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Protein

Retinoschisin

Gene

RS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be active in cell adhesion processes during retinal development.

GO - Molecular functioni

GO - Biological processi

  • adaptation of rhodopsin mediated signaling Source: Ensembl
  • cell adhesion Source: ProtInc
  • multicellular organism development Source: ProtInc
  • retina layer formation Source: Ensembl
  • visual perception Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Sensory transduction, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Retinoschisin
Alternative name(s):
X-linked juvenile retinoschisis protein
Gene namesi
Name:RS1
Synonyms:XLRS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:10457. RS1.

Subcellular locationi

GO - Cellular componenti

  • extracellular space Source: ProtInc
  • extrinsic component of plasma membrane Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Retinoschisis juvenile X-linked 1 (XLRS1)11 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA vitreo-retinal dystrophy characterized by macular pathology and by splitting of the superficial layer of the retina. Macular changes are present in almost all cases. In the fundi, radially oriented intraretinal foveomacular cysts are seen in a spoke-wheel configuration, with the absence of foveal reflex in most cases. In addition, approximately half of cases have bilateral peripheral retinoschisis in the inferotemporal part of the retina. Aside from the typical fundus appearance, strabismus, nystagmus, axial hyperopia, defective color vision and foveal ectopy can be present. The most important complications are vitreous hemorrhage, retinal detachment, and neovascular glaucoma.
See also OMIM:312700
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121L → H in XLRS1.
VAR_008209
Natural varianti13 – 131L → P in XLRS1. 1 Publication
VAR_008210
Natural varianti59 – 591C → S in XLRS1.
VAR_008211
Natural varianti65 – 651Y → C in XLRS1.
VAR_008212
Natural varianti70 – 701G → A in XLRS1. 1 Publication
VAR_008213
Natural varianti70 – 701G → S in XLRS1. 1 Publication
VAR_008214
Natural varianti72 – 721E → D in XLRS1.
VAR_008180
Natural varianti72 – 721E → K in XLRS1. 5 Publications
VAR_008181
Natural varianti73 – 731S → P in XLRS1. 1 Publication
VAR_065326
Natural varianti74 – 741G → V in XLRS1. 2 Publications
VAR_008182
Natural varianti85 – 851Missing in XLRS1. 1 Publication
VAR_023959
Natural varianti89 – 891Y → C in XLRS1. 1 Publication
VAR_008215
Natural varianti96 – 961W → R in XLRS1. 2 Publications
VAR_008183
Natural varianti98 – 981A → E in XLRS1. 1 Publication
VAR_008216
Natural varianti102 – 1021R → Q in XLRS1. 3 Publications
VAR_008217
Natural varianti102 – 1021R → W in XLRS1. 1 Publication
VAR_008184
Natural varianti103 – 1031L → R in XLRS1.
VAR_008218
Natural varianti108 – 1081F → C in XLRS1. 1 Publication
VAR_008219
Natural varianti109 – 1091G → E in XLRS1. 1 Publication
VAR_008220
Natural varianti109 – 1091G → R in XLRS1. 1 Publication
VAR_008185
Natural varianti109 – 1091G → W in XLRS1. 1 Publication
VAR_008221
Natural varianti110 – 1101C → Y in XLRS1.
VAR_008222
Natural varianti112 – 1121W → C in XLRS1.
VAR_008223
Natural varianti113 – 1131L → F in XLRS1.
VAR_008224
Natural varianti127 – 1271L → P in XLRS1.
VAR_008225
Natural varianti135 – 1351G → V in XLRS1.
VAR_008226
Natural varianti136 – 1361I → T in XLRS1.
VAR_008227
Natural varianti138 – 1381T → A in XLRS1.
VAR_008228
Natural varianti140 – 1401G → E in XLRS1.
VAR_008229
Natural varianti140 – 1401G → R in XLRS1. 2 Publications
VAR_008230
Natural varianti141 – 1411R → C in XLRS1. 2 Publications
VAR_008231
Natural varianti141 – 1411R → G in XLRS1.
VAR_008232
Natural varianti141 – 1411R → H in XLRS1. 1 Publication
VAR_008233
Natural varianti142 – 1421C → W in XLRS1. 1 Publication
VAR_008234
Natural varianti143 – 1431D → V in XLRS1.
VAR_008235
Natural varianti145 – 1451D → H in XLRS1. 1 Publication
VAR_065327
Natural varianti146 – 1461E → D in XLRS1.
VAR_008236
Natural varianti146 – 1461E → K in XLRS1. 1 Publication
VAR_008237
Natural varianti155 – 1551Y → C in XLRS1.
VAR_008238
Natural varianti156 – 1561R → G in XLRS1. 1 Publication
VAR_065328
Natural varianti163 – 1631W → C in XLRS1. 1 Publication
VAR_008240
Natural varianti178 – 1781G → D in XLRS1.
VAR_008241
Natural varianti182 – 1821R → C in XLRS1. 1 Publication
VAR_008242
Natural varianti192 – 1921P → L in XLRS1. 1 Publication
VAR_065329
Natural varianti192 – 1921P → R in XLRS1.
VAR_008243
Natural varianti192 – 1921P → S in XLRS1. 2 Publications
VAR_008244
Natural varianti193 – 1931P → L in XLRS1. 1 Publication
VAR_008245
Natural varianti193 – 1931P → S in XLRS1. 1 Publication
VAR_008246
Natural varianti197 – 1971R → C in XLRS1. 1 Publication
VAR_008247
Natural varianti197 – 1971R → H in XLRS1.
VAR_008248
Natural varianti199 – 1991I → T in XLRS1.
VAR_008249
Natural varianti200 – 2001R → C in XLRS1. 3 Publications
VAR_008251
Natural varianti200 – 2001R → H in XLRS1. 1 Publication
VAR_008252
Natural varianti203 – 2031P → L in XLRS1. 1 Publication
VAR_008253
Natural varianti207 – 2071H → Q in XLRS1.
VAR_008254
Natural varianti209 – 2091R → C in XLRS1. 1 Publication
VAR_065330
Natural varianti209 – 2091R → H in XLRS1. 1 Publication
VAR_008255
Natural varianti213 – 2131R → Q in XLRS1. 1 Publication
VAR_065331
Natural varianti213 – 2131R → W in XLRS1.
VAR_008256
Natural varianti215 – 2151E → K in XLRS1. 1 Publication
VAR_008257
Natural varianti215 – 2151E → Q in XLRS1.
VAR_008258
Natural varianti216 – 2161L → P in XLRS1.
VAR_008259
Natural varianti219 – 2191C → G in XLRS1.
VAR_008260
Natural varianti219 – 2191C → R in XLRS1.
VAR_008261
Natural varianti223 – 2231C → R in XLRS1. 2 Publications
VAR_008262

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiRS1.
MIMi312700. phenotype.
Orphaneti792. X-linked retinoschisis.
PharmGKBiPA34871.

Polymorphism and mutation databases

BioMutaiRS1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence analysisAdd
BLAST
Chaini24 – 224201RetinoschisinPRO_0000022695Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 – 40InterchainPROSITE-ProRule annotation1 Publication
Disulfide bondi59 – 59Interchain (with C-223)PROSITE-ProRule annotation1 Publication
Disulfide bondi63 ↔ 219PROSITE-ProRule annotation1 Publication
Disulfide bondi110 ↔ 142PROSITE-ProRule annotation1 Publication
Disulfide bondi223 – 223Interchain (with C-59)PROSITE-ProRule annotation1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PaxDbiO15537.
PeptideAtlasiO15537.
PRIDEiO15537.

PTM databases

iPTMnetiO15537.
PhosphoSiteiO15537.

Expressioni

Tissue specificityi

Restricted to the retina (at protein level). At the mRNA level, detected only within the photoreceptor cell layer, most prominently within the inner segments of the photoreceptors. Undetectable in the inner plexiform layers and the inner nuclear layer. At the protein level, found in the inner segment of the photoreceptors, the inner nuclear layer, the inner plexiform layer and the ganglion cell layer. At the macula, expressed in both the outer and inner nuclear layers and in the inner plexiform layer (at protein level).1 Publication

Developmental stagei

Up-regulated during the differentiation of a retinoblastoma cell line.1 Publication

Gene expression databases

BgeeiENSG00000102104.
CleanExiHS_RS1.
GenevisibleiO15537. HS.

Interactioni

Subunit structurei

Homooctamer of 4 homodimers; disulfide-linked.1 Publication

Protein-protein interaction databases

BioGridi112161. 2 interactions.
IntActiO15537. 3 interactions.
STRINGi9606.ENSP00000369320.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JD6electron microscopy4.10O24-224[»]
ProteinModelPortaliO15537.
SMRiO15537. Positions 68-219.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini63 – 219157F5/8 type CPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 F5/8 type C domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG410IIHQ. Eukaryota.
ENOG410YGW6. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000006700.
HOVERGENiHBG061301.
InParanoidiO15537.
OMAiAWLSKYQ.
OrthoDBiEOG091G0HLO.
PhylomeDBiO15537.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. FA58C.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
[Graphical view]
SMARTiSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
PROSITEiPS01285. FA58C_1. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O15537-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRKIEGFLL LLLFGYEATL GLSSTEDEGE DPWYQKACKC DCQGGPNALW
60 70 80 90 100
SAGATSLDCI PECPYHKPLG FESGEVTPDQ ITCSNPEQYV GWYSSWTANK
110 120 130 140 150
ARLNSQGFGC AWLSKFQDSS QWLQIDLKEI KVISGILTQG RCDIDEWMTK
160 170 180 190 200
YSVQYRTDER LNWIYYKDQT GNNRVFYGNS DRTSTVQNLL RPPIISRFIR
210 220
LIPLGWHVRI AIRMELLECV SKCA
Length:224
Mass (Da):25,592
Last modified:August 1, 1998 - v2
Checksum:iA3893895E6A7E292
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121L → H in XLRS1.
VAR_008209
Natural varianti13 – 131L → P in XLRS1. 1 Publication
VAR_008210
Natural varianti59 – 591C → S in XLRS1.
VAR_008211
Natural varianti65 – 651Y → C in XLRS1.
VAR_008212
Natural varianti70 – 701G → A in XLRS1. 1 Publication
VAR_008213
Natural varianti70 – 701G → S in XLRS1. 1 Publication
VAR_008214
Natural varianti72 – 721E → D in XLRS1.
VAR_008180
Natural varianti72 – 721E → K in XLRS1. 5 Publications
VAR_008181
Natural varianti73 – 731S → P in XLRS1. 1 Publication
VAR_065326
Natural varianti74 – 741G → V in XLRS1. 2 Publications
VAR_008182
Natural varianti85 – 851Missing in XLRS1. 1 Publication
VAR_023959
Natural varianti89 – 891Y → C in XLRS1. 1 Publication
VAR_008215
Natural varianti96 – 961W → R in XLRS1. 2 Publications
VAR_008183
Natural varianti98 – 981A → E in XLRS1. 1 Publication
VAR_008216
Natural varianti102 – 1021R → Q in XLRS1. 3 Publications
VAR_008217
Natural varianti102 – 1021R → W in XLRS1. 1 Publication
VAR_008184
Natural varianti103 – 1031L → R in XLRS1.
VAR_008218
Natural varianti108 – 1081F → C in XLRS1. 1 Publication
VAR_008219
Natural varianti109 – 1091G → E in XLRS1. 1 Publication
VAR_008220
Natural varianti109 – 1091G → R in XLRS1. 1 Publication
VAR_008185
Natural varianti109 – 1091G → W in XLRS1. 1 Publication
VAR_008221
Natural varianti110 – 1101C → Y in XLRS1.
VAR_008222
Natural varianti112 – 1121W → C in XLRS1.
VAR_008223
Natural varianti113 – 1131L → F in XLRS1.
VAR_008224
Natural varianti127 – 1271L → P in XLRS1.
VAR_008225
Natural varianti135 – 1351G → V in XLRS1.
VAR_008226
Natural varianti136 – 1361I → T in XLRS1.
VAR_008227
Natural varianti138 – 1381T → A in XLRS1.
VAR_008228
Natural varianti140 – 1401G → E in XLRS1.
VAR_008229
Natural varianti140 – 1401G → R in XLRS1. 2 Publications
VAR_008230
Natural varianti141 – 1411R → C in XLRS1. 2 Publications
VAR_008231
Natural varianti141 – 1411R → G in XLRS1.
VAR_008232
Natural varianti141 – 1411R → H in XLRS1. 1 Publication
VAR_008233
Natural varianti142 – 1421C → W in XLRS1. 1 Publication
VAR_008234
Natural varianti143 – 1431D → V in XLRS1.
VAR_008235
Natural varianti145 – 1451D → H in XLRS1. 1 Publication
VAR_065327
Natural varianti146 – 1461E → D in XLRS1.
VAR_008236
Natural varianti146 – 1461E → K in XLRS1. 1 Publication
VAR_008237
Natural varianti155 – 1551Y → C in XLRS1.
VAR_008238
Natural varianti156 – 1561R → G in XLRS1. 1 Publication
VAR_065328
Natural varianti158 – 1581D → N.
Corresponds to variant rs1800002 [ dbSNP | Ensembl ].
VAR_008239
Natural varianti163 – 1631W → C in XLRS1. 1 Publication
VAR_008240
Natural varianti178 – 1781G → D in XLRS1.
VAR_008241
Natural varianti182 – 1821R → C in XLRS1. 1 Publication
VAR_008242
Natural varianti192 – 1921P → L in XLRS1. 1 Publication
VAR_065329
Natural varianti192 – 1921P → R in XLRS1.
VAR_008243
Natural varianti192 – 1921P → S in XLRS1. 2 Publications
VAR_008244
Natural varianti193 – 1931P → L in XLRS1. 1 Publication
VAR_008245
Natural varianti193 – 1931P → S in XLRS1. 1 Publication
VAR_008246
Natural varianti197 – 1971R → C in XLRS1. 1 Publication
VAR_008247
Natural varianti197 – 1971R → H in XLRS1.
VAR_008248
Natural varianti199 – 1991I → T in XLRS1.
VAR_008249
Natural varianti200 – 2001R → C in XLRS1. 3 Publications
VAR_008251
Natural varianti200 – 2001R → H in XLRS1. 1 Publication
VAR_008252
Natural varianti203 – 2031P → L in XLRS1. 1 Publication
VAR_008253
Natural varianti207 – 2071H → Q in XLRS1.
VAR_008254
Natural varianti209 – 2091R → C in XLRS1. 1 Publication
VAR_065330
Natural varianti209 – 2091R → H in XLRS1. 1 Publication
VAR_008255
Natural varianti213 – 2131R → Q in XLRS1. 1 Publication
VAR_065331
Natural varianti213 – 2131R → W in XLRS1.
VAR_008256
Natural varianti215 – 2151E → K in XLRS1. 1 Publication
VAR_008257
Natural varianti215 – 2151E → Q in XLRS1.
VAR_008258
Natural varianti216 – 2161L → P in XLRS1.
VAR_008259
Natural varianti219 – 2191C → G in XLRS1.
VAR_008260
Natural varianti219 – 2191C → R in XLRS1.
VAR_008261
Natural varianti222 – 2221K → N.
Corresponds to variant rs1800004 [ dbSNP | Ensembl ].
VAR_012078
Natural varianti223 – 2231C → R in XLRS1. 2 Publications
VAR_008262

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018963
, AF018958, AF018959, AF018960, AF018961, AF018962 Genomic DNA. Translation: AAC18405.1.
AF014459 mRNA. Translation: AAC17928.1.
Z92542, Z94056 Genomic DNA. Translation: CAI42483.1.
Z94056, Z92542 Genomic DNA. Translation: CAI42776.1.
DQ426892 mRNA. Translation: ABD90543.1.
CCDSiCCDS14187.1.
RefSeqiNP_000321.1. NM_000330.3.
UniGeneiHs.715725.

Genome annotation databases

EnsembliENST00000379984; ENSP00000369320; ENSG00000102104.
GeneIDi6247.
KEGGihsa:6247.
UCSCiuc004cyo.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the RS1 gene

Retina International's Scientific Newsletter

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF018963
, AF018958, AF018959, AF018960, AF018961, AF018962 Genomic DNA. Translation: AAC18405.1.
AF014459 mRNA. Translation: AAC17928.1.
Z92542, Z94056 Genomic DNA. Translation: CAI42483.1.
Z94056, Z92542 Genomic DNA. Translation: CAI42776.1.
DQ426892 mRNA. Translation: ABD90543.1.
CCDSiCCDS14187.1.
RefSeqiNP_000321.1. NM_000330.3.
UniGeneiHs.715725.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3JD6electron microscopy4.10O24-224[»]
ProteinModelPortaliO15537.
SMRiO15537. Positions 68-219.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112161. 2 interactions.
IntActiO15537. 3 interactions.
STRINGi9606.ENSP00000369320.

PTM databases

iPTMnetiO15537.
PhosphoSiteiO15537.

Polymorphism and mutation databases

BioMutaiRS1.

Proteomic databases

PaxDbiO15537.
PeptideAtlasiO15537.
PRIDEiO15537.

Protocols and materials databases

DNASUi6247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379984; ENSP00000369320; ENSG00000102104.
GeneIDi6247.
KEGGihsa:6247.
UCSCiuc004cyo.4. human.

Organism-specific databases

CTDi6247.
GeneCardsiRS1.
GeneReviewsiRS1.
HGNCiHGNC:10457. RS1.
MalaCardsiRS1.
MIMi300839. gene.
312700. phenotype.
neXtProtiNX_O15537.
Orphaneti792. X-linked retinoschisis.
PharmGKBiPA34871.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IIHQ. Eukaryota.
ENOG410YGW6. LUCA.
GeneTreeiENSGT00760000119073.
HOGENOMiHOG000006700.
HOVERGENiHBG061301.
InParanoidiO15537.
OMAiAWLSKYQ.
OrthoDBiEOG091G0HLO.
PhylomeDBiO15537.

Miscellaneous databases

GeneWikiiRetinoschisin.
GenomeRNAii6247.
PROiO15537.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000102104.
CleanExiHS_RS1.
GenevisibleiO15537. HS.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000421. FA58C.
IPR008979. Galactose-bd-like.
[Graphical view]
PfamiPF00754. F5_F8_type_C. 1 hit.
[Graphical view]
SMARTiSM00231. FA58C. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
PROSITEiPS01285. FA58C_1. 1 hit.
PS50022. FA58C_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiXLRS1_HUMAN
AccessioniPrimary (citable) accession number: O15537
Secondary accession number(s): Q0QD39
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: September 7, 2016
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.