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   12-AUG-2020, entry version 172.
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 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   [14]
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   [15]
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   [16]
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   [17]
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   [18]
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   [19]
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   [20]
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   [21]
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   [22]
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   [23]
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   [24]
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   [25]
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   [26]
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   [27]
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   [28]
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   [29]
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   [30]
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   [31]
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   [32]
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   [33]
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   [34]
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   [35]
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   [36]
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   [37]
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   [38]
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   [39]
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   [40]
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   [41]
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   [42]
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   [43]
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   [44]
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   [45]
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   [46]
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:22520941, PubMed:21529378,
CC       PubMed:20940320, PubMed:20419159, PubMed:20399176, PubMed:19879838,
CC       PubMed:19036818, PubMed:18342597, PubMed:18200009). Its target viruses
CC       belong to diverse families, including retroviridae: human
CC       immunodeficiency virus type 1 (HIV-1), human immunodeficiency virus
CC       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:20399176,
CC       ECO:0000269|PubMed:20419159, ECO:0000269|PubMed:20686043,
CC       ECO:0000269|PubMed:20940320, ECO:0000269|PubMed:20943977,
CC       ECO:0000269|PubMed:21529378, ECO:0000269|PubMed:21621240,
CC       ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:22520941,
CC       ECO:0000269|PubMed:23028328, ECO:0000269|PubMed:26172439,
CC       ECO:0000269|PubMed:26378163, 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). {ECO:0000250|UniProtKB:Q811A2,
CC       ECO:0000269|PubMed:10329429, ECO:0000269|PubMed:19564354,
CC       ECO:0000269|PubMed:19737401, ECO:0000269|PubMed:19879838,
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}.
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   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   SMR; Q10589; -.
DR   BioGRID; 107149; 30.
DR   DIP; DIP-53216N; -.
DR   IntAct; Q10589; 27.
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   GlyGen; Q10589; 2 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; Q10589; -.
DR   PeptideAtlas; Q10589; -.
DR   PRIDE; Q10589; -.
DR   ProteomicsDB; 58866; -. [Q10589-1]
DR   ABCD; Q10589; 23 sequenced antibodies.
DR   Antibodypedia; 1532; 672 antibodies.
DR   DNASU; 684; -.
DR   Ensembl; ENST00000252593; ENSP00000252593; ENSG00000130303. [Q10589-1]
DR   GeneID; 684; -.
DR   KEGG; hsa:684; -.
DR   UCSC; uc060vid.1; human. [Q10589-1]
DR   CTD; 684; -.
DR   DisGeNET; 684; -.
DR   EuPathDB; HostDB:ENSG00000130303.12; -.
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   eggNOG; ENOG502TB0V; Eukaryota.
DR   GeneTree; ENSGT00390000013782; -.
DR   HOGENOM; CLU_104678_0_0_1; -.
DR   InParanoid; Q10589; -.
DR   KO; K06731; -.
DR   OMA; KNNASSC; -.
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   BioGRID-ORCS; 684; 6 hits in 876 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 left ovary and 223 other tissues.
DR   ExpressionAtlas; Q10589; baseline and differential.
DR   Genevisible; Q10589; HS.
DR   GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
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:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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: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:0043312; P:neutrophil degranulation; TAS:Reactome.
DR   GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; 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 interferon-gamma; ISS:UniProtKB.
DR   GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR   GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
DR   InterPro; IPR024886; BST2.
DR   PANTHER; PTHR15190; PTHR15190; 1.
DR   Pfam; PF16716; BST2; 1.
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; Immunity; Innate immunity;
KW   Isopeptide bond; Lipoprotein; Membrane; Polymorphism; Reference proteome;
KW   Signal-anchor; Transmembrane; Transmembrane helix; 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   HELIX           23..44
FT                   /evidence="ECO:0000244|PDB:2LK9"
FT   HELIX           52..148
FT                   /evidence="ECO:0000244|PDB:3MQ7"
FT   STRAND          152..154
FT                   /evidence="ECO:0000244|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
//