ID BST2_HUMAN Reviewed; 180 AA. AC Q10589; A8K4Y4; Q53G07; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 27-MAR-2024, entry version 190. DE RecName: Full=Bone marrow stromal antigen 2; DE Short=BST-2; DE AltName: Full=HM1.24 antigen; DE AltName: Full=Tetherin; DE AltName: CD_antigen=CD317; DE Flags: Precursor; GN Name=BST2; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=7607676; DOI=10.1016/0888-7543(95)80171-h; RA Ishikawa J., Kaisho T., Tomizawa H., Lee B.O., Kobune Y., Inazawa J., RA Oritani K., Itoh M., Ochi T., Ishihara K., Hirano T.; RT "Molecular cloning and chromosomal mapping of a bone marrow stromal cell RT surface gene, BST2, that may be involved in pre-B-cell growth."; RL Genomics 26:527-534(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND SUBUNIT. RX PubMed=10329429; DOI=10.1006/bbrc.1999.0683; RA Ohtomo T., Sugamata Y., Ozaki Y., Ono K., Yoshimura Y., Kawai S., RA Koishihara Y., Ozaki S., Kosaka M., Hirano T., Tsuchiya M.; RT "Molecular cloning and characterization of a surface antigen preferentially RT overexpressed on multiple myeloma cells."; RL Biochem. Biophys. Res. Commun. 258:583-591(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., RA Tanaka A., Yokoyama S.; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Blood; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP TISSUE SPECIFICITY, INDUCTION BY B-CELL ACTIVATION, AND NOMENCLATURE. RX PubMed=16157322; DOI=10.1016/j.cellimm.2005.08.002; RA Vidal-Laliena M., Romero X., March S., Requena V., Petriz J., Engel P.; RT "Characterization of antibodies submitted to the B cell section of the 8th RT Human Leukocyte Differentiation Antigens Workshop by flow cytometry and RT immunohistochemistry."; RL Cell. Immunol. 236:6-16(2005). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY, AND GPI-ANCHOR [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16602701; DOI=10.1021/pr050419u; RA Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S., RA Brodbeck U., Peck S.C., Jensen O.N.; RT "Modification-specific proteomics of plasma membrane proteins: RT identification and characterization of glycosylphosphatidylinositol- RT anchored proteins released upon phospholipase D treatment."; RL J. Proteome Res. 5:935-943(2006). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=17566972; DOI=10.1002/pmic.200700068; RA Omaetxebarria M.J., Elortza F., Rodriguez-Suarez E., Aloria K., RA Arizmendi J.M., Jensen O.N., Matthiesen R.; RT "Computational approach for identification and characterization of GPI- RT anchored peptides in proteomics experiments."; RL Proteomics 7:1951-1960(2007). RN [11] RP FUNCTION IN HIV-1 INFECTION, AND INDUCTION BY HIV-1 VPU (MICROBIAL RP INFECTION). RX PubMed=18342597; DOI=10.1016/j.chom.2008.03.001; RA Van Damme N., Goff D., Katsura C., Jorgenson R.L., Mitchell R., RA Johnson M.C., Stephens E.B., Guatelli J.; RT "The interferon-induced protein BST-2 restricts HIV-1 release and is RT downregulated from the cell surface by the viral Vpu protein."; RL Cell Host Microbe 3:245-252(2008). RN [12] RP FUNCTION, AND INDUCTION NY HIV-1 VPU (MICROBIAL INFECTION). RX PubMed=18200009; DOI=10.1038/nature06553; RA Neil S.J., Zang T., Bieniasz P.D.; RT "Tetherin inhibits retrovirus release and is antagonized by HIV-1 Vpu."; RL Nature 451:425-430(2008). RN [13] RP FUNCTION, AND INTERACTION WITH RNF115. RX PubMed=20019814; DOI=10.1371/journal.ppat.1000700; RA Miyakawa K., Ryo A., Murakami T., Ohba K., Yamaoka S., Fukuda M., RA Guatelli J., Yamamoto N.; RT "BCA2/Rabring7 promotes tetherin-dependent HIV-1 restriction."; RL PLoS Pathog. 5:e1000700-e1000700(2009). RN [14] RP FUNCTION IN HIV-1 INFECTION, GLYCOSYLATION AT ASN-65 AND ASN-92, RP SUBCELLULAR LOCATION, DISULFIDE BONDS, SUBUNIT, TOPOLOGY, GPI-ANCHOR, AND RP MUTAGENESIS OF ASN-65 AND ASN-92. RX PubMed=19879838; DOI=10.1016/j.cell.2009.08.039; RA Perez-Caballero D., Zang T., Ebrahimi A., McNatt M.W., Gregory D.A., RA Johnson M.C., Bieniasz P.D.; RT "Tetherin inhibits HIV-1 release by directly tethering virions to cells."; RL Cell 139:499-511(2009). RN [15] RP REVIEW. RX PubMed=19917491; DOI=10.1016/j.chom.2009.11.002; RA Gupta R.K., Towers G.J.; RT "A tail of Tetherin: how pandemic HIV-1 conquered the world."; RL Cell Host Microbe 6:393-395(2009). RN [16] RP INTERACTION WITH HIV-1 VPU (MICROBIAL INFECTION), AND INDUCTION BY HIV-1 RP VPU (MICROBIAL INFECTION). RX PubMed=19837671; DOI=10.1074/jbc.m109.058305; RA Iwabu Y., Fujita H., Kinomoto M., Kaneko K., Ishizaka Y., Tanaka Y., RA Sata T., Tokunaga K.; RT "HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin RT through transmembrane interactions leading to lysosomes."; RL J. Biol. Chem. 284:35060-35072(2009). RN [17] RP FUNCTION, AND INTERACTION WITH LILRA4/ILT7. RX PubMed=19564354; DOI=10.1084/jem.20090547; RA Cao W., Bover L., Cho M., Wen X., Hanabuchi S., Bao M., Rosen D.B., RA Wang Y.H., Shaw J.L., Du Q., Li C., Arai N., Yao Z., Lanier L.L., Liu Y.J.; RT "Regulation of TLR7/9 responses in plasmacytoid dendritic cells by BST2 and RT ILT7 receptor interaction."; RL J. Exp. Med. 206:1603-1614(2009). RN [18] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of multiple RT enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [19] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=19036818; DOI=10.1128/jvi.02211-08; RA Jouvenet N., Neil S.J., Zhadina M., Zang T., Kratovac Z., Lee Y., RA McNatt M., Hatziioannou T., Bieniasz P.D.; RT "Broad-spectrum inhibition of retroviral and filoviral particle release by RT tetherin."; RL J. Virol. 83:1837-1844(2009). RN [20] RP INTERACTION WITH HIV-2 ENV (MICROBIAL INFECTION), SUBCELLULAR LOCATION, AND RP INDUCTION BY HIV-2 ENV (MICROBIAL INFECTION). RX PubMed=19740980; DOI=10.1128/jvi.01515-09; RA Le Tortorec A., Neil S.J.; RT "Antagonism to and intracellular sequestration of human tetherin by the RT human immunodeficiency virus type 2 envelope glycoprotein."; RL J. Virol. 83:11966-11978(2009). RN [21] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-65. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N-linked RT cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [22] RP FUNCTION, INTERACTION WITH EBOLA GP PROTEIN (MICROBIAL INFECTION), AND RP INDUCTION BY EBOLA GP PROTEIN (MICROBIAL INFECTION). RX PubMed=19179289; DOI=10.1073/pnas.0811014106; RA Kaletsky R.L., Francica J.R., Agrawal-Gamse C., Bates P.; RT "Tetherin-mediated restriction of filovirus budding is antagonized by the RT Ebola glycoprotein."; RL Proc. Natl. Acad. Sci. U.S.A. 106:2886-2891(2009). RN [23] RP GLYCOSYLATION AT ASN-65 AND ASN-92, SUBUNIT, AND DISULFIDE BONDS. RX PubMed=19737401; DOI=10.1186/1742-4690-6-80; RA Andrew A.J., Miyagi E., Kao S., Strebel K.; RT "The formation of cysteine-linked dimers of BST-2/tetherin is important for RT inhibition of HIV-1 virus release but not for sensitivity to Vpu."; RL Retrovirology 6:80-80(2009). RN [24] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20686043; DOI=10.1128/jvi.00103-10; RA Radoshitzky S.R., Dong L., Chi X., Clester J.C., Retterer C., Spurgers K., RA Kuhn J.H., Sandwick S., Ruthel G., Kota K., Boltz D., Warren T., RA Kranzusch P.J., Whelan S.P., Bavari S.; RT "Infectious Lassa virus, but not filoviruses, is restricted by BST- RT 2/tetherin."; RL J. Virol. 84:10569-10580(2010). RN [25] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=20943977; DOI=10.1128/jvi.01328-10; RA Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.; RT "Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit RT vesicular stomatitis virus infection via distinct mechanisms."; RL J. Virol. 84:12646-12657(2010). RN [26] RP FUNCTION IN KSHV AND HIV-1 INFECTION, SUBCELLULAR LOCATION (MICROBIAL RP INFECTION), MUTAGENESIS OF LYS-18 AND LYS-21, UBIQUITINATION AT LYS-18 BY RP KSH VIRUS E3 UBIQUITIN-PROTEIN LIGASE K5 (MICROBIAL INFECTION), AND RP INDUCTION BY KSHV K5 (MICROBIAL INFECTION). RX PubMed=20419159; DOI=10.1371/journal.ppat.1000843; RA Pardieu C., Vigan R., Wilson S.J., Calvi A., Zang T., Bieniasz P., RA Kellam P., Towers G.J., Neil S.J.; RT "The RING-CH ligase K5 antagonizes restriction of KSHV and HIV-1 particle RT release by mediating ubiquitin-dependent endosomal degradation of RT tetherin."; RL PLoS Pathog. 6:E1000843-E1000843(2010). RN [27] RP REVIEW. RX PubMed=20688520; DOI=10.1016/j.tim.2010.06.010; RA Evans D.T., Serra-Moreno R., Singh R.K., Guatelli J.C.; RT "BST-2/tetherin: a new component of the innate immune response to enveloped RT viruses."; RL Trends Microbiol. 18:388-396(2010). RN [28] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [29] RP REVIEW. RX PubMed=22180752; DOI=10.3389/fmicb.2011.00250; RA Arias J.F., Iwabu Y., Tokunaga K.; RT "structural basis for the antiviral activity of Bst-2/tetherin and its RT viral antagonism."; RL Front. Microbiol. 2:250-250(2011). RN [30] RP REVIEW. RX PubMed=21166593; DOI=10.1089/jir.2010.0108; RA Andrew A., Strebel K.; RT "The interferon-inducible host factor bone marrow stromal antigen RT 2/tetherin restricts virion release, but is it actually a viral restriction RT factor?"; RL J. Interferon Cytokine Res. 31:137-144(2011). RN [31] RP REVIEW. RX PubMed=21222046; DOI=10.1007/s11481-010-9256-1; RA Kuhl B.D., Cheng V., Wainberg M.A., Liang C.; RT "Tetherin and its viral antagonists."; RL J. Neuroimmun. Pharmacol. 6:188-201(2011). RN [32] RP FUNCTION. RX PubMed=21529378; DOI=10.1186/1743-422x-8-198; RA Xu F., Tan J., Liu R., Xu D., Li Y., Geng Y., Liang C., Qiao W.; RT "Tetherin inhibits prototypic foamy virus release."; RL Virol. J. 8:198-198(2011). RN [33] RP FUNCTION. RX PubMed=21621240; DOI=10.1016/j.virol.2011.05.006; RA Watanabe R., Leser G.P., Lamb R.A.; RT "Influenza virus is not restricted by tetherin whereas influenza VLP RT production is restricted by tetherin."; RL Virology 417:50-56(2011). RN [34] RP REVIEW. RX PubMed=21994744; DOI=10.3390/v3050520; RA Le Tortorec A., Willey S., Neil S.J.; RT "Antiviral inhibition of enveloped virus release by tetherin/BST-2: action RT and counteraction."; RL Viruses 3:520-540(2011). RN [35] RP REVIEW. RX PubMed=22509177; DOI=10.3389/fmicb.2012.00131; RA Sato K., Gee P., Koyanagi Y.; RT "Vpu and BST2: still not there yet?"; RL Front. Microbiol. 3:131-131(2012). RN [36] RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH MMP14. RX PubMed=22065321; DOI=10.1002/jcb.23433; RA Gu G., Zhao D., Yin Z., Liu P.; RT "BST-2 binding with cellular MT1-MMP blocks cell growth and migration via RT decreasing MMP2 activity."; RL J. Cell. Biochem. 113:1013-1021(2012). RN [37] RP REVIEW. RX PubMed=22811908; DOI=10.1155/2012/424768; RA Hammonds J., Wang J.J., Spearman P.; RT "Restriction of retroviral replication by tetherin/BST-2."; RL Mol. Biol. Int. 2012:424768-424768(2012). RN [38] RP FUNCTION, SUBUNIT, ALTERNATIVE INITIATION (ISOFORMS 1 AND 2), INDUCTION, RP AND MUTAGENESIS OF 3-SER--SER-5; TYR-6 AND TYR-8. RX PubMed=23028328; DOI=10.1371/journal.ppat.1002931; RA Cocka L.J., Bates P.; RT "Identification of alternatively translated Tetherin isoforms with RT differing antiviral and signaling activities."; RL PLoS Pathog. 8:E1002931-E1002931(2012). RN [39] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22814378; DOI=10.1073/pnas.1210303109; RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.; RT "N-terminal acetylome analyses and functional insights of the N-terminal RT acetyltransferase NatB."; RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012). RN [40] RP FUNCTION. RX PubMed=22520941; DOI=10.1016/j.virol.2012.03.011; RA Dafa-Berger A., Kuzmina A., Fassler M., Yitzhak-Asraf H., Shemer-Avni Y., RA Taube R.; RT "Modulation of hepatitis C virus release by the interferon-induced protein RT BST-2/tetherin."; RL Virology 428:98-111(2012). RN [41] RP FUNCTION, SUBCELLULAR LOCATION, SUBCELLULAR LOCATION (MICROBIAL INFECTION), RP INTERACTION WITH LILRA4, AND GPI-ANCHOR. RX PubMed=26172439; DOI=10.1371/journal.ppat.1005024; RA Bego M.G., Cote E., Aschman N., Mercier J., Weissenhorn W., Cohen E.A.; RT "Vpu exploits the cross-talk between BST2 and the ILT7 receptor to suppress RT anti-HIV-1 responses by plasmacytoid dendritic Cells."; RL PLoS Pathog. 11:E1005024-E1005024(2015). RN [42] RP FUNCTION, INDUCTION (MICROBIAL INFECTION), INTERACTION WITH SARS-COV ORF7A RP PROTEIN (MICROBIAL INFECTION), AND SUBUNIT. RX PubMed=26378163; DOI=10.1128/jvi.02274-15; RA Taylor J.K., Coleman C.M., Postel S., Sisk J.M., Bernbaum J.G., RA Venkataraman T., Sundberg E.J., Frieman M.B.; RT "Severe Acute Respiratory Syndrome Coronavirus ORF7a Inhibits Bone Marrow RT Stromal Antigen 2 Virion Tethering through a Novel Mechanism of RT Glycosylation Interference."; RL J. Virol. 89:11820-11833(2015). RN [43] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [44] RP FUNCTION, INDUCTION (MICROBIAL INFECTION), SUBUNIT, AND MUTAGENESIS OF RP CYS-53; CYS-63 AND CYS-91. RX PubMed=31199522; DOI=10.1002/jmv.25518; RA Wang S.M., Huang K.J., Wang C.T.; RT "Severe acute respiratory syndrome coronavirus spike protein counteracts RT BST2-mediated restriction of virus-like particle release."; RL J. Med. Virol. 91:1743-1750(2019). RN [45] RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 87-147, FUNCTION, DOMAIN, RP DISULFIDE BONDS, SUBUNIT, SUBCELLULAR LOCATION, AND CIRCULAR DICHROISM. RX PubMed=20399176; DOI=10.1016/j.chom.2010.03.005; RA Hinz A., Miguet N., Natrajan G., Usami Y., Yamanaka H., Renesto P., RA Hartlieb B., McCarthy A.A., Simorre J.P., Gottlinger H., Weissenhorn W.; RT "Structural basis of HIV-1 tethering to membranes by the BST-2/tetherin RT ectodomain."; RL Cell Host Microbe 7:314-323(2010). RN [46] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 47-152, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=20880831; DOI=10.1073/pnas.1008206107; RA Schubert H.L., Zhai Q., Sandrin V., Eckert D.M., Garcia-Maya M., Saul L., RA Sundquist W.I., Steiner R.A., Hill C.P.; RT "Structural and functional studies on the extracellular domain of RT BST2/tetherin in reduced and oxidized conformations."; RL Proc. Natl. Acad. Sci. U.S.A. 107:17951-17956(2010). RN [47] RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 47-161, SUBUNIT, FUNCTION, AND RP DISULFIDE BONDS. RX PubMed=20940320; DOI=10.1073/pnas.1011485107; RA Yang H., Wang J., Jia X., McNatt M.W., Zang T., Pan B., Meng W., Wang H.W., RA Bieniasz P.D., Xiong Y.; RT "Structural insight into the mechanisms of enveloped virus tethering by RT tetherin."; RL Proc. Natl. Acad. Sci. U.S.A. 107:18428-18432(2010). CC -!- FUNCTION: IFN-induced antiviral host restriction factor which CC efficiently blocks the release of diverse mammalian enveloped viruses CC by directly tethering nascent virions to the membranes of infected CC cells. Acts as a direct physical tether, holding virions to the cell CC membrane and linking virions to each other. The tethered virions can be CC internalized by endocytosis and subsequently degraded or they can CC remain on the cell surface. In either case, their spread as cell-free CC virions is restricted (PubMed:20019814, PubMed:22520941, CC PubMed:21529378, PubMed:20940320, PubMed:20419159, PubMed:20399176, CC PubMed:19879838, PubMed:19036818, PubMed:18342597, PubMed:18200009). CC Its target viruses belong to diverse families, including retroviridae: CC human immunodeficiency virus type 1 (HIV-1), human immunodeficiency CC virus type 2 (HIV-2), simian immunodeficiency viruses (SIVs), equine CC infectious anemia virus (EIAV), feline immunodeficiency virus (FIV), CC prototype foamy virus (PFV), Mason-Pfizer monkey virus (MPMV), human T- CC cell leukemia virus type 1 (HTLV-1), Rous sarcoma virus (RSV) and CC murine leukemia virus (MLV), flavivirideae: hepatitis C virus (HCV), CC filoviridae: ebola virus (EBOV) and marburg virus (MARV), arenaviridae: CC lassa virus (LASV) and machupo virus (MACV), herpesviridae: kaposis CC sarcoma-associated herpesvirus (KSHV), rhabdoviridae: vesicular CC stomatitis virus (VSV), orthomyxoviridae: influenza A virus, CC paramyxoviridae: nipah virus, and coronaviridae: SARS-CoV CC (PubMed:22520941, PubMed:21621240, PubMed:21529378, PubMed:20943977, CC PubMed:20686043, PubMed:20419159, PubMed:20399176, PubMed:19879838, CC PubMed:19179289, PubMed:18342597, PubMed:18200009, PubMed:26378163, CC PubMed:31199522). Can inhibit cell surface proteolytic activity of CC MMP14 causing decreased activation of MMP15 which results in inhibition CC of cell growth and migration (PubMed:22065321). Can stimulate signaling CC by LILRA4/ILT7 and consequently provide negative feedback to the CC production of IFN by plasmacytoid dendritic cells in response to viral CC infection (PubMed:19564354, PubMed:26172439). Plays a role in the CC organization of the subapical actin cytoskeleton in polarized CC epithelial cells. Isoform 1 and isoform 2 are both effective viral CC restriction factors but have differing antiviral and signaling CC activities (PubMed:23028328, PubMed:26172439). Isoform 2 is resistant CC to HIV-1 Vpu-mediated degradation and restricts HIV-1 viral budding in CC the presence of Vpu (PubMed:23028328, PubMed:26172439). Isoform 1 acts CC as an activator of NF-kappa-B and this activity is inhibited by isoform CC 2 (PubMed:23028328). {ECO:0000269|PubMed:18200009, CC ECO:0000269|PubMed:18342597, ECO:0000269|PubMed:19036818, CC ECO:0000269|PubMed:19179289, ECO:0000269|PubMed:19564354, CC ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20019814, CC ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20419159, CC ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20940320, CC ECO:0000269|PubMed:20943977, ECO:0000269|PubMed:21529378, CC ECO:0000269|PubMed:21621240, ECO:0000269|PubMed:22065321, CC ECO:0000269|PubMed:22520941, ECO:0000269|PubMed:23028328, CC ECO:0000269|PubMed:26172439, ECO:0000269|PubMed:26378163, CC ECO:0000269|PubMed:31199522}. CC -!- SUBUNIT: Parallel homodimer; disulfide-linked. May form homotetramers CC under reducing conditions. Isoform 1 and isoform 2 form homodimers and CC also heterodimers with each other. Dimerization is essential for its CC antiviral activity (PubMed:26378163, PubMed:10329429, PubMed:19737401, CC PubMed:19879838, PubMed:23028328, PubMed:20399176, PubMed:20880831, CC PubMed:20940320, PubMed:31199522). Interacts (via cytoplasmic domain) CC with ARHGAP44 (By similarity). Interacts with MMP14 (via C-terminal CC cytoplasmic tail) (PubMed:22065321). Interacts with LILRA4/ILT7 CC (PubMed:19564354). Interacts with RNF115 (PubMed:20019814). CC {ECO:0000250|UniProtKB:Q811A2, ECO:0000269|PubMed:10329429, CC ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:19737401, CC ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20019814, CC ECO:0000269|PubMed:20399176, ECO:0000269|PubMed:20880831, CC ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:22065321, CC ECO:0000269|PubMed:23028328, ECO:0000269|PubMed:26378163, CC ECO:0000269|PubMed:31199522}. CC -!- SUBUNIT: (Microbial infection) Interacts with ebola GP protein. CC {ECO:0000269|PubMed:19179289}. CC -!- SUBUNIT: (Microbial infection) Interacts (via transmembrane domain) CC with HIV-1 VPU (via transmembrane domain). CC {ECO:0000269|PubMed:19837671}. CC -!- SUBUNIT: (Microbial infection) Interacts with HIV-2 ENV. CC {ECO:0000269|PubMed:19740980}. CC -!- SUBUNIT: (Microbial infection) Interacts with SARS-CoV ORF7a protein. CC {ECO:0000269|PubMed:26378163}. CC -!- INTERACTION: CC Q10589; Q10589: BST2; NbExp=10; IntAct=EBI-2476339, EBI-2476339; CC Q10589; P60033: CD81; NbExp=3; IntAct=EBI-2476339, EBI-712921; CC Q10589; P59901: LILRA4; NbExp=2; IntAct=EBI-2476339, EBI-2841591; CC Q10589; P35585: Ap1m1; Xeno; NbExp=2; IntAct=EBI-2476339, EBI-1040251; CC Q10589; A9QPL9: GP; Xeno; NbExp=2; IntAct=EBI-2476339, EBI-15754841; CC Q10589; P69699: vpu; Xeno; NbExp=7; IntAct=EBI-2476339, EBI-10757638; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell CC membrane {ECO:0000269|PubMed:26172439}; Single-pass type II membrane CC protein. Cell membrane {ECO:0000269|PubMed:19879838, CC ECO:0000269|PubMed:26172439}; Lipid-anchor, GPI-anchor CC {ECO:0000269|PubMed:19879838, ECO:0000305|PubMed:26172439}. Membrane CC raft. Cytoplasm. Apical cell membrane {ECO:0000250}. Note=Shuttles CC between the cell membrane, where it is present predominantly in CC membrane/lipid rafts, and the trans-Golgi network. Forms a complex with CC MMP14 and localizes to the cytoplasm. CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network CC {ECO:0000269|PubMed:26172439}. Late endosome CC {ECO:0000269|PubMed:20419159}. Note=(Microbial infection) HIV-1 VPU and CC HIV-2 ENV can target it to the trans-Golgi network thus sequestering it CC away from virus assembly sites on the cell membrane. Targeted to late CC endosomes upon KSHV infection and subsequent ubiquitination. CC {ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:26172439}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative initiation; Named isoforms=2; CC Name=1; Synonyms=l-Tetherin; CC IsoId=Q10589-1; Sequence=Displayed; CC Name=2; Synonyms=s-Tetherin; CC IsoId=Q10589-2; Sequence=VSP_053250; CC -!- TISSUE SPECIFICITY: Predominantly expressed in liver, lung, heart and CC placenta. Lower levels in pancreas, kidney, skeletal muscle and brain. CC Overexpressed in multiple myeloma cells. Highly expressed during B-cell CC development, from pro-B precursors to plasma cells. Highly expressed on CC T-cells, monocytes, NK cells and dendritic cells (at protein level). CC {ECO:0000269|PubMed:10329429, ECO:0000269|PubMed:16157322}. CC -!- INDUCTION: By type I interferons. {ECO:0000269|PubMed:16157322, CC ECO:0000269|PubMed:23028328}. CC -!- INDUCTION: (Microbial infection) Down-regulated by HIV-1 VPU protein. CC Antagonizes its function by targeting it to the trans-Golgi network, CC sequestering it away from virus assembly sites on the cell membrane. CC VPU also acts as an adapter molecule linking it to BTRC, a substrate CC recognition subunit of the Skp1/Cullin/F-box protein E3 ubiquitin CC ligase, inducing its ubiquitination and subsequent proteasomal CC degradation. {ECO:0000269|PubMed:18200009, ECO:0000269|PubMed:18342597, CC ECO:0000269|PubMed:19837671}. CC -!- INDUCTION: (Microbial infection) Down-regulated by HIV-2 ENV protein. CC Antagonizes its function by targeting it to the trans-Golgi network, CC sequestering it away from virus assembly sites on the cell membrane. CC {ECO:0000269|PubMed:19740980}. CC -!- INDUCTION: (Microbial infection) Down-regulated by KSHV K5 protein. K5 CC ubiquitinates it leading to its targeting to late endosomes and CC degradation. {ECO:0000269|PubMed:20419159}. CC -!- INDUCTION: (Microbial infection) Down-regulated by ebola virus GP CC protein. {ECO:0000269|PubMed:19179289}. CC -!- INDUCTION: (Microbial infection) Made inactive by SARS-CoV ORF7a CC protein through impairing proper glycosylation (PubMed:26378163). May CC be down-regulated by SARS-CoV Spike protein through lysosomal CC degradation pathway (PubMed:31199522). {ECO:0000269|PubMed:26378163, CC ECO:0000269|PubMed:31199522}. CC -!- DOMAIN: The extracellular coiled coil domain forms an extended 170 A CC long semi-flexible rod-like structure important for virion retention at CC the cell surface and prevention of virus spreading. CC {ECO:0000269|PubMed:20399176}. CC -!- PTM: Monoubiquitinated by KSHV E3 ubiquitin-protein ligase K5, leading CC to its targeting to late endosomes and degradation. CC {ECO:0000269|PubMed:20419159}. CC -!- PTM: The GPI anchor is essential for its antiviral activity. CC -!- MISCELLANEOUS: Tetherin shows evidence of positive (adaptive) CC selection, presumably as a result of evolutionary pressure applied by CC antagonistic viral proteins that counteract its inhibitiory activity CC and this has led to the species-specific tetherin sensitivity to viral CC countermeasures. For example, Tantalus monkey tetherin cannot be CC abrogated by HIV-1 VPU due to variation in the tetherin transmembrane CC region. Similarly, SIV Nefs are able to overcome simian tetherins, but CC not human tetherin, due to a unique 5-amino-acid deletion in the CC cytoplasmic tail domain of human tetherin (PubMed:19917491). CC {ECO:0000305|PubMed:19917491}. CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative initiation at Met- CC 13 of isoform 1. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tetherin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; D28137; BAA05679.1; -; mRNA. DR EMBL; AK223124; BAD96844.1; -; mRNA. DR EMBL; AK291099; BAF83788.1; -; mRNA. DR EMBL; AC010319; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84602.1; -; Genomic_DNA. DR EMBL; BC033873; AAH33873.1; -; mRNA. DR CCDS; CCDS12358.1; -. [Q10589-1] DR PIR; A56836; A56836. DR RefSeq; NP_004326.1; NM_004335.3. [Q10589-1] DR PDB; 2LK9; NMR; -; A=18-47. DR PDB; 2X7A; X-ray; 2.77 A; A/B/C/D/E/F/G/H/I/J/K=87-147. DR PDB; 2XG7; X-ray; 3.45 A; A/C=51-151. DR PDB; 3MQ7; X-ray; 2.28 A; A/B/C/D/E/F/G/H/I/J/K/L=47-161. DR PDB; 3MQ9; X-ray; 2.80 A; A/B/C/D/E/F/G/H=66-139. DR PDB; 3MQB; X-ray; 3.20 A; A/B/E/F=47-161. DR PDB; 3MQC; X-ray; 2.80 A; A/B/C/D=47-161. DR PDB; 3NWH; X-ray; 2.60 A; A/B/C/D=47-152. DR PDB; 4P6Z; X-ray; 3.00 A; T=1-21. DR PDB; 6CM9; EM; 3.73 A; L/N/T=2-21. DR PDB; 6CRI; EM; 6.80 A; N/T/Y/Z/c/d=2-21. DR PDB; 6D83; EM; 4.27 A; L/T=2-21. DR PDB; 6D84; EM; 6.72 A; L/O/R/T=2-21. DR PDB; 6DFF; EM; 3.90 A; L/T=2-21. DR PDB; 7Q9A; X-ray; 2.10 A; C=22-31. DR PDBsum; 2LK9; -. DR PDBsum; 2X7A; -. DR PDBsum; 2XG7; -. DR PDBsum; 3MQ7; -. DR PDBsum; 3MQ9; -. DR PDBsum; 3MQB; -. DR PDBsum; 3MQC; -. DR PDBsum; 3NWH; -. DR PDBsum; 4P6Z; -. DR PDBsum; 6CM9; -. DR PDBsum; 6CRI; -. DR PDBsum; 6D83; -. DR PDBsum; 6D84; -. DR PDBsum; 6DFF; -. DR PDBsum; 7Q9A; -. DR AlphaFoldDB; Q10589; -. DR BMRB; Q10589; -. DR SMR; Q10589; -. DR BioGRID; 107149; 52. DR DIP; DIP-53216N; -. DR IntAct; Q10589; 29. DR MINT; Q10589; -. DR STRING; 9606.ENSP00000252593; -. DR TCDB; 1.D.118.1.1; the pore-forming b18 peptide derived from the b49mod1 protein (b49-b18) family. DR GlyConnect; 1044; 11 N-Linked glycans (2 sites). DR GlyCosmos; Q10589; 2 sites, 9 glycans. DR GlyGen; Q10589; 6 sites, 9 N-linked glycans (2 sites), 2 O-linked glycans (4 sites). DR iPTMnet; Q10589; -. DR PhosphoSitePlus; Q10589; -. DR SwissPalm; Q10589; -. DR BioMuta; BST2; -. DR DMDM; 1705508; -. DR EPD; Q10589; -. DR jPOST; Q10589; -. DR MassIVE; Q10589; -. DR MaxQB; Q10589; -. DR PaxDb; 9606-ENSP00000252593; -. DR PeptideAtlas; Q10589; -. DR ProteomicsDB; 58866; -. [Q10589-1] DR Pumba; Q10589; -. DR ABCD; Q10589; 23 sequenced antibodies. DR Antibodypedia; 1532; 895 antibodies from 45 providers. DR DNASU; 684; -. DR Ensembl; ENST00000252593.7; ENSP00000252593.6; ENSG00000130303.14. [Q10589-1] DR GeneID; 684; -. DR KEGG; hsa:684; -. DR MANE-Select; ENST00000252593.7; ENSP00000252593.6; NM_004335.4; NP_004326.1. DR UCSC; uc060vid.1; human. [Q10589-1] DR AGR; HGNC:1119; -. DR CTD; 684; -. DR DisGeNET; 684; -. DR GeneCards; BST2; -. DR HGNC; HGNC:1119; BST2. DR HPA; ENSG00000130303; Tissue enhanced (ovary). DR MIM; 600534; gene. DR neXtProt; NX_Q10589; -. DR OpenTargets; ENSG00000130303; -. DR PharmGKB; PA25436; -. DR VEuPathDB; HostDB:ENSG00000130303; -. DR eggNOG; ENOG502TB0V; Eukaryota. DR GeneTree; ENSGT00390000013782; -. DR HOGENOM; CLU_104678_0_0_1; -. DR InParanoid; Q10589; -. DR OMA; IIFTIKA; -. DR OrthoDB; 4851957at2759; -. DR PhylomeDB; Q10589; -. DR TreeFam; TF338345; -. DR PathwayCommons; Q10589; -. DR Reactome; R-HSA-6798695; Neutrophil degranulation. DR Reactome; R-HSA-909733; Interferon alpha/beta signaling. DR Reactome; R-HSA-9692916; SARS-CoV-1 activates/modulates innate immune responses. DR SignaLink; Q10589; -. DR BioGRID-ORCS; 684; 17 hits in 1175 CRISPR screens. DR ChiTaRS; BST2; human. DR EvolutionaryTrace; Q10589; -. DR GeneWiki; Tetherin; -. DR GenomeRNAi; 684; -. DR Pharos; Q10589; Tbio. DR PRO; PR:Q10589; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q10589; Protein. DR Bgee; ENSG00000130303; Expressed in right adrenal gland and 187 other cell types or tissues. DR ExpressionAtlas; Q10589; baseline and differential. DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB. DR GO; GO:0035577; C:azurophil granule membrane; TAS:Reactome. DR GO; GO:0009986; C:cell surface; IMP:CACAO. DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell. DR GO; GO:0005771; C:multivesicular body; IMP:CACAO. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB. DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB. DR GO; GO:0042113; P:B cell activation; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IDA:UniProtKB. DR GO; GO:0045087; P:innate immune response; IDA:UniProtKB. DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB. DR GO; GO:0030336; P:negative regulation of cell migration; IDA:UniProtKB. DR GO; GO:1901253; P:negative regulation of intracellular transport of viral material; IDA:UniProtKB. DR GO; GO:0002737; P:negative regulation of plasmacytoid dendritic cell cytokine production; IDA:UniProtKB. DR GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB. DR GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; HMP:UniProtKB. DR GO; GO:0070665; P:positive regulation of leukocyte proliferation; TAS:GO_Central. DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB. DR GO; GO:0035455; P:response to interferon-alpha; ISS:UniProtKB. DR GO; GO:0035456; P:response to interferon-beta; ISS:UniProtKB. DR GO; GO:0034341; P:response to type II interferon; ISS:UniProtKB. DR GO; GO:0009615; P:response to virus; IDA:UniProtKB. DR DisProt; DP02885; -. DR Gene3D; 1.20.5.1700; -; 1. DR InterPro; IPR024886; BST2. DR PANTHER; PTHR15190; BONE MARROW STROMAL ANTIGEN 2; 1. DR PANTHER; PTHR15190:SF1; BONE MARROW STROMAL ANTIGEN 2; 1. DR Pfam; PF16716; BST2; 1. DR Genevisible; Q10589; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative initiation; Antiviral defense; B-cell activation; KW Cell membrane; Coiled coil; Cytoplasm; Disulfide bond; Endosome; KW Glycoprotein; Golgi apparatus; GPI-anchor; Host-virus interaction; KW Immunity; Innate immunity; Isopeptide bond; Lipoprotein; Membrane; KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix; KW Ubl conjugation. FT CHAIN 1..161 FT /note="Bone marrow stromal antigen 2" FT /id="PRO_0000065005" FT PROPEP 162..180 FT /note="Removed in mature form" FT /evidence="ECO:0000255" FT /id="PRO_0000253552" FT TOPO_DOM 1..20 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 21..48 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 49..161 FT /note="Extracellular" FT /evidence="ECO:0000255" FT COILED 68..152 FT LIPID 161 FT /note="GPI-anchor amidated serine" FT /evidence="ECO:0000255" FT CARBOHYD 65 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973, ECO:0000269|PubMed:19737401, FT ECO:0000269|PubMed:19879838" FT CARBOHYD 92 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:19737401, FT ECO:0000269|PubMed:19879838" FT DISULFID 53 FT /note="Interchain" FT DISULFID 63 FT /note="Interchain" FT DISULFID 91 FT /note="Interchain" FT CROSSLNK 18 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:20419159" FT VAR_SEQ 1..12 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000305" FT /id="VSP_053250" FT VARIANT 143 FT /note="V -> F (in dbSNP:rs1804402)" FT /id="VAR_012067" FT MUTAGEN 3..5 FT /note="STS->AAA: Partial resistance to Vpu." FT /evidence="ECO:0000269|PubMed:23028328" FT MUTAGEN 6 FT /note="Y->A: Partial resistance to Vpu and significantly FT reduced activation of NF-kB; when associated with A-8." FT /evidence="ECO:0000269|PubMed:23028328" FT MUTAGEN 8 FT /note="Y->A: Partial resistance to Vpu and significantly FT reduced activation of NF-kB; when associated with A-6." FT /evidence="ECO:0000269|PubMed:23028328" FT MUTAGEN 18 FT /note="K->R: Abolishes redistribution to late endosomes in FT cells expressing KSH virus E3 ubiquitin-protein ligase K5." FT /evidence="ECO:0000269|PubMed:20419159" FT MUTAGEN 21 FT /note="K->R: No effect on redistribution to late endosomes FT in cells expressing KSH virus E3 ubiquitin-protein ligase FT K5." FT /evidence="ECO:0000269|PubMed:20419159" FT MUTAGEN 53 FT /note="C->A: Prevents homodimerization and inhibition of FT SARS-CoV, HCoV-229E, and HIV-1 viral particles production FT ex vivo; when associated with A-63 and A-91." FT /evidence="ECO:0000269|PubMed:31199522" FT MUTAGEN 63 FT /note="C->A: Prevents homodimerization and inhibition of FT SARS-CoV, HCoV-229E, and HIV-1 viral particles production FT ex vivo; when associated with A-53 and A-91." FT /evidence="ECO:0000269|PubMed:31199522" FT MUTAGEN 65 FT /note="N->A: Loss of glycosylation site." FT /evidence="ECO:0000269|PubMed:19879838" FT MUTAGEN 91 FT /note="C->A: Prevents homodimerization and inhibition of FT SARS-CoV, HCoV-229E, and HIV-1 viral particles production FT ex vivo; when associated with A-53 and A-63." FT /evidence="ECO:0000269|PubMed:31199522" FT MUTAGEN 92 FT /note="N->A: Loss of glycosylation site. Impairs anti-viral FT activity." FT /evidence="ECO:0000269|PubMed:19879838" FT CONFLICT 141 FT /note="N -> D (in Ref. 4; BAD96844)" FT /evidence="ECO:0000305" FT STRAND 25..28 FT /evidence="ECO:0007829|PDB:7Q9A" FT HELIX 52..148 FT /evidence="ECO:0007829|PDB:3MQ7" FT STRAND 152..154 FT /evidence="ECO:0007829|PDB:3MQB" SQ SEQUENCE 180 AA; 19769 MW; CAF52340D69061EE CRC64; MASTSYDYCR VPMEDGDKRC KLLLGIGILV LLIIVILGVP LIIFTIKANS EACRDGLRAV MECRNVTHLL QQELTEAQKG FQDVEAQAAT CNHTVMALMA SLDAEKAQGQ KKVEELEGEI TTLNHKLQDA SAEVERLRRE NQVLSVRIAD KKYYPSSQDS SSAAAPQLLI VLLGLSALLQ //