XLRS1_HUMAN
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 03-AUG-2022, entry version 181.
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC 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., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., 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., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., 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., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., 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., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., 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., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA 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 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., Yates J.R.,
RA 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 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-linked
RT 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 in
RT either intracellular retention or incorrect assembly of the functionally
RT 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., Wang T.,
RA Roseman A.M., Baldock C.;
RT "Structural analysis of X-linked retinoschisis mutations reveals distinct
RT 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:0007744|PDB:3JD6}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.10 ANGSTROMS) OF 24-224, SUBUNIT, AND
RP 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 cell-
RT 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/pl00008705;
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 gene
RT 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 senile
RT 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., Hamel C.P.;
RT "X-linked retinoschisis with a novel substitutive amino acid (P193S) in
RT 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., Oguchi Y.,
RA 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; ARG-96;
RP GLN-102; ARG-140; TRP-142; CYS-163; SER-192; CYS-200; HIS-200 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 evidence
RT 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 and
RT 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; GLN-213
RP AND ARG-223.
RX PubMed=17615541;
RA Li X., Ma X., Tao Y.;
RT "Clinical features of X linked juvenile retinoschisis in Chinese families
RT 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., Pamer Z.,
RA Knezy K., Salacz G., Janaky M., Ferencz M., Hargitai J., Papp A.,
RA Farkas A.;
RT "Clinical and genetic findings in Hungarian patients with X-linked juvenile
RT 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 a
CC role in cell-cell adhesion processes in the retina, via homomeric
CC interaction between octamers present on the surface of two neighboring
CC cells (PubMed:27114531). Required for normal structure and function of
CC the retina (PubMed:19093009). {ECO:0000250|UniProtKB:Q9Z1L4,
CC ECO:0000269|PubMed:19093009, 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 (PubMed:27798099,
CC PubMed:26812435, PubMed:27114531). Two stacked octamers can assemble to
CC form a hexadecamer (PubMed:27798099, PubMed:26812435, PubMed:27114531).
CC {ECO:0000269|PubMed:15644328, ECO:0000269|PubMed:19849666,
CC ECO:0000269|PubMed:26812435, ECO:0000269|PubMed:27114531,
CC 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 protein
CC {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 lipid
CC 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 photoreceptors,
CC the inner nuclear layer, the inner plexiform layer and the ganglion
CC cell layer (at protein level). At the macula, expressed in both the
CC outer and inner nuclear layers and in the inner plexiform layer (at
CC protein level) (PubMed:10915776). Detected in retina (PubMed:9326935).
CC Detected only within the photoreceptor cell layer, most prominently
CC within the inner segments of the photoreceptors (PubMed:10915776).
CC Undetectable in 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 are
CC 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 the
CC typical fundus appearance, strabismus, nystagmus, axial hyperopia,
CC defective color vision and foveal ectopy can be present. The most
CC important complications are vitreous hemorrhage, retinal detachment,
CC and neovascular glaucoma. {ECO:0000269|PubMed:10079181,
CC ECO:0000269|PubMed:10220153, ECO:0000269|PubMed:10234514,
CC ECO:0000269|PubMed:10450864, ECO:0000269|PubMed:10533068,
CC ECO:0000269|PubMed:17304551, ECO:0000269|PubMed:17615541,
CC ECO:0000269|PubMed:17631851, ECO:0000269|PubMed:19093009,
CC ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:27798099,
CC ECO:0000269|PubMed:9326935, ECO:0000269|PubMed:9760195,
CC ECO:0000269|Ref.14}. Note=The disease is caused by variants affecting
CC the gene represented in this entry.
CC -!- WEB RESOURCE: Name=Mutations of the RS1 gene; Note=Retina
CC International's Scientific Newsletter;
CC URL="https://www.retina-international.org/files/sci-news/xlrsmut.htm";
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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 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 AlphaFoldDB; O15537; -.
DR SMR; O15537; -.
DR BioGRID; 112161; 2.
DR CORUM; O15537; -.
DR IntAct; O15537; 4.
DR STRING; 9606.ENSP00000369320; -.
DR TCDB; 8.A.154.1.1; the retinoschisin (rs1) family.
DR iPTMnet; O15537; -.
DR PhosphoSitePlus; O15537; -.
DR BioMuta; RS1; -.
DR MassIVE; O15537; -.
DR PaxDb; O15537; -.
DR PeptideAtlas; O15537; -.
DR PRIDE; O15537; -.
DR ProteomicsDB; 48745; -.
DR Antibodypedia; 24146; 88 antibodies from 13 providers.
DR DNASU; 6247; -.
DR Ensembl; ENST00000379984.4; ENSP00000369320.3; ENSG00000102104.9.
DR GeneID; 6247; -.
DR KEGG; hsa:6247; -.
DR MANE-Select; ENST00000379984.4; ENSP00000369320.3; NM_000330.4; NP_000321.1.
DR UCSC; uc004cyo.4; human.
DR CTD; 6247; -.
DR DisGeNET; 6247; -.
DR GeneCards; RS1; -.
DR GeneReviews; RS1; -.
DR HGNC; HGNC:10457; RS1.
DR HPA; ENSG00000102104; Tissue enriched (retina).
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 VEuPathDB; HostDB:ENSG00000102104; -.
DR eggNOG; ENOG502QU6Y; Eukaryota.
DR GeneTree; ENSGT00940000161181; -.
DR HOGENOM; CLU_030066_2_0_1; -.
DR InParanoid; O15537; -.
DR OMA; VCKCDCQ; -.
DR OrthoDB; 1047682at2759; -.
DR PhylomeDB; O15537; -.
DR PathwayCommons; O15537; -.
DR SignaLink; O15537; -.
DR SIGNOR; O15537; -.
DR BioGRID-ORCS; 6247; 9 hits in 683 CRISPR screens.
DR ChiTaRS; RS1; human.
DR GeneWiki; Retinoschisin; -.
DR GenomeRNAi; 6247; -.
DR Pharos; O15537; Tbio.
DR PRO; PR:O15537; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O15537; protein.
DR Bgee; ENSG00000102104; Expressed in oocyte and 19 other tissues.
DR Genevisible; O15537; HS.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; IGI:ARUK-UCL.
DR GO; GO:0098984; C:neuron to neuron synapse; ISS:ARUK-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:ARUK-UCL.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate 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:0001654; P:eye 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 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; Disease variant;
KW Disulfide bond; Lipid-binding; Membrane; Reference proteome; Secreted;
KW Sensory transduction; Signal; Vision.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..224
FT /note="Retinoschisin"
FT /id="PRO_0000022695"
FT DOMAIN 63..219
FT /note="F5/8 type C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 40
FT /note="Interchain"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000269|PubMed:15644328"
FT DISULFID 59
FT /note="Interchain (with C-223)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000269|PubMed:15644328"
FT DISULFID 63..219
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000269|PubMed:15644328, ECO:0007744|PDB:3JD6"
FT DISULFID 110..142
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000269|PubMed:15644328, ECO:0007744|PDB:3JD6"
FT DISULFID 223
FT /note="Interchain (with C-59)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081,
FT ECO:0000269|PubMed:15644328"
FT VARIANT 12
FT /note="L -> H (in XLRS1; dbSNP:rs62645879)"
FT /id="VAR_008209"
FT VARIANT 13
FT /note="L -> P (in XLRS1; dbSNP:rs104894935)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008210"
FT VARIANT 59
FT /note="C -> S (in XLRS1; loss of octamerization; no effect
FT on secretion; dbSNP:rs62645889)"
FT /evidence="ECO:0000269|PubMed:27798099"
FT /id="VAR_008211"
FT VARIANT 65
FT /note="Y -> C (in XLRS1; dbSNP:rs62645892)"
FT /id="VAR_008212"
FT VARIANT 70
FT /note="G -> A (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008213"
FT VARIANT 70
FT /note="G -> S (in XLRS1; dbSNP:rs62645894)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008214"
FT VARIANT 72
FT /note="E -> D (in XLRS1; dbSNP:rs104894932)"
FT /id="VAR_008180"
FT VARIANT 72
FT /note="E -> G (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:17631851"
FT /id="VAR_080439"
FT VARIANT 72
FT /note="E -> K (in XLRS1; dbSNP:rs104894928)"
FT /evidence="ECO:0000269|PubMed:10220153,
FT ECO:0000269|PubMed:10234514, ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:19093009, ECO:0000269|PubMed:9760195"
FT /id="VAR_008181"
FT VARIANT 73
FT /note="S -> P (in XLRS1; dbSNP:rs62645899)"
FT /evidence="ECO:0000269|PubMed:17615541"
FT /id="VAR_065326"
FT VARIANT 74
FT /note="G -> V (in XLRS1; dbSNP:rs104894933)"
FT /evidence="ECO:0000269|PubMed:10234514,
FT ECO:0000269|PubMed:10533068"
FT /id="VAR_008182"
FT VARIANT 85
FT /note="Missing (in XLRS1; dbSNP:rs61750458)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_023959"
FT VARIANT 89
FT /note="Y -> C (in XLRS1; dbSNP:rs61752060)"
FT /evidence="ECO:0000269|PubMed:10220153"
FT /id="VAR_008215"
FT VARIANT 96
FT /note="W -> R (in XLRS1; dbSNP:rs61752063)"
FT /evidence="ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:9326935"
FT /id="VAR_008183"
FT VARIANT 98
FT /note="A -> E (in XLRS1; dbSNP:rs61752065)"
FT /evidence="ECO:0000269|PubMed:10450864"
FT /id="VAR_008216"
FT VARIANT 102
FT /note="R -> Q (in XLRS1; dbSNP:rs61752068)"
FT /evidence="ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:17304551, ECO:0000269|PubMed:17615541"
FT /id="VAR_008217"
FT VARIANT 102
FT /note="R -> W (in XLRS1; dbSNP:rs61752067)"
FT /evidence="ECO:0000269|PubMed:9326935"
FT /id="VAR_008184"
FT VARIANT 103
FT /note="L -> R (in XLRS1; dbSNP:rs61752069)"
FT /id="VAR_008218"
FT VARIANT 108
FT /note="F -> C (in XLRS1; dbSNP:rs61752072)"
FT /evidence="ECO:0000269|PubMed:10450864"
FT /id="VAR_008219"
FT VARIANT 109
FT /note="G -> E (in XLRS1; dbSNP:rs281865345)"
FT /evidence="ECO:0000269|PubMed:10220153"
FT /id="VAR_008220"
FT VARIANT 109
FT /note="G -> R (in XLRS1; dbSNP:rs104894934)"
FT /evidence="ECO:0000269|PubMed:10234514"
FT /id="VAR_008185"
FT VARIANT 109
FT /note="G -> W (in XLRS1; dbSNP:rs104894934)"
FT /evidence="ECO:0000269|PubMed:10450864"
FT /id="VAR_008221"
FT VARIANT 110
FT /note="C -> Y (in XLRS1; loss of secretion into the
FT extracellular space; may impair protein folding;
FT dbSNP:rs61752075)"
FT /evidence="ECO:0000269|PubMed:19849666"
FT /id="VAR_008222"
FT VARIANT 112
FT /note="W -> C (in XLRS1; dbSNP:rs61752144)"
FT /id="VAR_008223"
FT VARIANT 113
FT /note="L -> F (in XLRS1; dbSNP:rs61752145)"
FT /id="VAR_008224"
FT VARIANT 127
FT /note="L -> P (in XLRS1; dbSNP:rs61752149)"
FT /id="VAR_008225"
FT VARIANT 135
FT /note="G -> V (in XLRS1; dbSNP:rs61752152)"
FT /id="VAR_008226"
FT VARIANT 136
FT /note="I -> T (in XLRS1; dbSNP:rs61752153)"
FT /id="VAR_008227"
FT VARIANT 138
FT /note="T -> A (in XLRS1; dbSNP:rs61752154)"
FT /id="VAR_008228"
FT VARIANT 140
FT /note="G -> E (in XLRS1; dbSNP:rs61752157)"
FT /id="VAR_008229"
FT VARIANT 140
FT /note="G -> R (in XLRS1; dbSNP:rs61752156)"
FT /evidence="ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:19093009"
FT /id="VAR_008230"
FT VARIANT 141
FT /note="R -> C (in XLRS1; dbSNP:rs61752158)"
FT /evidence="ECO:0000269|PubMed:10450864,
FT ECO:0000269|PubMed:19093009"
FT /id="VAR_008231"
FT VARIANT 141
FT /note="R -> G (in XLRS1; dbSNP:rs61752158)"
FT /id="VAR_008232"
FT VARIANT 141
FT /note="R -> H (in XLRS1; no effect on oligomerization; no
FT effect on protein stability; dbSNP:rs61752159)"
FT /evidence="ECO:0000269|PubMed:17631851,
FT ECO:0000269|PubMed:19093009, ECO:0000269|PubMed:27798099"
FT /id="VAR_008233"
FT VARIANT 142
FT /note="C -> W (in XLRS1; dbSNP:rs1800001)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008234"
FT VARIANT 143
FT /note="D -> V (in XLRS1; dbSNP:rs61753161)"
FT /id="VAR_008235"
FT VARIANT 145
FT /note="D -> H (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:17615541"
FT /id="VAR_065327"
FT VARIANT 146
FT /note="E -> D (in XLRS1; dbSNP:rs61753163)"
FT /id="VAR_008236"
FT VARIANT 146
FT /note="E -> K (in XLRS1; dbSNP:rs61753162)"
FT /evidence="ECO:0000269|PubMed:10450864"
FT /id="VAR_008237"
FT VARIANT 155
FT /note="Y -> C (in XLRS1; dbSNP:rs61753165)"
FT /id="VAR_008238"
FT VARIANT 156
FT /note="R -> G (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:17615541"
FT /id="VAR_065328"
FT VARIANT 158
FT /note="D -> N (in dbSNP:rs1800002)"
FT /id="VAR_008239"
FT VARIANT 163
FT /note="W -> C (in XLRS1; dbSNP:rs61753166)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008240"
FT VARIANT 178
FT /note="G -> D (in XLRS1; dbSNP:rs61753169)"
FT /id="VAR_008241"
FT VARIANT 182
FT /note="R -> C (in XLRS1; dbSNP:rs61753171)"
FT /evidence="ECO:0000269|PubMed:10220153"
FT /id="VAR_008242"
FT VARIANT 192
FT /note="P -> L (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:19093009"
FT /id="VAR_065329"
FT VARIANT 192
FT /note="P -> R (in XLRS1; dbSNP:rs61753175)"
FT /id="VAR_008243"
FT VARIANT 192
FT /note="P -> S (in XLRS1; dbSNP:rs61753174)"
FT /evidence="ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:19093009"
FT /id="VAR_008244"
FT VARIANT 193
FT /note="P -> L (in XLRS1; dbSNP:rs281865352)"
FT /evidence="ECO:0000269|PubMed:9760195"
FT /id="VAR_008245"
FT VARIANT 193
FT /note="P -> S (in XLRS1; dbSNP:rs281865351)"
FT /evidence="ECO:0000269|Ref.14"
FT /id="VAR_008246"
FT VARIANT 197
FT /note="R -> C (in XLRS1; dbSNP:rs281865354)"
FT /evidence="ECO:0000269|PubMed:10079181"
FT /id="VAR_008247"
FT VARIANT 197
FT /note="R -> H (in XLRS1; dbSNP:rs281865355)"
FT /evidence="ECO:0000269|PubMed:17631851"
FT /id="VAR_008248"
FT VARIANT 199
FT /note="I -> T (in XLRS1; dbSNP:rs281865356)"
FT /id="VAR_008249"
FT VARIANT 200
FT /note="R -> C (in XLRS1; dbSNP:rs281865357)"
FT /evidence="ECO:0000269|PubMed:10450864,
FT ECO:0000269|PubMed:10533068, ECO:0000269|PubMed:17615541,
FT ECO:0000269|PubMed:17631851"
FT /id="VAR_008251"
FT VARIANT 200
FT /note="R -> H (in XLRS1; dbSNP:rs281865358)"
FT /evidence="ECO:0000269|PubMed:10533068"
FT /id="VAR_008252"
FT VARIANT 203
FT /note="P -> L (in XLRS1; dbSNP:rs104894930)"
FT /evidence="ECO:0000269|PubMed:10220153"
FT /id="VAR_008253"
FT VARIANT 206
FT /note="W -> C (in XLRS1)"
FT /evidence="ECO:0000269|PubMed:17631851"
FT /id="VAR_080440"
FT VARIANT 207
FT /note="H -> Q (in XLRS1; decreases protein stability; does
FT not abrogate oligomerization or secretion;
FT dbSNP:rs281865360)"
FT /evidence="ECO:0000269|PubMed:19849666"
FT /id="VAR_008254"
FT VARIANT 209
FT /note="R -> C (in XLRS1; dbSNP:rs281865361)"
FT /evidence="ECO:0000269|PubMed:19093009"
FT /id="VAR_065330"
FT VARIANT 209
FT /note="R -> H (in XLRS1; dbSNP:rs281865362)"
FT /evidence="ECO:0000269|PubMed:17615541"
FT /id="VAR_008255"
FT VARIANT 213
FT /note="R -> Q (in XLRS1; dbSNP:rs281865364)"
FT /evidence="ECO:0000269|PubMed:17615541"
FT /id="VAR_065331"
FT VARIANT 213
FT /note="R -> W (in XLRS1; dbSNP:rs281865365)"
FT /id="VAR_008256"
FT VARIANT 215
FT /note="E -> K (in XLRS1; dbSNP:rs281865367)"
FT /evidence="ECO:0000269|PubMed:10450864"
FT /id="VAR_008257"
FT VARIANT 215
FT /note="E -> Q (in XLRS1; dbSNP:rs281865367)"
FT /id="VAR_008258"
FT VARIANT 216
FT /note="L -> P (in XLRS1; dbSNP:rs281865368)"
FT /id="VAR_008259"
FT VARIANT 219
FT /note="C -> G (in XLRS1; dbSNP:rs281865369)"
FT /id="VAR_008260"
FT VARIANT 219
FT /note="C -> R (in XLRS1; dbSNP:rs281865369)"
FT /id="VAR_008261"
FT VARIANT 222
FT /note="K -> N (in dbSNP:rs1800004)"
FT /id="VAR_012078"
FT VARIANT 223
FT /note="C -> R (in XLRS1; dbSNP:rs104894929)"
FT /evidence="ECO:0000269|PubMed:10533068,
FT ECO:0000269|PubMed:17615541"
FT /id="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
