Rs1
entrez
20147
canonical
uniprot
Q9Z1L4
canonical
ensembl
ENSMUSG00000031293
resolver
ensp
ENSMUSP00000033650
resolver
enst
ENSMUST00000033650
resolver
genesymbol
Rs1
resolver
genesymbol_syn
Rs1h
resolver
genesymbol_syn
Xlrs1
resolver
uniprot_entry
XLRS1_MOUSE
resolver
amino_acid_sequence
MPHKIEGFFLLLLFGYEATLGLSSTEDEGEDPWYQKACKCDCQVGANALWSAGATSLDCIPECPYHKPLGFESGEVTPDQITCSNPEQYVGWYSSWTANKARLNSQGFGCAWLSKYQDSSQWLQIDLKEIKVISGILTQGRCDIDEWVTKYSVQYRTDERLNWIYYKDQTGNNRVFYGNSDRSSTVQNLLRPPIISRFIRLIPLGWHVRIAIRMELLECASKCA
uniprot
proteins
function
FUNCTION: Binds negatively charged membrane lipids, such as phosphatidylserine and phosphoinositides (PubMed:17325137, PubMed:20677810). 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 (By similarity). Required for normal structure and function of the retina (PubMed:11983912, PubMed:17325137). {ECO:0000250|UniProtKB:O15537, ECO:0000269|PubMed:11983912, ECO:0000269|PubMed:17325137, ECO:0000269|PubMed:20677810}.
uniprot
proteins
mass_dalton
25575
uniprot
proteins
mutagenesis
MUTAGEN 89; /note="Y->C: Decreases phosphatidylserine binding."; /evidence="ECO:0000269|PubMed:17325137"; MUTAGEN 92; /note="W->C: Decreases phosphatidylserine binding."; /evidence="ECO:0000269|PubMed:17325137
uniprot
proteins
pubmed
10023077
uniprot
proteins
pubmed
10051329
uniprot
proteins
pubmed
10915776
uniprot
proteins
pubmed
11983912
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
17325137
uniprot
proteins
pubmed
20677810
uniprot
proteins
sequence_length
224
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:O15537}. Cell membrane {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}; Peripheral membrane protein {ECO:0000269|PubMed:17325137, ECO:0000269|PubMed:20677810}; Extracellular side {ECO:0000269|PubMed:17325137, ECO:0000305|PubMed:20677810}. 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:0000269|PubMed:20677810}.
uniprot
proteins