^[1]

Clinical significance

Mutations in this gene are responsible for X-linked retinoschisis an early-onset macular degeneration in males that results in a splitting of the inner layers of the retina and severe loss in vision.^[3]

References

1. Sauer CG, Gehrig A, Warneke-Wittstock R, Marquardt A, Ewing CC, Gibson A, Lorenz B, Jurklies B, Weber BH (Nov 1997). "Positional cloning of the gene associated with X-linked juvenile retinoschisis". Nat Genet 17 (2): 164–70. doi:10.1038/ng1097-164. PMID 9326935.
2. Molday LL, Wu WW, Molday RS (Nov 2007). "Retinoschisin (RS1), the protein encoded by the X-linked retinoschisis gene, is anchored to the surface of retinal photoreceptor and bipolar cells through its interactions with a Na/K ATPase-SARM1 complex". J Biol Chem 282 (45): 32792–801. doi:10.1074/jbc.M706321200. PMID 17804407.
3. "Entrez Gene: RS1 retinoschisis (X-linked, juvenile) 1".

Further reading

• Sikkink SK, Biswas S, Parry NR, et al. (2007). "X-linked retinoschisis: an update.". J. Med. Genet. 44 (4): 225–32. doi:10.1136/jmg.2006.047340. PMC 2598044. PMID 17172462.
• Alitalo T, Kruse TA, de la Chapelle A (1991). "Refined localization of the gene causing X-linked juvenile retinoschisis.". Genomics 9 (3): 505–10. doi:10.1016/0888-7543(91)90417-D. PMID 2032721.
• Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
• Hotta Y, Fujiki K, Hayakawa M, et al. (1998). "Japanese juvenile retinoschisis is caused by mutations of the XLRS1 gene.". Hum. Genet. 103 (2): 142–4. doi:10.1007/pl00008705. PMID 9760195.
• Shastry BS, Hejtmancik FJ, Trese MT (1999). "Recurrent missense (R197C) and nonsense (Y89X) mutations in the XLRS1 gene in families with X-linked retinoschisis.". Biochem. Biophys. Res. Commun. 256 (2): 317–9. doi:10.1006/bbrc.1999.0323. PMID 10079181.
• Mashima Y, Shinoda K, Ishida S, et al. (1999). "Identification of four novel mutations of the XLRS1 gene in Japanese patients with X-linked juvenile retinoschisis. Mutation in brief no. 234. Online.". Hum. Mutat. 13 (4): 338. doi:10.1002/(SICI)1098-1004(1999)13:4<338::AID-HUMU16>3.0.CO;2-0. PMID 10220153.
• Huopaniemi L, Rantala A, Forsius H, et al. (1999). "Three widespread founder mutations contribute to high incidence of X-linked juvenile retinoschisis in Finland.". Eur. J. Hum. Genet. 7 (3): 368–76. doi:10.1038/sj.ejhg.5200300. PMID 10234514.
• Gehrig A, White K, Lorenz B, et al. (1999). "Assessment of RS1 in X-linked juvenile retinoschisis and sporadic senile retinoschisis.". Clin. Genet. 55 (6): 461–5. doi:10.1034/j.1399-0004.1999.550611.x. PMID 10450864.
• Hiriyanna KT, Bingham EL, Yashar BM, et al. (2000). "Novel mutations in XLRS1 causing retinoschisis, including first evidence of putative leader sequence change.". Hum. Mutat. 14 (5): 423–7. doi:10.1002/(SICI)1098-1004(199911)14:5<423::AID-HUMU8>3.0.CO;2-D. PMID 10533068.
• Grayson C, Reid SN, Ellis JA, et al. (2000). "Retinoschisin, the X-linked retinoschisis protein, is a secreted photoreceptor protein, and is expressed and released by Weri-Rb1 cells.". Hum. Mol. Genet. 9 (12): 1873–9. doi:10.1093/hmg/9.12.1873. PMID 10915776.
• Weber BH, Schrewe H, Molday LL, et al. (2002). "Inactivation of the murine X-linked juvenile retinoschisis gene, Rs1h, suggests a role of retinoschisin in retinal cell layer organization and synaptic structure.". Proc. Natl. Acad. Sci. U.S.A. 99 (9): 6222–7. doi:10.1073/pnas.092528599. PMC 122930. PMID 11983912.
• Tuvdendorj D, Isashiki Y, Ohba N, et al. (2002). "Two Japanese patients with mutations in the XLRS1 gene.". Retina (Philadelphia, Pa.) 22 (3): 354–7. doi:10.1097/00006982-200206000-00017. PMID 12055472.
• Wistow G, Bernstein SL, Wyatt MK, et al. (2002). "Expressed sequence tag analysis of human retina for the NEIBank Project: retbindin, an abundant, novel retinal cDNA and alternative splicing of other retina-preferred gene transcripts.". Mol. Vis. 8: 196–204. PMID 12107411.
• Inoue Y, Yamamoto S, Inoue T, et al. (2002). "Two novel point mutations of the XLRS1 gene in patients with X-linked juvenile retinoschisis.". Am. J. Ophthalmol. 134 (4): 622–4. doi:10.1016/S0002-9394(02)01592-1. PMID 12383832.
• Wang T, Waters CT, Rothman AM, et al. (2003). "Intracellular retention of mutant retinoschisin is the pathological mechanism underlying X-linked retinoschisis.". Hum. Mol. Genet. 11 (24): 3097–105. doi:10.1093/hmg/11.24.3097. PMID 12417531.
• Tanimoto N, Usui T, Takagi M, et al. (2003). "Electroretinographic findings in three family members with X-linked juvenile retinoschisis associated with a novel Pro192Thr mutation of the XLRS1 gene.". Jpn. J. Ophthalmol. 46 (5): 568–76. doi:10.1016/S0021-5155(02)00539-7. PMID 12457918.
• Wu WW, Molday RS (2003). "Defective discoidin domain structure, subunit assembly, and endoplasmic reticulum processing of retinoschisin are primary mechanisms responsible for X-linked retinoschisis.". J. Biol. Chem. 278 (30): 28139–46. doi:10.1074/jbc.M302464200. PMID 12746437.
• Fraternali F, Cavallo L, Musco G (2003). "Effects of pathological mutations on the stability of a conserved amino acid triad in retinoschisin.". FEBS Lett. 544 (1-3): 21–6. doi:10.1016/S0014-5793(03)00433-2. PMID 12782284.
• Sato M, Oshika T, Kaji Y, Nose H (2003). "Three novel mutations in the X-linked juvenile retinoschisis (XLRS1) gene in 6 Japanese patients, 1 of whom had Turner's syndrome.". Ophthalmic Res. 35 (5): 295–300. doi:10.1159/000072151. PMID 12920343.

External links

• GeneReview/NCBI/NIH/UW entry on X-Linked Juvenile Retinoschisis

This article incorporates text from the United States National Library of Medicine, which is in the public domain.