RS1
entrez
6247
canonical
uniprot
O15537
canonical
ensembl
ENSG00000102104
resolver
ensp
ENSP00000369320
resolver
enst
ENST00000379984
resolver
genesymbol
RS1
resolver
genesymbol_syn
XLRS1
resolver
hgnc
HGNC:10457
resolver
uniprot
Q0QD39
resolver
uniprot_entry
XLRS1_HUMAN
resolver
uniprot_sec
Q0QD39
resolver
amino_acid_sequence
MSRKIEGFLLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQGGPNALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKFQDSSQWLQIDLKEIKVISGILTQGRCDIDEWMTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRTSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECVSKCA
uniprot
proteins
disease_involvement
DISEASE: Retinoschisis juvenile X-linked 1 (XLRS1) [MIM:312700]: A 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. {ECO:0000269|PubMed:10079181, ECO:0000269|PubMed:10220153, ECO:0000269|PubMed:10234514, ECO:0000269|PubMed:10450864, ECO:0000269|PubMed:10533068, ECO:0000269|PubMed:17304551, ECO:0000269|PubMed:17615541, ECO:0000269|PubMed:17631851, ECO:0000269|PubMed:19093009, ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:27798099, ECO:0000269|PubMed:9326935, ECO:0000269|PubMed:9618178, ECO:0000269|PubMed:9760195, ECO:0000269|Ref.15}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (By similarity). May play a role in cell-cell adhesion processes in the retina, via homomeric interaction between octamers present on the surface of two neighboring cells (PubMed:27114531). Required for normal structure and function of the retina (PubMed:19093009). {ECO:0000250|UniProtKB:Q9Z1L4, ECO:0000269|PubMed:19093009, ECO:0000305|PubMed:27114531}.
uniprot
proteins
mass_dalton
25592
uniprot
proteins
pubmed
10079181
uniprot
proteins
pubmed
10220153
uniprot
proteins
pubmed
10234514
uniprot
proteins
pubmed
10450864
uniprot
proteins
pubmed
10533068
uniprot
proteins
pubmed
10915776
uniprot
proteins
pubmed
15644328
uniprot
proteins
pubmed
15772651
uniprot
proteins
pubmed
17286855
uniprot
proteins
pubmed
17304551
uniprot
proteins
pubmed
17615541
uniprot
proteins
pubmed
17631851
uniprot
proteins
pubmed
19093009
uniprot
proteins
pubmed
19849666
uniprot
proteins
pubmed
26812435
uniprot
proteins
pubmed
27114531
uniprot
proteins
pubmed
27798099
uniprot
proteins
pubmed
9326935
uniprot
proteins
pubmed
9618178
uniprot
proteins
pubmed
9760195
uniprot
proteins
sequence_length
224
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10915776, ECO:0000269|PubMed:19849666, ECO:0000269|PubMed:26812435}. Cell membrane {ECO:0000250|UniProtKB:Q9Z1L4}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9Z1L4}; Extracellular side {ECO:0000250|UniProtKB:Q9Z1L4}. Note=Binds to phosphatidylserine-containing lipid membranes and embeds itself partially into the lipid bilayer. Lipid-binding requires the presence of Ca(2+) ions. {ECO:0000250|UniProtKB:Q9Z1L4}.
uniprot
proteins