BST2
entrez
684
canonical
uniprot
Q10589
canonical
ensembl
ENSG00000130303
resolver
ensp
ENSP00000252593
resolver
genesymbol
BST2
resolver
hgnc
HGNC:1119
resolver
uniprot
A8K4Y4
resolver
uniprot
Q53G07
resolver
uniprot_entry
BST2_HUMAN
resolver
uniprot_sec
A8K4Y4
resolver
uniprot_sec
Q53G07
resolver
amino_acid_sequence
MASTSYDYCRVPMEDGDKRCKLLLGIGILVLLIIVILGVPLIIFTIKANSEACRDGLRAVMECRNVTHLLQQELTEAQKGFQDVEAQAATCNHTVMALMASLDAEKAQGQKKVEELEGEITTLNHKLQDASAEVERLRRENQVLSVRIADKKYYPSSQDSSSAAAPQLLIVLLGLSALLQ
uniprot
proteins
function
FUNCTION: IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted (PubMed:18200009, PubMed:18342597, PubMed:19036818, PubMed:19879838, PubMed:20019814, PubMed:20399176, PubMed:20419159, PubMed:20940320, PubMed:21529378, PubMed:22520941, PubMed:37922253). Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae: influenza A virus, paramyxoviridae: nipah virus, and coronaviridae: SARS-CoV (PubMed:18200009, PubMed:18342597, PubMed:19179289, PubMed:19879838, PubMed:20399176, PubMed:20419159, PubMed:20686043, PubMed:20943977, PubMed:21529378, PubMed:21621240, PubMed:22520941, PubMed:26378163, PubMed:31199522). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration (PubMed:22065321). Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection (PubMed:19564354, PubMed:26172439). Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells. Isoform 1 and isoform 2 are both effective viral restriction factors but have differing antiviral and signaling activities (PubMed:23028328, PubMed:26172439). Isoform 2 is resistant to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in the presence of Vpu (PubMed:23028328, PubMed:26172439). Isoform 1 acts as an activator of NF-kappa-B and this activity is inhibited by isoform 2 (PubMed:23028328). {ECO:0000269|PubMed:18200009, ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19036818, ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20019814, ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21529378, ECO:0000269|PubMed:21621240, ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:22520941, ECO:0000269|PubMed:23028328, ECO:0000269|PubMed:26172439, ECO:0000269|PubMed:26378163, ECO:0000269|PubMed:31199522, ECO:0000269|PubMed:37922253}.
uniprot
proteins
mass_dalton
19769
uniprot
proteins
mutagenesis
MUTAGEN 3..5; /note="STS->AAA: Partial resistance to Vpu."; /evidence="ECO:0000269|PubMed:23028328"; MUTAGEN 6; /note="Y->A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-8."; /evidence="ECO:0000269|PubMed:23028328"; MUTAGEN 8; /note="Y->A: Partial resistance to Vpu and significantly reduced activation of NF-kB; when associated with A-6."; /evidence="ECO:0000269|PubMed:23028328"; MUTAGEN 18; /note="K->R: Abolishes redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5."; /evidence="ECO:0000269|PubMed:20419159"; MUTAGEN 21; /note="K->R: No effect on redistribution to late endosomes in cells expressing KSH virus E3 ubiquitin-protein ligase K5."; /evidence="ECO:0000269|PubMed:20419159"; MUTAGEN 53; /note="C->A: Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-63 and A-91."; /evidence="ECO:0000269|PubMed:31199522"; MUTAGEN 63; /note="C->A: Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-53 and A-91."; /evidence="ECO:0000269|PubMed:31199522"; MUTAGEN 65; /note="N->A: Loss of glycosylation site."; /evidence="ECO:0000269|PubMed:19879838"; MUTAGEN 91; /note="C->A: Prevents homodimerization and inhibition of SARS-CoV, HCoV-229E, and HIV-1 viral particles production ex vivo; when associated with A-53 and A-63."; /evidence="ECO:0000269|PubMed:31199522"; MUTAGEN 92; /note="N->A: Loss of glycosylation site. Impairs anti-viral activity."; /evidence="ECO:0000269|PubMed:19879838
uniprot
proteins
post_translational_modification
PTM: Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5, leading to its targeting to late endosomes and degradation. {ECO:0000269|PubMed:20419159}.; PTM: The GPI anchor is essential for its antiviral activity.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:37922253}.
uniprot
proteins
protein_family
Tetherin family
uniprot
proteins
pubmed
10329429
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15057824
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16157322
uniprot
proteins
pubmed
16602701
uniprot
proteins
pubmed
17566972
uniprot
proteins
pubmed
18200009
uniprot
proteins
pubmed
18342597
uniprot
proteins
pubmed
19036818
uniprot
proteins
pubmed
19159218
uniprot
proteins
pubmed
19179289
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19564354
uniprot
proteins
pubmed
19737401
uniprot
proteins
pubmed
19740980
uniprot
proteins
pubmed
19837671
uniprot
proteins
pubmed
19879838
uniprot
proteins
pubmed
19917491
uniprot
proteins
pubmed
20019814
uniprot
proteins
pubmed
20399176
uniprot
proteins
pubmed
20419159
uniprot
proteins
pubmed
20686043
uniprot
proteins
pubmed
20688520
uniprot
proteins
pubmed
20880831
uniprot
proteins
pubmed
20940320
uniprot
proteins
pubmed
20943977
uniprot
proteins
pubmed
21166593
uniprot
proteins
pubmed
21222046
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21529378
uniprot
proteins
pubmed
21621240
uniprot
proteins
pubmed
21994744
uniprot
proteins
pubmed
22065321
uniprot
proteins
pubmed
22180752
uniprot
proteins
pubmed
22509177
uniprot
proteins
pubmed
22520941
uniprot
proteins
pubmed
22811908
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23028328
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
26172439
uniprot
proteins
pubmed
26378163
uniprot
proteins
pubmed
31199522
uniprot
proteins
pubmed
37922253
uniprot
proteins
pubmed
7607676
uniprot
proteins
sequence_length
180
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell membrane {ECO:0000269|PubMed:26172439}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:26172439, ECO:0000269|PubMed:37922253}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19879838, ECO:0000305|PubMed:26172439}. Membrane raft. Cytoplasm. Apical cell membrane {ECO:0000250}. Note=Shuttles between the cell membrane, where it is present predominantly in membrane/lipid rafts, and the trans-Golgi network. Forms a complex with MMP14 and localizes to the cytoplasm.; SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:26172439}. Late endosome {ECO:0000269|PubMed:20419159}. Note=(Microbial infection) HIV-1 VPU and HIV-2 ENV can target it to the trans-Golgi network thus sequestering it away from virus assembly sites on the cell membrane. Targeted to late endosomes upon KSHV infection and subsequent ubiquitination. {ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:26172439}.
uniprot
proteins
transmembrane_region
TRANSMEM 21..48; /note="Helical; Signal-anchor for type II membrane protein"; /evidence="ECO:0000255
uniprot
proteins