BSG
entrez
682
canonical
uniprot
P35613
canonical
ensembl
ENSG00000172270
resolver
ensp
ENSP00000333769
resolver
ensp
ENSP00000343809
resolver
ensp
ENSP00000344707
resolver
ensp
ENSP00000473664
resolver
genesymbol
BSG
resolver
genesymbol
hEMMPRIN
resolver
genesymbol_syn
BSG
resolver
hgnc
HGNC:1116
resolver
uniprot
A6NJW1
resolver
uniprot
D3YLG5
resolver
uniprot
Q54A51
resolver
uniprot
Q7Z796
resolver
uniprot
Q8IZL7
resolver
uniprot_entry
BASI_HUMAN
resolver
uniprot_entry
Q54A51_HUMAN
resolver
uniprot_sec
A6NJW1
resolver
uniprot_sec
D3YLG5
resolver
uniprot_sec
Q7Z796
resolver
uniprot_sec
Q8IZL7
resolver
amino_acid_sequence
MAAALFVLLGFALLGTHGASGAAGFVQAPLSQQRWVGGSVELHCEAVGSPVPEIQWWFEGQGPNDTCSQLWDGARLDRVHIHATYHQHAASTISIDTLVEEDTGTYECRASNDPDRNHLTRAPRVKWVRAQAVVLVLEPGTVFTTVEDLGSKILLTCSLNDSATEVTGHRWLKGGVVLKEDALPGQKTEFKVDSDDQWGEYSCVFLPEPMGTANIQLHGPPRVKAVKSSEHINEGETAMLVCKSESVPPVTDWAWYKITDSEDKALMNGSESRFFVSSSQGRSELHIENLNMEADPGQYRCNGTSSKGSDQAIITLRVRSHLAALWPFLGIVAEVLVLVTIIFIYEKRRKPEDVLDDDDAGSAPLKSSGQHQNDKGKNVRQRNSS
uniprot
proteins
function
FUNCTION: [Isoform 1]: Essential for normal retinal maturation and development (By similarity). Acts as a retinal cell surface receptor for NXNL1 and plays an important role in NXNL1-mediated survival of retinal cone photoreceptors (PubMed:25957687). In association with glucose transporter SLC16A1/GLUT1 and NXNL1, promotes retinal cone survival by enhancing aerobic glycolysis and accelerating the entry of glucose into photoreceptors (PubMed:25957687). May act as a potent stimulator of IL6 secretion in multiple cell lines that include monocytes (PubMed:21620857). {ECO:0000250|UniProtKB:P18572, ECO:0000269|PubMed:21620857, ECO:0000269|PubMed:25957687}.; FUNCTION: [Isoform 1]: (Microbial infection) Erythrocyte receptor for P.falciparum RH5 which is essential for erythrocyte invasion by the merozoite stage of P.falciparum isolates 3D7 and Dd2. {ECO:0000269|PubMed:22080952}.; FUNCTION: [Isoform 2]: Signaling receptor for cyclophilins, essential for PPIA/CYPA and PPIB/CYPB-dependent signaling related to chemotaxis and adhesion of immune cells (PubMed:11688976, PubMed:11943775). Plays an important role in targeting monocarboxylate transporters SLC16A1/GLUT1, SLC16A11 and SLC16A12 to the plasma membrane (PubMed:17127621, PubMed:21778275, PubMed:28666119). Acts as a coreceptor for vascular endothelial growth factor receptor 2 (KDR/VEGFR2) in endothelial cells enhancing its VEGFA-mediated activation and downstream signaling (PubMed:25825981). Promotes angiogenesis through EPAS1/HIF2A-mediated up-regulation of VEGFA (isoform VEGF-165 and VEGF-121) and KDR/VEGFR2 in endothelial cells (PubMed:19837976). Plays a key role in regulating tumor growth, invasion, metastasis and neoangiogenesis by stimulating the production and release of extracellular matrix metalloproteinases and KDR/VEGFR2 by both tumor cells and stromal cells (fibroblasts and endothelial cells) (PubMed:11992541, PubMed:12553375, PubMed:15833850). {ECO:0000269|PubMed:11688976, ECO:0000269|PubMed:11943775, ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:12553375, ECO:0000269|PubMed:15833850, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:19837976, ECO:0000269|PubMed:21778275, ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:28666119}.; FUNCTION: [Isoform 2]: (Microbial infection) Erythrocyte receptor for P.falciparum RH5 which is essential for erythrocyte invasion by the merozoite stage of P.falciparum isolates 3D7, Dd2, 7G8 and HB3 (PubMed:22080952, PubMed:26195724). Binding of P.falciparum RH5 results in BSG dimerization which triggers an increase in intracellular Ca(2+) in the erythrocyte (PubMed:28409866). This essential step leads to a rearrangement of the erythrocyte cytoskeleton required for the merozoite invasion (PubMed:28409866). {ECO:0000269|PubMed:22080952, ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866}.; FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate human SARS coronavirus (SARS-CoV-1) infection via its interaction with virus-associated PPIA/CYPA. {ECO:0000269|PubMed:15688292}.; FUNCTION: [Isoform 2]: (Microbial infection) Can facilitate HIV-1 infection via its interaction with virus-associated PPIA/CYPA. {ECO:0000269|PubMed:11353871}.; FUNCTION: [Isoform 2]: (Microbial infection) First described as a receptor for severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), it is not required for SARS-CoV-2 infection. {ECO:0000269|PubMed:33432067, ECO:0000303|PubMed:32307653}.; FUNCTION: [Isoform 2]: (Microbial infection) Acts as a receptor for measles virus. {ECO:0000269|PubMed:20147391}.; FUNCTION: [Isoform 2]: (Microbial infection) Promotes entry of pentamer-expressing human cytomegalovirus (HCMV) into epithelial and endothelial cells. {ECO:0000269|PubMed:29739904}.; FUNCTION: Plays a role in neurite outgrowth. {ECO:0000250|UniProtKB:P18572}.
uniprot
proteins
mass_dalton
42200
uniprot
proteins
mutagenesis
MUTAGEN 67; /note="C->M: Loss of ability to stimulate interleukin-6 secretion."; /evidence="ECO:0000269|PubMed:21620857"; MUTAGEN 160; /note="N->D: No effect on the interaction with P.falciparum RH5; when associated with D-268 and D-302."; /evidence="ECO:0000269|PubMed:22080952"; MUTAGEN 268; /note="N->D: No effect on the interaction with P.falciparum RH5; when associated with D-160 and D-302."; /evidence="ECO:0000269|PubMed:22080952"; MUTAGEN 302; /note="N->D: No effect on the interaction with P.falciparum RH5; when associated with D-160 and D-268."; /evidence="ECO:0000269|PubMed:22080952"; MUTAGEN P35613-2:27; /note="F->L: Severe reduction in the interaction with P.falciparum RH5."; /evidence="ECO:0000269|PubMed:24297912"; MUTAGEN P35613-2:32; /note="D->E: No effect on the interaction with P.falciparum RH5."; /evidence="ECO:0000269|PubMed:24297912"; MUTAGEN P35613-2:75; /note="K->E: No effect on the interaction with P.falciparum RH5."; /evidence="ECO:0000269|PubMed:24297912"; MUTAGEN P35613-2:100; /note="Q->K: Severe reduction in the interaction with P.falciparum RH5."; /evidence="ECO:0000269|PubMed:24297912"; MUTAGEN P35613-2:102; /note="H->HH: Severe reduction in the interaction with P.falciparum RH5."; /evidence="ECO:0000269|PubMed:24297912"; MUTAGEN P35613-2:144; /note="D->A: Reduced interaction with KDR/VEGFR2."; /evidence="ECO:0000269|PubMed:25825981"; MUTAGEN P35613-2:180..181; /note="PG->AA: Loss of its ability to mediate chemotactic activity of PPIA/CYPA."; /evidence="ECO:0000269|PubMed:11943775"; MUTAGEN P35613-2:182; /note="Q->A: Reduced interaction with KDR/VEGFR2. Significant loss of interaction with KDR/VEGFR2; when associated with A-184."; /evidence="ECO:0000269|PubMed:25825981"; MUTAGEN P35613-2:184; /note="R->A: Reduced interaction with KDR/VEGFR2. Significant loss of interaction with KDR/VEGFR2; when associated with A-182."; /evidence="ECO:0000269|PubMed:25825981"; MUTAGEN P35613-2:195; /note="Q->A: Reduced interaction with KDR/VEGFR2. Complete loss of interaction with KDR/VEGFR2 when associated with A-199."; /evidence="ECO:0000269|PubMed:25825981"; MUTAGEN P35613-2:199; /note="T->A: Reduced interaction with KDR/VEGFR2. Complete loss of interaction with KDR/VEGFR2; when associated with A-195."; /evidence="ECO:0000269|PubMed:25825981"; MUTAGEN P35613-2:211; /note="P->A: Loss of interaction with PPIL2."; /evidence="ECO:0000269|PubMed:15946952
uniprot
proteins
post_translational_modification
PTM: [Isoform 2]: N-glycosylated. {ECO:0000269|PubMed:21536654}.; PTM: [Isoform 3]: N-glycosylated. {ECO:0000269|PubMed:21536654}.; PTM: [Isoform 4]: N-glycosylated. {ECO:0000269|PubMed:21536654}.
uniprot
proteins
pubmed
11353871
uniprot
proteins
pubmed
11688976
uniprot
proteins
pubmed
11943775
uniprot
proteins
pubmed
11992541
uniprot
proteins
pubmed
12553375
uniprot
proteins
pubmed
12754519
uniprot
proteins
pubmed
12792908
uniprot
proteins
pubmed
12939332
uniprot
proteins
pubmed
12975309
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15340161
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15688292
uniprot
proteins
pubmed
15833850
uniprot
proteins
pubmed
15946952
uniprot
proteins
pubmed
1634773
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17127621
uniprot
proteins
pubmed
17267690
uniprot
proteins
pubmed
1783610
uniprot
proteins
pubmed
18430721
uniprot
proteins
pubmed
1846736
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19768682
uniprot
proteins
pubmed
19837976
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20147391
uniprot
proteins
pubmed
21245143
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21536654
uniprot
proteins
pubmed
21620857
uniprot
proteins
pubmed
21778275
uniprot
proteins
pubmed
22080952
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24297912
uniprot
proteins
pubmed
25132548
uniprot
proteins
pubmed
25825981
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
25957687
uniprot
proteins
pubmed
26195724
uniprot
proteins
pubmed
27503893
uniprot
proteins
pubmed
28409866
uniprot
proteins
pubmed
28666119
uniprot
proteins
pubmed
29739904
uniprot
proteins
pubmed
32307653
uniprot
proteins
pubmed
32867305
uniprot
proteins
pubmed
33333023
uniprot
proteins
pubmed
33432067
uniprot
proteins
pubmed
34625749
uniprot
proteins
pubmed
37158588
uniprot
proteins
pubmed
38364890
uniprot
proteins
pubmed
7812975
uniprot
proteins
pubmed
9130641
uniprot
proteins
pubmed
9767135
uniprot
proteins
sequence_length
385
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:25957687}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P18572}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P18572}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:11992541, ECO:0000269|PubMed:15688292, ECO:0000269|PubMed:15946952, ECO:0000269|PubMed:17127621, ECO:0000269|PubMed:21536654, ECO:0000269|PubMed:25825981, ECO:0000269|PubMed:26195724, ECO:0000269|PubMed:28409866, ECO:0000269|PubMed:29739904}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Endosome {ECO:0000269|PubMed:29739904}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:15688292}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}. Basolateral cell membrane {ECO:0000269|PubMed:17267690}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000269|PubMed:21536654}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P26453}.
uniprot
proteins
transmembrane_region
TRANSMEM 326..344; /note="Helical"; /evidence="ECO:0000269|PubMed:34625749, ECO:0000269|PubMed:38364890, ECO:0007744|PDB:7DCE, ECO:0007744|PDB:8XEJ
uniprot
proteins