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   17-JUN-2020, entry version 171.
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.
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 IN HIV-1 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, AND INDUCTION BY HIV-1 VPU.
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, SUBCELLULAR LOCATION, AND INDUCTION BY HIV-2
RP   ENV.
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, AND INDUCTION BY EBOLA GP
RP   PROTEIN.
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, MUTAGENESIS OF
RP   LYS-18 AND LYS-21, AND UBIQUITINATION AT LYS-18 BY KSH VIRUS E3
RP   UBIQUITIN-PROTEIN LIGASE K5.
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, 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   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   [42]
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   [43]
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   [44]
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. Its target viruses belong to diverse families,
CC       including retroviridae: human immunodeficiency virus type 1 (HIV-1),
CC       human immunodeficiency virus type 2 (HIV-2), simian immunodeficiency
CC       viruses (SIVs), equine infectious anemia virus (EIAV), feline
CC       immunodeficiency virus (FIV), prototype foamy virus (PFV), Mason-Pfizer
CC       monkey virus (MPMV), human T-cell leukemia virus type 1 (HTLV-1), Rous
CC       sarcoma virus (RSV) and murine leukemia virus (MLV), flavivirideae:
CC       hepatitis C virus (HCV), filoviridae: ebola virus (EBOV) and marburg
CC       virus (MARV), arenaviridae: lassa virus (LASV) and machupo virus
CC       (MACV), herpesviridae: kaposis sarcoma-associated herpesvirus (KSHV),
CC       rhabdoviridae: vesicular stomatitis virus (VSV), orthomyxoviridae:
CC       influenza A virus, and paramyxoviridae: nipah virus. Can inhibit cell
CC       surface proteolytic activity of MMP14 causing decreased activation of
CC       MMP15 which results in inhibition of cell growth and migration. Can
CC       stimulate signaling by LILRA4/ILT7 and consequently provide negative
CC       feedback to the production of IFN by plasmacytoid dendritic cells in
CC       response to viral infection (PubMed:19564354, PubMed:26172439). Plays a
CC       role in the organization of the subapical actin cytoskeleton in
CC       polarized epithelial cells. Isoform 1 and isoform 2 are both effective
CC       viral 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   -!- 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. Interacts (via cytoplasmic domain) with ARHGAP44
CC       (By similarity). Interacts with MMP14 (via C-terminal cytoplasmic tail)
CC       (PubMed:22065321). Interacts with LILRA4/ILT7 (PubMed:19564354,
CC       PubMed:26172439). Interacts (via transmembrane domain) with HIV-1 VPU
CC       (via transmembrane domain) (PubMed:19837671). Interacts with HIV-2 ENV
CC       and ebola GP protein (PubMed:19740980, PubMed:19179289). {ECO:0000250,
CC       ECO:0000269|PubMed:10329429, ECO:0000269|PubMed:19179289,
CC       ECO:0000269|PubMed:19564354, ECO:0000269|PubMed:19737401,
CC       ECO:0000269|PubMed:19740980, ECO:0000269|PubMed:19837671,
CC       ECO:0000269|PubMed:19879838, ECO:0000269|PubMed:20399176,
CC       ECO:0000269|PubMed:20880831, ECO:0000269|PubMed:20940320,
CC       ECO:0000269|PubMed:22065321, ECO:0000269|PubMed:23028328}.
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}. Late
CC       endosome {ECO:0000269|PubMed:20419159}. Membrane raft. Cytoplasm.
CC       Apical cell membrane {ECO:0000250}. Note=Shuttles between the cell
CC       membrane, where it is present predominantly in membrane/lipid rafts,
CC       and the trans-Golgi network. HIV-1 VPU and HIV-2 ENV can target it to
CC       the trans-Golgi network thus sequestering it away from virus assembly
CC       sites on the cell membrane. Targeted to late endosomes upon KSHV
CC       infection and subsequent ubiquitination. Forms a complex with MMP14 and
CC       localizes to the cytoplasm.
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. Down-regulated by viral antagonistic
CC       factors which include: HIV-1 VPU protein, HIV-2 ENV protein, KSHV K5
CC       protein and ebola virus GP protein. VPU and ENV antagonize its function
CC       by targeting it to the trans-Golgi network, sequestering it away from
CC       virus assembly sites on the cell membrane. VPU also acts as an adapter
CC       molecule linking it to BTRC, a substrate recognition subunit of the
CC       Skp1/Cullin/F-box protein E3 ubiquitin ligase, inducing its
CC       ubiquitination and subsequent proteasomal degradation. K5 ubiquitinates
CC       it leading to its targeting to late endosomes and degradation.
CC       {ECO:0000269|PubMed:16157322, ECO:0000269|PubMed:19179289,
CC       ECO:0000269|PubMed:19740980, ECO:0000269|PubMed:19837671,
CC       ECO:0000269|PubMed:23028328}.
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   GlyConnect; 1044; -.
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; 671 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; ENOG410JE1U; Eukaryota.
DR   eggNOG; ENOG41115GP; LUCA.
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   Reactome; R-HSA-6798695; Neutrophil degranulation.
DR   Reactome; R-HSA-909733; Interferon alpha/beta signaling.
DR   BioGRID-ORCS; 684; 3 hits in 787 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 208 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         65
FT                   /note="N->A: Loss of glycosylation site."
FT                   /evidence="ECO:0000269|PubMed:19879838"
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
//