Scarb2
entrez
12492
canonical
uniprot
O35114
canonical
ensembl
ENSMUSG00000029426
resolver
ensp
ENSMUSP00000031377
resolver
enst
ENSMUST00000031377
resolver
genesymbol
Scarb2
resolver
uniprot
Q3UNF8
resolver
uniprot_entry
SCRB2_MOUSE
resolver
uniprot_sec
Q3UNF8
resolver
amino_acid_sequence
MGRCCFYTAGTLSLLLLVTSVTLLVARVFQKAVDQTIEKNMVLQNGTKVFNSWEKPPLPVYIQFYFFNVTNPEEILQGEIPLLEEVGPYTYRELRNKANIQFGENGTTISAVTNKAYVFERNQSVGDPNVDLIRTINIPLLTVVDLAQLTLLRELIEAMLKAYQQKLFVIHTVHELLWGYKDEILSLVHIFKPDVSPNFGLFYERNGTNDGEYVFLTGEDNYLNFSKIVEWNGKTSLDWWTTDTCNMINGTDGDSFHPLISKDEVLYLFPSDLCRSVHITFSSFENVEGLPAFRYKVPAEILANTSENAGFCIPEGNCMDSGVLNISICKNGAPIIMSFPHFYQADEKFVSAIKGMHPNKEEHESFVDINPLTGIILRGAKRFQINTYVRKLDDFVETGDIRTMVFPVMYLNESVLIDKETANQLKSVINTTLVVTNIPYIIMALGVFFGLVFTWLACRGQGSMDEGTADERAPLIRT
uniprot
proteins
function
FUNCTION: Acts as a lysosomal receptor for glucosylceramidase (GBA1) targeting. {ECO:0000269|PubMed:18022370, ECO:0000269|PubMed:24162852}.
uniprot
proteins
mass_dalton
54044
uniprot
proteins
mutagenesis
MUTAGEN 45; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 68; /note="N->Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 105; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 122; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 155; /note="L->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 156; /note="I->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 159; /note="M->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 160; /note="L->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 162; /note="A->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 163; /note="Y->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 166; /note="K->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 184; /note="I->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 187; /note="L->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 191; /note="F->D: Abolishes interaction with GBA1. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 206; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 224; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 249; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 304; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 325; /note="N->Q: Loss of glycosylation site. Causes retention in the endoplasmic reticulum and abolishes normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 400; /note="D->K: Slightly increased GBA1 binding. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 412; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852"; MUTAGEN 430; /note="N->Q: Loss of glycosylation site. No effect on normal location in lysosomes."; /evidence="ECO:0000269|PubMed:24162852
uniprot
proteins
post_translational_modification
PTM: Acylated by palmitic acid group(s). {ECO:0000250}.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:19349973}.
uniprot
proteins
protein_family
CD36 family
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
18022370
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
24162852
uniprot
proteins
pubmed
9399579
uniprot
proteins
sequence_length
478
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}; Multi-pass membrane protein {ECO:0000269|PubMed:24162852, ECO:0000269|PubMed:9399579}.
uniprot
proteins
transmembrane_region
TRANSMEM 5..27; /note="Helical"; /evidence="ECO:0000255"; TRANSMEM 434..459; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins