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Protein

Bone marrow stromal antigen 2

Gene

Bst2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

IFN-induced antiviral host restriction factor which efficiently blocks the release of diverse mammalian enveloped viruses by directly tethering nascent virions to the membranes of infected cells. Acts as a direct physical tether, holding virions to the cell membrane and linking virions to each other. The tethered virions can be internalized by endocytosis and subsequently degraded or they can remain on the cell surface. In either case, their spread as cell-free virions is restricted. Its target viruses belong to diverse families, including retroviridae: human immunodeficiency virus type 1 (HIV-1), mouse mammary tumor virus (MMTV) and murine leukemia virus (MLV), filoviridae: ebola virus (EBOV), arenaviridae: lassa virus (LASV), and rhabdoviridae: vesicular stomatitis virus (VSV). Can inhibit cell surface proteolytic activity of MMP14 causing decreased activation of MMP15 which results in inhibition of cell growth and migration. Can stimulate signaling by LILRA4/ILT7 and consequently provide negative feedback to the production of IFN by plasmacytoid dendritic cells in response to viral infection. Plays a role in the organization of the subapical actin cytoskeleton in polarized epithelial cells.8 Publications

GO - Molecular functioni

GO - Biological processi

  • defense response to virus Source: GO_Central
  • innate immune response Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of cell migration Source: UniProtKB
  • negative regulation of intracellular transport of viral material Source: UniProtKB
  • negative regulation of plasmacytoid dendritic cell cytokine production Source: UniProtKB
  • negative regulation of viral genome replication Source: UniProtKB
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • regulation of actin cytoskeleton organization Source: UniProtKB
  • response to interferon-alpha Source: UniProtKB
  • response to interferon-beta Source: UniProtKB
  • response to interferon-gamma Source: UniProtKB
  • response to virus Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Immunity, Innate immunity

Names & Taxonomyi

Protein namesi
Recommended name:
Bone marrow stromal antigen 2
Short name:
BST-2
Alternative name(s):
HM1.24 antigen
CD_antigen: CD317
Gene namesi
Name:Bst2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:1916800. Bst2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3030CytoplasmicSequence analysisAdd
BLAST
Transmembranei31 – 5121Helical; Signal-anchor for type II membrane proteinSequence analysisAdd
BLAST
Topological domaini52 – 152101ExtracellularSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endosome, Golgi apparatus, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 152152Bone marrow stromal antigen 2PRO_0000253553Add
BLAST
Propeptidei153 – 17220Removed in mature formSequence analysisPRO_0000253554Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi58 – 58Interchain1 Publication
Disulfide bondi68 – 68Interchain1 Publication
Glycosylationi70 – 701N-linked (GlcNAc...)1 Publication
Glycosylationi94 – 941N-linked (GlcNAc...); atypical1 Publication
Disulfide bondi96 – 96Interchain1 Publication
Glycosylationi97 – 971N-linked (GlcNAc...)Sequence analysis
Lipidationi152 – 1521GPI-anchor amidated serineSequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein, GPI-anchor, Lipoprotein

Proteomic databases

EPDiQ8R2Q8.
MaxQBiQ8R2Q8.
PaxDbiQ8R2Q8.
PeptideAtlasiQ8R2Q8.
PRIDEiQ8R2Q8.

PTM databases

iPTMnetiQ8R2Q8.
PhosphoSiteiQ8R2Q8.
SwissPalmiQ8R2Q8.

Expressioni

Tissue specificityi

In naive mice, specifically expressed on type I interferon-producing cells (at protein level).1 Publication

Inductioni

By viral or other interferon-inducing stimulation in most cell types (at protein level). Down-regulated by ebola virus GP protein.2 Publications

Gene expression databases

BgeeiQ8R2Q8.
CleanExiMM_BST2.
GenevisibleiQ8R2Q8. MM.

Interactioni

Subunit structurei

Parallel homodimer; disulfide-linked. May form homotetramers under reducing conditions. Dimerization is essential for its antiviral activity. Interacts (via cytoplasmic domain) with ARHGAP44 (By similarity). Interacts with MMP14 (via C-terminal cytoplasmic tail) (By similarity). Interacts with LILRA4/ILT7 (By similarity).By similarity

Protein-protein interaction databases

IntActiQ8R2Q8. 1 interaction.
STRINGi10090.ENSMUSP00000051921.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi59 – 14385Combined sources
Turni144 – 1463Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NI0X-ray1.60A/B53-151[»]
ProteinModelPortaliQ8R2Q8.
SMRiQ8R2Q8. Positions 57-151.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8R2Q8.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili74 – 147741 PublicationAdd
BLAST

Domaini

The extracellular coiled coil domain forms an extended 170 A long semi-flexible rod-like structure important for virion retention at the cell surface and prevention of virus spreading.By similarity

Keywords - Domaini

Coiled coil, Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410JE1U. Eukaryota.
ENOG41115GP. LUCA.
GeneTreeiENSGT00390000013782.
HOGENOMiHOG000013084.
HOVERGENiHBG004902.
InParanoidiQ8R2Q8.
KOiK06731.
OMAiECRNTTH.
OrthoDBiEOG7D59R5.
PhylomeDBiQ8R2Q8.
TreeFamiTF338345.

Family and domain databases

InterProiIPR024886. BST2.
[Graphical view]
PANTHERiPTHR15190. PTHR15190. 1 hit.
PfamiPF16716. BST2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8R2Q8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPSFYHYLP VPMDEMGGKQ GWGSHRQWLG AAILVVLFGV TLVILTIYFA
60 70 80 90 100
VTANSVACRD GLRAQAECRN TTHLLQRQLT RTQDSLLQAE TQANSCNLTV
110 120 130 140 150
VTLQESLEKK VSQALEQQAR IKELENEVTK LNQELENLRI QKETSSTVQV
160 170
NSGSSMVVSS LLVLKVSLFL LF
Length:172
Mass (Da):19,152
Last modified:June 1, 2002 - v1
Checksum:iA2032FD01FAF601A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009361 mRNA. Translation: BAC25254.1.
AK154399 mRNA. Translation: BAE32560.1.
BC027328 mRNA. Translation: AAH27328.1.
BC056638 mRNA. Translation: AAH56638.1.
BC087949 mRNA. Translation: AAH87949.1.
CCDSiCCDS22397.1.
RefSeqiNP_932763.1. NM_198095.2.
UniGeneiMm.260325.

Genome annotation databases

EnsembliENSMUST00000051672; ENSMUSP00000051921; ENSMUSG00000046718.
GeneIDi69550.
KEGGimmu:69550.
UCSCiuc009mdr.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK009361 mRNA. Translation: BAC25254.1.
AK154399 mRNA. Translation: BAE32560.1.
BC027328 mRNA. Translation: AAH27328.1.
BC056638 mRNA. Translation: AAH56638.1.
BC087949 mRNA. Translation: AAH87949.1.
CCDSiCCDS22397.1.
RefSeqiNP_932763.1. NM_198095.2.
UniGeneiMm.260325.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3NI0X-ray1.60A/B53-151[»]
ProteinModelPortaliQ8R2Q8.
SMRiQ8R2Q8. Positions 57-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ8R2Q8. 1 interaction.
STRINGi10090.ENSMUSP00000051921.

PTM databases

iPTMnetiQ8R2Q8.
PhosphoSiteiQ8R2Q8.
SwissPalmiQ8R2Q8.

Proteomic databases

EPDiQ8R2Q8.
MaxQBiQ8R2Q8.
PaxDbiQ8R2Q8.
PeptideAtlasiQ8R2Q8.
PRIDEiQ8R2Q8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051672; ENSMUSP00000051921; ENSMUSG00000046718.
GeneIDi69550.
KEGGimmu:69550.
UCSCiuc009mdr.1. mouse.

Organism-specific databases

CTDi684.
MGIiMGI:1916800. Bst2.

Phylogenomic databases

eggNOGiENOG410JE1U. Eukaryota.
ENOG41115GP. LUCA.
GeneTreeiENSGT00390000013782.
HOGENOMiHOG000013084.
HOVERGENiHBG004902.
InParanoidiQ8R2Q8.
KOiK06731.
OMAiECRNTTH.
OrthoDBiEOG7D59R5.
PhylomeDBiQ8R2Q8.
TreeFamiTF338345.

Miscellaneous databases

ChiTaRSiBst2. mouse.
EvolutionaryTraceiQ8R2Q8.
PROiQ8R2Q8.
SOURCEiSearch...

Gene expression databases

BgeeiQ8R2Q8.
CleanExiMM_BST2.
GenevisibleiQ8R2Q8. MM.

Family and domain databases

InterProiIPR024886. BST2.
[Graphical view]
PANTHERiPTHR15190. PTHR15190. 1 hit.
PfamiPF16716. BST2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Dendritic cell and Tongue.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech II.
    Tissue: Liver and Mammary tumor.
  3. "Molecular cloning and characterization of a surface antigen preferentially overexpressed on multiple myeloma cells."
    Ohtomo T., Sugamata Y., Ozaki Y., Ono K., Yoshimura Y., Kawai S., Koishihara Y., Ozaki S., Kosaka M., Hirano T., Tsuchiya M.
    Biochem. Biophys. Res. Commun. 258:583-591(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION.
  4. "Bone marrow stromal cell antigen 2 is a specific marker of type I IFN-producing cells in the naive mouse, but a promiscuous cell surface antigen following IFN stimulation."
    Blasius A.L., Giurisato E., Cella M., Schreiber R.D., Shaw A.S., Colonna M.
    J. Immunol. 177:3260-3265(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION BY INTERFERONS, FUNCTION.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-70 AND ASN-94.
  6. "Tetherin-mediated restriction of filovirus budding is antagonized by the Ebola glycoprotein."
    Kaletsky R.L., Francica J.R., Agrawal-Gamse C., Bates P.
    Proc. Natl. Acad. Sci. U.S.A. 106:2886-2891(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INDUCTION BY EBOLA GP PROTEIN.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Heart, Liver, Lung and Spleen.
  8. Cited for: FUNCTION.
  9. "Endogenous CD317/Tetherin limits replication of HIV-1 and murine leukemia virus in rodent cells and is resistant to antagonists from primate viruses."
    Goffinet C., Schmidt S., Kern C., Oberbremer L., Keppler O.T.
    J. Virol. 84:11374-11384(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. "Interferon-induced tetherin restricts vesicular stomatitis virus release in neurons."
    Sarojini S., Theofanis T., Reiss C.S.
    DNA Cell Biol. 30:965-974(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. "Tetherin is a key effector of the antiretroviral activity of type I interferon in vitro and in vivo."
    Liberatore R.A., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 108:18097-18101(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Paradoxical roles of BST2/tetherin in promoting type I IFN response and viral infection."
    Swiecki M., Wang Y., Gilfillan S., Lenschow D.J., Colonna M.
    J. Immunol. 188:2488-2492(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Restriction of retroviral replication by tetherin/BST-2."
    Hammonds J., Wang J.J., Spearman P.
    Mol. Biol. Int. 2012:424768-424768(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  14. "Bone marrow stromal cell antigen 2 (BST-2) restricts mouse mammary tumor virus (MMTV) replication in vivo."
    Jones P.H., Mehta H.V., Maric M., Roller R.J., Okeoma C.M.
    Retrovirology 9:10-10(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  15. "Structural and biophysical analysis of BST-2/tetherin ectodomains reveals an evolutionary conserved design to inhibit virus release."
    Swiecki M., Scheaffer S.M., Allaire M., Fremont D.H., Colonna M., Brett T.J.
    J. Biol. Chem. 286:2987-2997(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 53-151, COILED-COIL DOMAIN, SUBUNIT, DISULFIDE BONDS.

Entry informationi

Entry nameiBST2_MOUSE
AccessioniPrimary (citable) accession number: Q8R2Q8
Secondary accession number(s): Q8CEY7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 17, 2006
Last sequence update: June 1, 2002
Last modified: July 6, 2016
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.