BST2_HUMAN
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 03-AUG-2022, entry version 181.
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}.
CC ---------------------------------------------------------------------------
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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 AlphaFoldDB; Q10589; -.
DR BMRB; Q10589; -.
DR SMR; Q10589; -.
DR BioGRID; 107149; 47.
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 GlyGen; Q10589; 3 sites, 9 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
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; 730 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 CTD; 684; -.
DR DisGeNET; 684; -.
DR GeneCards; BST2; -.
DR HGNC; HGNC:1119; BST2.
DR HPA; ENSG00000130303; Tissue enhanced (adrenal gland, 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; FYHYLPV; -.
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 SignaLink; Q10589; -.
DR BioGRID-ORCS; 684; 16 hits in 1088 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 185 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: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: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: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 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 DisProt; DP02885; -.
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; 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 HELIX 23..44
FT /evidence="ECO:0007829|PDB:2LK9"
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
