BST2_MOUSE
ID BST2_MOUSE Reviewed; 172 AA.
AC Q8R2Q8; Q8CEY7;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Bone marrow stromal antigen 2;
DE Short=BST-2;
DE AltName: Full=HM1.24 antigen;
DE AltName: CD_antigen=CD317;
DE Flags: Precursor;
GN Name=Bst2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Liver, and Mammary tumor;
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 [3]
RP IDENTIFICATION.
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 [4]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY INTERFERONS, AND
RP FUNCTION.
RX PubMed=16920966; DOI=10.4049/jimmunol.177.5.3260;
RA Blasius A.L., Giurisato E., Cella M., Schreiber R.D., Shaw A.S.,
RA Colonna M.;
RT "Bone marrow stromal cell antigen 2 is a specific marker of type I IFN-
RT producing cells in the naive mouse, but a promiscuous cell surface antigen
RT following IFN stimulation.";
RL J. Immunol. 177:3260-3265(2006).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-94.
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 [6]
RP FUNCTION, AND INDUCTION BY EBOLA GP 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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Heart, Liver, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION.
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 [9]
RP FUNCTION.
RX PubMed=20702620; DOI=10.1128/jvi.01067-10;
RA Goffinet C., Schmidt S., Kern C., Oberbremer L., Keppler O.T.;
RT "Endogenous CD317/Tetherin limits replication of HIV-1 and murine leukemia
RT virus in rodent cells and is resistant to antagonists from primate
RT viruses.";
RL J. Virol. 84:11374-11384(2010).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21919738; DOI=10.1089/dna.2011.1384;
RA Sarojini S., Theofanis T., Reiss C.S.;
RT "Interferon-induced tetherin restricts vesicular stomatitis virus release
RT in neurons.";
RL DNA Cell Biol. 30:965-974(2011).
RN [11]
RP FUNCTION.
RX PubMed=22025715; DOI=10.1073/pnas.1113694108;
RA Liberatore R.A., Bieniasz P.D.;
RT "Tetherin is a key effector of the antiretroviral activity of type I
RT interferon in vitro and in vivo.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:18097-18101(2011).
RN [12]
RP FUNCTION.
RX PubMed=22327075; DOI=10.4049/jimmunol.1103145;
RA Swiecki M., Wang Y., Gilfillan S., Lenschow D.J., Colonna M.;
RT "Paradoxical roles of BST2/tetherin in promoting type I IFN response and
RT viral infection.";
RL J. Immunol. 188:2488-2492(2012).
RN [13]
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 [14]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=22284121; DOI=10.1186/1742-4690-9-10;
RA Jones P.H., Mehta H.V., Maric M., Roller R.J., Okeoma C.M.;
RT "Bone marrow stromal cell antigen 2 (BST-2) restricts mouse mammary tumor
RT virus (MMTV) replication in vivo.";
RL Retrovirology 9:10-10(2012).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 53-151, COILED-COIL DOMAIN,
RP SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=21084286; DOI=10.1074/jbc.m110.190538;
RA Swiecki M., Scheaffer S.M., Allaire M., Fremont D.H., Colonna M.,
RA Brett T.J.;
RT "Structural and biophysical analysis of BST-2/tetherin ectodomains reveals
RT an evolutionary conserved design to inhibit virus release.";
RL J. Biol. Chem. 286:2987-2997(2011).
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 mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV),
CC filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and
CC rhabdoviridae: vesicular stomatitis virus (VSV). 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. Plays a role in the organization of the
CC subapical actin cytoskeleton in polarized epithelial cells.
CC {ECO:0000269|PubMed:16920966, ECO:0000269|PubMed:19179289,
CC ECO:0000269|PubMed:20686043, ECO:0000269|PubMed:20702620,
CC ECO:0000269|PubMed:21919738, ECO:0000269|PubMed:22025715,
CC ECO:0000269|PubMed:22284121, ECO:0000269|PubMed:22327075}.
CC -!- SUBUNIT: Parallel homodimer; disulfide-linked. May form homotetramers
CC under reducing conditions. Dimerization is essential for its antiviral
CC activity. Interacts (via cytoplasmic domain) with ARHGAP44 (By
CC similarity). Interacts with MMP14 (via C-terminal cytoplasmic tail) (By
CC similarity). Interacts with LILRA4/ILT7 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell
CC membrane; Single-pass type II membrane protein. Cell membrane
CC {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. Late endosome
CC {ECO:0000250}. Membrane raft {ECO:0000250}. Cytoplasm {ECO:0000250}.
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. Forms a complex with MMP14 and localizes
CC to the cytoplasm (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: In naive mice, specifically expressed on type I
CC interferon-producing cells (at protein level).
CC {ECO:0000269|PubMed:16920966}.
CC -!- INDUCTION: By viral or other interferon-inducing stimulation in most
CC cell types (at protein level). Down-regulated by ebola virus GP
CC protein. {ECO:0000269|PubMed:16920966, ECO:0000269|PubMed:19179289}.
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. {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK009361; BAC25254.1; -; mRNA.
DR EMBL; AK154399; BAE32560.1; -; mRNA.
DR EMBL; BC027328; AAH27328.1; -; mRNA.
DR EMBL; BC056638; AAH56638.1; -; mRNA.
DR EMBL; BC087949; AAH87949.1; -; mRNA.
DR CCDS; CCDS22397.1; -.
DR RefSeq; NP_932763.1; NM_198095.2.
DR PDB; 3NI0; X-ray; 1.60 A; A/B=53-151.
DR PDBsum; 3NI0; -.
DR AlphaFoldDB; Q8R2Q8; -.
DR SMR; Q8R2Q8; -.
DR BioGRID; 213524; 2.
DR IntAct; Q8R2Q8; 1.
DR STRING; 10090.ENSMUSP00000051921; -.
DR GlyGen; Q8R2Q8; 3 sites.
DR iPTMnet; Q8R2Q8; -.
DR PhosphoSitePlus; Q8R2Q8; -.
DR SwissPalm; Q8R2Q8; -.
DR EPD; Q8R2Q8; -.
DR jPOST; Q8R2Q8; -.
DR MaxQB; Q8R2Q8; -.
DR PaxDb; Q8R2Q8; -.
DR PeptideAtlas; Q8R2Q8; -.
DR PRIDE; Q8R2Q8; -.
DR ProteomicsDB; 273708; -.
DR Antibodypedia; 1532; 730 antibodies from 45 providers.
DR DNASU; 69550; -.
DR Ensembl; ENSMUST00000051672; ENSMUSP00000051921; ENSMUSG00000046718.
DR GeneID; 69550; -.
DR KEGG; mmu:69550; -.
DR UCSC; uc009mdr.1; mouse.
DR CTD; 684; -.
DR MGI; MGI:1916800; Bst2.
DR VEuPathDB; HostDB:ENSMUSG00000046718; -.
DR eggNOG; ENOG502TB0V; Eukaryota.
DR GeneTree; ENSGT00390000013782; -.
DR HOGENOM; CLU_104678_2_0_1; -.
DR InParanoid; Q8R2Q8; -.
DR OMA; FYHYLPV; -.
DR OrthoDB; 1579815at2759; -.
DR PhylomeDB; Q8R2Q8; -.
DR TreeFam; TF338345; -.
DR Reactome; R-MMU-6798695; Neutrophil degranulation.
DR BioGRID-ORCS; 69550; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Bst2; mouse.
DR EvolutionaryTrace; Q8R2Q8; -.
DR PRO; PR:Q8R2Q8; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R2Q8; protein.
DR Bgee; ENSMUSG00000046718; Expressed in left lobe of liver and 165 other tissues.
DR Genevisible; Q8R2Q8; MM.
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:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:MGI.
DR GO; GO:0051607; P:defense response to virus; ISO:MGI.
DR GO; GO:0045087; P:innate immune response; IMP:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR GO; GO:0030336; P:negative regulation of cell migration; ISS: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; ISS:UniProtKB.
DR GO; GO:0045071; P:negative regulation of viral genome replication; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISS:UniProtKB.
DR GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
DR GO; GO:0035456; P:response to interferon-beta; IDA:UniProtKB.
DR GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
DR GO; GO:0009615; P:response to virus; IDA:UniProtKB.
DR InterPro; IPR024886; BST2.
DR PANTHER; PTHR15190; PTHR15190; 1.
DR Pfam; PF16716; BST2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coiled coil; Cytoplasm; Disulfide bond;
KW Endosome; Glycoprotein; Golgi apparatus; GPI-anchor; Immunity;
KW Innate immunity; Lipoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..152
FT /note="Bone marrow stromal antigen 2"
FT /id="PRO_0000253553"
FT PROPEP 153..172
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000253554"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 31..51
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 52..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT COILED 74..147
FT /evidence="ECO:0000269|PubMed:21084286"
FT LIPID 152
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 70
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine; atypical"
FT /evidence="ECO:0000269|PubMed:19349973"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:21084286"
FT DISULFID 68
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:21084286"
FT DISULFID 96
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:21084286"
FT HELIX 59..143
FT /evidence="ECO:0007829|PDB:3NI0"
FT TURN 144..146
FT /evidence="ECO:0007829|PDB:3NI0"
SQ SEQUENCE 172 AA; 19152 MW; A2032FD01FAF601A CRC64;
MAPSFYHYLP VPMDEMGGKQ GWGSHRQWLG AAILVVLFGV TLVILTIYFA VTANSVACRD
GLRAQAECRN TTHLLQRQLT RTQDSLLQAE TQANSCNLTV VTLQESLEKK VSQALEQQAR
IKELENEVTK LNQELENLRI QKETSSTVQV NSGSSMVVSS LLVLKVSLFL LF
