ID XLRS1_HUMAN Reviewed; 224 AA. AC O15537; Q0QD39; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 2. DT 13-FEB-2019, entry version 163. DE RecName: Full=Retinoschisin; DE AltName: Full=X-linked juvenile retinoschisis protein; DE Flags: Precursor; GN Name=RS1; Synonyms=XLRS1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS XLRS1 ARG-96 AND RP TRP-102, AND TISSUE SPECIFICITY. RC TISSUE=Retina; RX PubMed=9326935; DOI=10.1038/ng1097-164; RA Sauer C.G., Gehrig A., Warneke-Wittstock R., Marquardt A., Ewing C.C., RA Gibson A., Lorenz B., Jurklies B., Weber B.H.; RT "Positional cloning of the gene associated with X-linked juvenile RT retinoschisis."; RL Nat. Genet. 17:164-170(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15772651; DOI=10.1038/nature03440; RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., RA Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., RA Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S., RA Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., RA Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., RA Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., RA Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., RA Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., RA Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., RA Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., RA Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., RA Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., RA Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., RA Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., RA Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., RA Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., RA Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., RA Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., RA Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., RA Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., RA Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., RA Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., RA Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., RA Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., RA de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., RA Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., RA Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., RA Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., RA Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., RA Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., RA Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., RA Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., RA Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., RA Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., RA Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., RA Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., RA Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., RA Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., RA Williams G., Williams L., Williamson A., Williamson H., Wilming L., RA Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., RA Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., RA Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., RA Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., RA Gibbs R.A., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence of the human X chromosome."; RL Nature 434:325-337(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-35. RC TISSUE=Retina; RX PubMed=17286855; DOI=10.1186/1471-2164-8-42; RA Roni V., Carpio R., Wissinger B.; RT "Mapping of transcription start sites of human retina expressed RT genes."; RL BMC Genomics 8:42-42(2007). RN [4] RP TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION. RX PubMed=10915776; DOI=10.1093/hmg/9.12.1873; RA Grayson C., Reid S.N., Ellis J.A., Rutherford A., Sowden J.C., RA Yates J.R., Farber D.B., Trump D.; RT "Retinoschisin, the X-linked retinoschisis protein, is a secreted RT photoreceptor protein, and is expressed and released by Weri-Rb1 RT cells."; RL Hum. Mol. Genet. 9:1873-1879(2000). RN [5] RP SUBUNIT, AND DISULFIDE BONDS. RX PubMed=15644328; DOI=10.1074/jbc.M413117200; RA Wu W.W., Wong J.P., Kast J., Molday R.S.; RT "RS1, a discoidin domain-containing retinal cell adhesion protein RT associated with X-linked retinoschisis, exists as a novel disulfide- RT linked octamer."; RL J. Biol. Chem. 280:10721-10730(2005). RN [6] RP SUBCELLULAR LOCATION, SUBUNIT, AND CHARACTERIZATION OF VARIANTS XLRS1 RP SER-59 AND TYR-110. RX PubMed=19849666; DOI=10.1042/BJ20091179; RA Gleghorn L.J., Trump D., Bulleid N.J.; RT "Wild-type and missense mutants of retinoschisin co-assemble resulting RT in either intracellular retention or incorrect assembly of the RT functionally active octamer."; RL Biochem. J. 425:275-283(2009). RN [7] RP STRUCTURE BY ELECTRON MICROSCOPY (4.2 ANGSTROMS), SUBUNIT, AND RP CHARACTERIZATION OF VARIANTS XLRS1 HIS-141 AND GLN-207. RX PubMed=27798099; DOI=10.1093/hmg/ddw345; RA Ramsay E.P., Collins R.F., Owens T.W., Siebert C.A., Jones R.P., RA Wang T., Roseman A.M., Baldock C.; RT "Structural analysis of X-linked retinoschisis mutations reveals RT distinct classes which differentially effect retinoschisin function."; RL Hum. Mol. Genet. 25:5311-5320(2016). RN [8] RP STRUCTURE BY ELECTRON MICROSCOPY, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=26812435; DOI=10.1371/journal.pone.0147653; RA Bush M., Setiaputra D., Yip C.K., Molday R.S.; RT "Cog-Wheel Octameric Structure of RS1, the Discoidin Domain Containing RT Retinal Protein Associated with X-Linked Retinoschisis."; RL PLoS ONE 11:E0147653-E0147653(2016). RN [9] {ECO:0000244|PDB:3JD6} RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF 24-224, SUBUNIT, RP AND DISULFIDE BONDS. RX PubMed=27114531; DOI=10.1073/pnas.1519048113; RA Tolun G., Vijayasarathy C., Huang R., Zeng Y., Li Y., Steven A.C., RA Sieving P.A., Heymann J.B.; RT "Paired octamer rings of retinoschisin suggest a junctional model for RT cell-cell adhesion in the retina."; RL Proc. Natl. Acad. Sci. U.S.A. 113:5287-5292(2016). RN [10] RP VARIANTS XLRS1 LYS-72 AND LEU-193. RX PubMed=9760195; DOI=10.1007/s004390050796; RA Hotta Y., Fujiki K., Hayakawa M., Ohta T., Fujimaki T., Tamaki K., RA Yokoyama T., Kanai A., Hirakata A., Hida T., Nishina S., Azuma N.; RT "Japanese juvenile retinoschisis is caused by mutations of the XLRS1 RT gene."; RL Hum. Genet. 103:142-144(1998). RN [11] RP VARIANT XLRS1 CYS-197. RX PubMed=10079181; DOI=10.1006/bbrc.1999.0323; RA Shastry B.S., Hejtmancik F.J., Trese M.T.; RT "Recurrent missense (R197C) and nonsense (Y89X) mutations in the XLRS1 RT gene in families with X-linked retinoschisis."; RL Biochem. Biophys. Res. Commun. 256:317-319(1999). RN [12] RP VARIANTS XLRS1 GLU-98; CYS-108; TRP-109; CYS-141; LYS-146; CYS-200 AND RP LYS-215. RX PubMed=10450864; DOI=10.1034/j.1399-0004.1999.550611.x; RA Gehrig A., White K., Lorenz B., Andrassi M., Clemens S., Weber B.H.; RT "Assessment of RS1 in X-linked juvenile retinoschisis and sporadic RT senile retinoschisis."; RL Clin. Genet. 55:461-465(1999). RN [13] RP VARIANTS XLRS1 LYS-72; VAL-74 AND ARG-109. RX PubMed=10234514; DOI=10.1038/sj.ejhg.5200300; RA Huopaniemi L., Rantala A., Forsius H., Somer M., de la Chapelle A., RA Alitalo T.; RT "Three widespread founder mutations contribute to high incidence of X- RT linked juvenile retinoschisis in Finland."; RL Eur. J. Hum. Genet. 7:368-376(1999). RN [14] RP VARIANT XLRS1 SER-193. RA Duval P.-A., Marlhens F., Griffoin J.-M., Millet P., Arnaud B., RA Hamel C.P.; RT "X-linked retinoschisis with a novel substitutive amino acid (P193S) RT in XLRS1."; RL Hum. Mutat. 13:259-259(1999). RN [15] RP VARIANTS XLRS1 LYS-72; CYS-89; GLU-109; CYS-182 AND LEU-203. RX PubMed=10220153; RX DOI=10.1002/(SICI)1098-1004(1999)13:4<338::AID-HUMU16>3.0.CO;2-0; RA Mashima Y., Shinoda K., Ishida S., Ozawa Y., Kudoh J., Iwata T., RA Oguchi Y., Shimizu N.; RT "Identification of four novel mutations of the XLRS1 gene in Japanese RT patients with X-linked juvenile retinoschisis."; RL Hum. Mutat. 13:338-338(1999). RN [16] RP VARIANTS XLRS1 PRO-13; SER-70; ALA-70; LYS-72; VAL-74; ASN-85 DEL; RP ARG-96; GLN-102; ARG-140; TRP-142; CYS-163; SER-192; CYS-200; HIS-200 RP AND ARG-223. RX PubMed=10533068; RX DOI=10.1002/(SICI)1098-1004(199911)14:5<423::AID-HUMU8>3.0.CO;2-D; RA Hiriyanna K.T., Bingham E.L., Yashar B.M., Ayyagari R., Fishman G., RA Small K.W., Weinberg D.V., Weleber R.G., Lewis R.A., Andreasson S., RA Richards J.E., Sieving P.A.; RT "Novel mutations in XLRS1 causing retinoschisis, including first RT evidence of putative leader sequence change."; RL Hum. Mutat. 14:423-427(1999). RN [17] RP VARIANT XLRS1 GLN-102. RX PubMed=17304551; DOI=10.1002/ajmg.a.31568; RA Saldana M., Thompson J., Monk E., Trump D., Long V., Sheridan E.; RT "X-linked retinoschisis in a female with a heterozygous RS1 missense RT mutation."; RL Am. J. Med. Genet. A 143:608-609(2007). RN [18] RP VARIANTS XLRS1 GLY-72; HIS-141; HIS-197; CYS-200 AND CYS-206. RX PubMed=17631851; DOI=10.1016/j.ajo.2007.05.016; RA Shukla D., Rajendran A., Gibbs D., Suganthalakshmi B., Zhang K., RA Sundaresan P.; RT "Unusual manifestations of x-linked retinoschisis: clinical profile RT and diagnostic evaluation."; RL Am. J. Ophthalmol. 144:419-423(2007). RN [19] RP VARIANTS XLRS1 PRO-73; GLN-102; HIS-145; GLY-156; CYS-200; HIS-209; RP GLN-213 AND ARG-223. RX PubMed=17615541; RA Li X., Ma X., Tao Y.; RT "Clinical features of X linked juvenile retinoschisis in Chinese RT families associated with novel mutations in the RS1 gene."; RL Mol. Vis. 13:804-812(2007). RN [20] RP VARIANTS XLRS1 LYS-72; ARG-140; CYS-141; HIS-141; SER-192; LEU-192 AND RP CYS-209, AND FUNCTION. RX PubMed=19093009; RA Lesch B., Szabo V., Kanya M., Somfai G.M., Vamos R., Varsanyi B., RA Pamer Z., Knezy K., Salacz G., Janaky M., Ferencz M., Hargitai J., RA Papp A., Farkas A.; RT "Clinical and genetic findings in Hungarian patients with X-linked RT juvenile retinoschisis."; RL Mol. Vis. 14:2321-2332(2008). CC -!- FUNCTION: Binds negatively charged membrane lipids, such as CC phosphatidylserine and phosphoinositides (By similarity). May play CC a role in cell-cell adhesion processes in the retina, via CC homomeric interaction between octamers present on the surface of CC two neighboring cells (PubMed:27114531). Required for normal CC structure and function of the retina (PubMed:19093009). CC {ECO:0000250|UniProtKB:Q9Z1L4, ECO:0000269|PubMed:19093009, CC ECO:0000305|PubMed:27114531}. CC -!- SUBUNIT: Homooctamer of 4 homodimers; disulfide-linked CC (PubMed:15644328, PubMed:19849666). The homooctamer has a flat, CC cogwheel structure with a diameter of about 14 nm CC (PubMed:27798099, PubMed:26812435, PubMed:27114531). Two stacked CC octamers can assemble to form a hexadecamer (PubMed:27798099, CC PubMed:26812435, PubMed:27114531). {ECO:0000269|PubMed:15644328, CC ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:26812435, CC ECO:0000269|PubMed:27114531, ECO:0000269|PubMed:27798099}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10915776, CC ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:26812435}. Cell CC membrane {ECO:0000250|UniProtKB:Q9Z1L4}; Peripheral membrane CC protein {ECO:0000250|UniProtKB:Q9Z1L4}; Extracellular side CC {ECO:0000250|UniProtKB:Q9Z1L4}. Note=Binds to phosphatidylserine- CC containing lipid membranes and embeds itself partially into the CC lipid bilayer. Lipid-binding requires the presence of Ca(2+) ions. CC {ECO:0000250|UniProtKB:Q9Z1L4}. CC -!- TISSUE SPECIFICITY: Restricted to the retina (at protein level) CC (PubMed:10915776). Detected in the inner segment of the CC photoreceptors, the inner nuclear layer, the inner plexiform layer CC and the ganglion cell layer (at protein level). At the macula, CC expressed in both the outer and inner nuclear layers and in the CC inner plexiform layer (at protein level) (PubMed:10915776). CC Detected in retina (PubMed:9326935). Detected only within the CC photoreceptor cell layer, most prominently within the inner CC segments of the photoreceptors (PubMed:10915776). Undetectable in CC the inner plexiform layers and the inner nuclear layer CC (PubMed:10915776). {ECO:0000269|PubMed:10915776, CC ECO:0000269|PubMed:9326935}. CC -!- DEVELOPMENTAL STAGE: Up-regulated during the differentiation of a CC retinoblastoma cell line. {ECO:0000269|PubMed:10915776}. CC -!- DISEASE: Retinoschisis juvenile X-linked 1 (XLRS1) [MIM:312700]: A CC vitreo-retinal dystrophy characterized by macular pathology and by CC splitting of the superficial layer of the retina. Macular changes CC are present in almost all cases. In the fundi, radially oriented CC intraretinal foveomacular cysts are seen in a spoke-wheel CC configuration, with the absence of foveal reflex in most cases. In CC addition, approximately half of cases have bilateral peripheral CC retinoschisis in the inferotemporal part of the retina. Aside from CC the typical fundus appearance, strabismus, nystagmus, axial CC hyperopia, defective color vision and foveal ectopy can be CC present. The most important complications are vitreous hemorrhage, CC retinal detachment, and neovascular glaucoma. CC {ECO:0000269|PubMed:10079181, ECO:0000269|PubMed:10220153, CC ECO:0000269|PubMed:10234514, ECO:0000269|PubMed:10450864, CC ECO:0000269|PubMed:10533068, ECO:0000269|PubMed:17304551, CC ECO:0000269|PubMed:17615541, ECO:0000269|PubMed:17631851, CC ECO:0000269|PubMed:19093009, ECO:0000269|PubMed:19849666, CC ECO:0000269|PubMed:27798099, ECO:0000269|PubMed:9326935, CC ECO:0000269|PubMed:9760195, ECO:0000269|Ref.14}. Note=The disease CC is caused by mutations affecting the gene represented in this CC entry. CC -!- WEB RESOURCE: Name=Mutations of the RS1 gene; Note=Retina CC International's Scientific Newsletter; CC URL="http://www.retina-international.org/files/sci-news/xlrsmut.htm"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; AF018963; AAC18405.1; -; Genomic_DNA. DR EMBL; AF018958; AAC18405.1; JOINED; Genomic_DNA. DR EMBL; AF018959; AAC18405.1; JOINED; Genomic_DNA. DR EMBL; AF018960; AAC18405.1; JOINED; Genomic_DNA. DR EMBL; AF018961; AAC18405.1; JOINED; Genomic_DNA. DR EMBL; AF018962; AAC18405.1; JOINED; Genomic_DNA. DR EMBL; AF014459; AAC17928.1; -; mRNA. DR EMBL; Z92542; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; Z94056; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; DQ426892; ABD90543.1; -; mRNA. DR CCDS; CCDS14187.1; -. DR RefSeq; NP_000321.1; NM_000330.3. DR UniGene; Hs.715725; -. DR PDB; 3JD6; EM; 4.10 A; O=24-224. DR PDB; 5N6W; EM; 4.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P=24-224. DR PDBsum; 3JD6; -. DR PDBsum; 5N6W; -. DR ProteinModelPortal; O15537; -. DR SMR; O15537; -. DR BioGrid; 112161; 2. DR CORUM; O15537; -. DR IntAct; O15537; 4. DR STRING; 9606.ENSP00000369320; -. DR iPTMnet; O15537; -. DR PhosphoSitePlus; O15537; -. DR BioMuta; RS1; -. DR PaxDb; O15537; -. DR PeptideAtlas; O15537; -. DR PRIDE; O15537; -. DR ProteomicsDB; 48745; -. DR DNASU; 6247; -. DR Ensembl; ENST00000379984; ENSP00000369320; ENSG00000102104. DR GeneID; 6247; -. DR KEGG; hsa:6247; -. DR UCSC; uc004cyo.4; human. DR CTD; 6247; -. DR DisGeNET; 6247; -. DR EuPathDB; HostDB:ENSG00000102104.8; -. DR GeneCards; RS1; -. DR GeneReviews; RS1; -. DR HGNC; HGNC:10457; RS1. DR HPA; HPA059546; -. DR MalaCards; RS1; -. DR MIM; 300839; gene. DR MIM; 312700; phenotype. DR neXtProt; NX_O15537; -. DR OpenTargets; ENSG00000102104; -. DR Orphanet; 792; X-linked retinoschisis. DR PharmGKB; PA34871; -. DR eggNOG; ENOG410IIHQ; Eukaryota. DR eggNOG; ENOG410YGW6; LUCA. DR GeneTree; ENSGT00940000161181; -. DR HOGENOM; HOG000006700; -. DR HOVERGEN; HBG061301; -. DR InParanoid; O15537; -. DR OMA; WLSKFND; -. DR OrthoDB; 1047682at2759; -. DR PhylomeDB; O15537; -. DR SIGNOR; O15537; -. DR GeneWiki; Retinoschisin; -. DR GenomeRNAi; 6247; -. DR PRO; PR:O15537; -. DR Proteomes; UP000005640; Chromosome X. DR Bgee; ENSG00000102104; Expressed in 41 organ(s), highest expression level in eye. DR Genevisible; O15537; HS. DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB. DR GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl. DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IEA:Ensembl. DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; IEA:Ensembl. DR GO; GO:0080025; F:phosphatidylinositol-3,5-bisphosphate binding; IEA:Ensembl. DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:Ensembl. DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IEA:Ensembl. DR GO; GO:0070273; F:phosphatidylinositol-4-phosphate binding; IEA:Ensembl. DR GO; GO:0010314; F:phosphatidylinositol-5-phosphate binding; IEA:Ensembl. DR GO; GO:0001786; F:phosphatidylserine binding; ISS:UniProtKB. DR GO; GO:0016062; P:adaptation of rhodopsin mediated signaling; IEA:Ensembl. DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc. DR GO; GO:0007275; P:multicellular organism development; TAS:ProtInc. DR GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB. DR GO; GO:0010842; P:retina layer formation; IEA:Ensembl. DR GO; GO:0007601; P:visual perception; IMP:UniProtKB. DR CDD; cd00057; FA58C; 1. DR Gene3D; 2.60.120.260; -; 1. DR InterPro; IPR000421; FA58C. DR InterPro; IPR008979; Galactose-bd-like_sf. DR Pfam; PF00754; F5_F8_type_C; 1. DR SMART; SM00231; FA58C; 1. DR SUPFAM; SSF49785; SSF49785; 1. DR PROSITE; PS01285; FA58C_1; 1. DR PROSITE; PS50022; FA58C_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell membrane; Complete proteome; KW Disease mutation; Disulfide bond; Lipid-binding; Membrane; KW Polymorphism; Reference proteome; Secreted; Sensory transduction; KW Signal; Vision. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 224 Retinoschisin. FT /FTId=PRO_0000022695. FT DOMAIN 63 219 F5/8 type C. {ECO:0000255|PROSITE- FT ProRule:PRU00081}. FT DISULFID 40 40 Interchain. {ECO:0000255|PROSITE- FT ProRule:PRU00081, FT ECO:0000269|PubMed:15644328}. FT DISULFID 59 59 Interchain (with C-223). FT {ECO:0000255|PROSITE-ProRule:PRU00081, FT ECO:0000269|PubMed:15644328}. FT DISULFID 63 219 {ECO:0000244|PDB:3JD6, FT ECO:0000255|PROSITE-ProRule:PRU00081, FT ECO:0000269|PubMed:15644328}. FT DISULFID 110 142 {ECO:0000244|PDB:3JD6, FT ECO:0000255|PROSITE-ProRule:PRU00081, FT ECO:0000269|PubMed:15644328}. FT DISULFID 223 223 Interchain (with C-59). FT {ECO:0000255|PROSITE-ProRule:PRU00081, FT ECO:0000269|PubMed:15644328}. FT VARIANT 12 12 L -> H (in XLRS1; dbSNP:rs62645879). FT /FTId=VAR_008209. FT VARIANT 13 13 L -> P (in XLRS1; dbSNP:rs104894935). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008210. FT VARIANT 59 59 C -> S (in XLRS1; loss of octamerization; FT no effect on secretion; FT dbSNP:rs62645889). FT {ECO:0000269|PubMed:27798099}. FT /FTId=VAR_008211. FT VARIANT 65 65 Y -> C (in XLRS1; dbSNP:rs62645892). FT /FTId=VAR_008212. FT VARIANT 70 70 G -> A (in XLRS1). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008213. FT VARIANT 70 70 G -> S (in XLRS1; dbSNP:rs62645894). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008214. FT VARIANT 72 72 E -> D (in XLRS1; dbSNP:rs104894932). FT /FTId=VAR_008180. FT VARIANT 72 72 E -> G (in XLRS1). FT {ECO:0000269|PubMed:17631851}. FT /FTId=VAR_080439. FT VARIANT 72 72 E -> K (in XLRS1; dbSNP:rs104894928). FT {ECO:0000269|PubMed:10220153, FT ECO:0000269|PubMed:10234514, FT ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:19093009, FT ECO:0000269|PubMed:9760195}. FT /FTId=VAR_008181. FT VARIANT 73 73 S -> P (in XLRS1; dbSNP:rs62645899). FT {ECO:0000269|PubMed:17615541}. FT /FTId=VAR_065326. FT VARIANT 74 74 G -> V (in XLRS1; dbSNP:rs104894933). FT {ECO:0000269|PubMed:10234514, FT ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008182. FT VARIANT 85 85 Missing (in XLRS1). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_023959. FT VARIANT 89 89 Y -> C (in XLRS1; dbSNP:rs61752060). FT {ECO:0000269|PubMed:10220153}. FT /FTId=VAR_008215. FT VARIANT 96 96 W -> R (in XLRS1; dbSNP:rs61752063). FT {ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:9326935}. FT /FTId=VAR_008183. FT VARIANT 98 98 A -> E (in XLRS1; dbSNP:rs61752065). FT {ECO:0000269|PubMed:10450864}. FT /FTId=VAR_008216. FT VARIANT 102 102 R -> Q (in XLRS1; dbSNP:rs61752068). FT {ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:17304551, FT ECO:0000269|PubMed:17615541}. FT /FTId=VAR_008217. FT VARIANT 102 102 R -> W (in XLRS1; dbSNP:rs61752067). FT {ECO:0000269|PubMed:9326935}. FT /FTId=VAR_008184. FT VARIANT 103 103 L -> R (in XLRS1; dbSNP:rs61752069). FT /FTId=VAR_008218. FT VARIANT 108 108 F -> C (in XLRS1; dbSNP:rs61752072). FT {ECO:0000269|PubMed:10450864}. FT /FTId=VAR_008219. FT VARIANT 109 109 G -> E (in XLRS1; dbSNP:rs281865345). FT {ECO:0000269|PubMed:10220153}. FT /FTId=VAR_008220. FT VARIANT 109 109 G -> R (in XLRS1; dbSNP:rs104894934). FT {ECO:0000269|PubMed:10234514}. FT /FTId=VAR_008185. FT VARIANT 109 109 G -> W (in XLRS1; dbSNP:rs104894934). FT {ECO:0000269|PubMed:10450864}. FT /FTId=VAR_008221. FT VARIANT 110 110 C -> Y (in XLRS1; loss of secretion into FT the extracellular space; may impair FT protein folding; dbSNP:rs61752075). FT {ECO:0000269|PubMed:19849666}. FT /FTId=VAR_008222. FT VARIANT 112 112 W -> C (in XLRS1; dbSNP:rs61752144). FT /FTId=VAR_008223. FT VARIANT 113 113 L -> F (in XLRS1; dbSNP:rs61752145). FT /FTId=VAR_008224. FT VARIANT 127 127 L -> P (in XLRS1; dbSNP:rs61752149). FT /FTId=VAR_008225. FT VARIANT 135 135 G -> V (in XLRS1; dbSNP:rs61752152). FT /FTId=VAR_008226. FT VARIANT 136 136 I -> T (in XLRS1; dbSNP:rs61752153). FT /FTId=VAR_008227. FT VARIANT 138 138 T -> A (in XLRS1; dbSNP:rs61752154). FT /FTId=VAR_008228. FT VARIANT 140 140 G -> E (in XLRS1; dbSNP:rs61752157). FT /FTId=VAR_008229. FT VARIANT 140 140 G -> R (in XLRS1; dbSNP:rs61752156). FT {ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:19093009}. FT /FTId=VAR_008230. FT VARIANT 141 141 R -> C (in XLRS1; dbSNP:rs61752158). FT {ECO:0000269|PubMed:10450864, FT ECO:0000269|PubMed:19093009}. FT /FTId=VAR_008231. FT VARIANT 141 141 R -> G (in XLRS1; dbSNP:rs61752158). FT /FTId=VAR_008232. FT VARIANT 141 141 R -> H (in XLRS1; no effect on FT oligomerization; no effect on protein FT stability; dbSNP:rs61752159). FT {ECO:0000269|PubMed:17631851, FT ECO:0000269|PubMed:19093009, FT ECO:0000269|PubMed:27798099}. FT /FTId=VAR_008233. FT VARIANT 142 142 C -> W (in XLRS1; dbSNP:rs1800001). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008234. FT VARIANT 143 143 D -> V (in XLRS1; dbSNP:rs61753161). FT /FTId=VAR_008235. FT VARIANT 145 145 D -> H (in XLRS1). FT {ECO:0000269|PubMed:17615541}. FT /FTId=VAR_065327. FT VARIANT 146 146 E -> D (in XLRS1; dbSNP:rs61753163). FT /FTId=VAR_008236. FT VARIANT 146 146 E -> K (in XLRS1; dbSNP:rs61753162). FT {ECO:0000269|PubMed:10450864}. FT /FTId=VAR_008237. FT VARIANT 155 155 Y -> C (in XLRS1; dbSNP:rs61753165). FT /FTId=VAR_008238. FT VARIANT 156 156 R -> G (in XLRS1). FT {ECO:0000269|PubMed:17615541}. FT /FTId=VAR_065328. FT VARIANT 158 158 D -> N (in dbSNP:rs1800002). FT /FTId=VAR_008239. FT VARIANT 163 163 W -> C (in XLRS1; dbSNP:rs61753166). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008240. FT VARIANT 178 178 G -> D (in XLRS1; dbSNP:rs61753169). FT /FTId=VAR_008241. FT VARIANT 182 182 R -> C (in XLRS1; dbSNP:rs61753171). FT {ECO:0000269|PubMed:10220153}. FT /FTId=VAR_008242. FT VARIANT 192 192 P -> L (in XLRS1). FT {ECO:0000269|PubMed:19093009}. FT /FTId=VAR_065329. FT VARIANT 192 192 P -> R (in XLRS1; dbSNP:rs61753175). FT /FTId=VAR_008243. FT VARIANT 192 192 P -> S (in XLRS1; dbSNP:rs61753174). FT {ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:19093009}. FT /FTId=VAR_008244. FT VARIANT 193 193 P -> L (in XLRS1; dbSNP:rs281865352). FT {ECO:0000269|PubMed:9760195}. FT /FTId=VAR_008245. FT VARIANT 193 193 P -> S (in XLRS1; dbSNP:rs281865351). FT {ECO:0000269|Ref.14}. FT /FTId=VAR_008246. FT VARIANT 197 197 R -> C (in XLRS1; dbSNP:rs281865354). FT {ECO:0000269|PubMed:10079181}. FT /FTId=VAR_008247. FT VARIANT 197 197 R -> H (in XLRS1; dbSNP:rs281865355). FT {ECO:0000269|PubMed:17631851}. FT /FTId=VAR_008248. FT VARIANT 199 199 I -> T (in XLRS1; dbSNP:rs281865356). FT /FTId=VAR_008249. FT VARIANT 200 200 R -> C (in XLRS1; dbSNP:rs281865357). FT {ECO:0000269|PubMed:10450864, FT ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:17615541, FT ECO:0000269|PubMed:17631851}. FT /FTId=VAR_008251. FT VARIANT 200 200 R -> H (in XLRS1; dbSNP:rs281865358). FT {ECO:0000269|PubMed:10533068}. FT /FTId=VAR_008252. FT VARIANT 203 203 P -> L (in XLRS1; dbSNP:rs104894930). FT {ECO:0000269|PubMed:10220153}. FT /FTId=VAR_008253. FT VARIANT 206 206 W -> C (in XLRS1). FT {ECO:0000269|PubMed:17631851}. FT /FTId=VAR_080440. FT VARIANT 207 207 H -> Q (in XLRS1; decreases protein FT stability; does not abrogate FT oligomerization or secretion; FT dbSNP:rs281865360). FT {ECO:0000269|PubMed:19849666}. FT /FTId=VAR_008254. FT VARIANT 209 209 R -> C (in XLRS1; dbSNP:rs281865361). FT {ECO:0000269|PubMed:19093009}. FT /FTId=VAR_065330. FT VARIANT 209 209 R -> H (in XLRS1; dbSNP:rs281865362). FT {ECO:0000269|PubMed:17615541}. FT /FTId=VAR_008255. FT VARIANT 213 213 R -> Q (in XLRS1; dbSNP:rs281865364). FT {ECO:0000269|PubMed:17615541}. FT /FTId=VAR_065331. FT VARIANT 213 213 R -> W (in XLRS1; dbSNP:rs281865365). FT /FTId=VAR_008256. FT VARIANT 215 215 E -> K (in XLRS1; dbSNP:rs281865367). FT {ECO:0000269|PubMed:10450864}. FT /FTId=VAR_008257. FT VARIANT 215 215 E -> Q (in XLRS1; dbSNP:rs281865367). FT /FTId=VAR_008258. FT VARIANT 216 216 L -> P (in XLRS1; dbSNP:rs281865368). FT /FTId=VAR_008259. FT VARIANT 219 219 C -> G (in XLRS1; dbSNP:rs281865369). FT /FTId=VAR_008260. FT VARIANT 219 219 C -> R (in XLRS1; dbSNP:rs281865369). FT /FTId=VAR_008261. FT VARIANT 222 222 K -> N (in dbSNP:rs1800004). FT /FTId=VAR_012078. FT VARIANT 223 223 C -> R (in XLRS1; dbSNP:rs104894929). FT {ECO:0000269|PubMed:10533068, FT ECO:0000269|PubMed:17615541}. FT /FTId=VAR_008262. SQ SEQUENCE 224 AA; 25592 MW; A3893895E6A7E292 CRC64; MSRKIEGFLL LLLFGYEATL GLSSTEDEGE DPWYQKACKC DCQGGPNALW SAGATSLDCI PECPYHKPLG FESGEVTPDQ ITCSNPEQYV GWYSSWTANK ARLNSQGFGC AWLSKFQDSS QWLQIDLKEI KVISGILTQG RCDIDEWMTK YSVQYRTDER LNWIYYKDQT GNNRVFYGNS DRTSTVQNLL RPPIISRFIR LIPLGWHVRI AIRMELLECV SKCA //