BST2_RAT
ID BST2_RAT Reviewed; 172 AA.
AC Q811A2;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Bone marrow stromal antigen 2;
DE Short=BST-2;
DE AltName: Full=Protein DAMP-1;
DE AltName: CD_antigen=CD317;
DE Flags: Precursor;
GN Name=Bst2; Synonyms=Damp1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, TOPOLOGY, GPI-ANCHOR,
RP GLYCOSYLATION, AND SUBCELLULAR LOCATION.
RC STRAIN=Wistar; TISSUE=Liver;
RX PubMed=12956872; DOI=10.1034/j.1600-0854.2003.00129.x;
RA Kupzig S., Korolchuk V., Rollason R., Sugden A., Wilde A., Banting G.;
RT "Bst-2/HM1.24 is a raft-associated apical membrane protein with an unusual
RT topology.";
RL Traffic 4:694-709(2003).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ARHGAP44.
RX PubMed=19273615; DOI=10.1083/jcb.200804154;
RA Rollason R., Korolchuk V., Hamilton C., Jepson M., Banting G.;
RT "A CD317/tetherin-RICH2 complex plays a critical role in the organization
RT of the subapical actin cytoskeleton in polarized epithelial cells.";
RL J. Cell Biol. 184:721-736(2009).
RN [3]
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).
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 (By similarity). Plays a role in the
CC organization of the subapical actin cytoskeleton in polarized
CC epithelial cells. {ECO:0000250, ECO:0000269|PubMed:19273615,
CC ECO:0000269|PubMed:20702620}.
CC -!- SUBUNIT: Parallel homodimer; disulfide-linked. May form homotetramers
CC under reducing conditions. Dimerization is essential for its antiviral
CC activity. Interacts with MMP14 (via C-terminal cytoplasmic tail) (By
CC similarity). Interacts with LILRA4/ILT7 (By similarity). Interacts (via
CC cytoplasmic domain) with ARHGAP44. {ECO:0000250,
CC ECO:0000269|PubMed:19273615}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network. Cell
CC membrane; Single-pass type II membrane protein. Cell membrane; Lipid-
CC anchor, GPI-anchor. Late endosome {ECO:0000250}. Membrane raft.
CC Cytoplasm {ECO:0000250}. Apical cell membrane. Note=Shuttles between
CC the cell membrane, where it is present predominantly in membrane/lipid
CC rafts, and the trans-Golgi network. Forms a complex with MMP14 and
CC localizes to the cytoplasm (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC brain and liver. Present in liver (at protein level).
CC {ECO:0000269|PubMed:12956872}.
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 -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12956872}.
CC -!- PTM: The GPI anchor is essential for its antiviral activity.
CC {ECO:0000250}.
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DR EMBL; AJ538349; CAD61869.1; -; mRNA.
DR RefSeq; NP_937767.1; NM_198134.2.
DR AlphaFoldDB; Q811A2; -.
DR SMR; Q811A2; -.
DR BioGRID; 266956; 1.
DR IntAct; Q811A2; 1.
DR STRING; 10116.ENSRNOP00000031515; -.
DR GlyGen; Q811A2; 2 sites.
DR iPTMnet; Q811A2; -.
DR PhosphoSitePlus; Q811A2; -.
DR PaxDb; Q811A2; -.
DR PRIDE; Q811A2; -.
DR Ensembl; ENSRNOT00000091906; ENSRNOP00000073737; ENSRNOG00000059900.
DR GeneID; 378947; -.
DR KEGG; rno:378947; -.
DR UCSC; RGD:727849; rat.
DR CTD; 684; -.
DR RGD; 727849; Bst2.
DR eggNOG; ENOG502TB0V; Eukaryota.
DR GeneTree; ENSGT00390000013782; -.
DR InParanoid; Q811A2; -.
DR OrthoDB; 1579815at2759; -.
DR PhylomeDB; Q811A2; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q811A2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005771; C:multivesicular body; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0051607; P:defense response to virus; ISO:RGD.
DR GO; GO:0045087; P:innate immune response; ISS: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; ISS: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; ISS:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP: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; ISS:UniProtKB.
DR InterPro; IPR024886; BST2.
DR PANTHER; PTHR15190; PTHR15190; 1.
DR Pfam; PF16716; BST2; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Coiled coil; Cytoplasm; Disulfide bond; Endosome;
KW Glycoprotein; Golgi apparatus; GPI-anchor; Immunity; Innate immunity;
KW Isopeptide bond; Lipoprotein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..152
FT /note="Bone marrow stromal antigen 2"
FT /id="PRO_0000253555"
FT PROPEP 153..172
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000253556"
FT TOPO_DOM 1..26
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 27..47
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 48..152
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT COILED 103..149
FT /evidence="ECO:0000255"
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:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 58
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 68
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 96
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT CROSSLNK 20
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q10589"
SQ SEQUENCE 172 AA; 19674 MW; 5B1018EBBDD0FB19 CRC64;
MAPSFYHYLP VAMDERWEPK GWSIRRWWLV AAILVVLIGV VLVCLIVYFA NAAHSEACKN
GLRLQDECRN TTHLLKHQLT RAQDSLLQTE MQANSCNQTV MDLRDSLKKK VSQTQEQQAR
IKELENKIER LNQELENLRT QKEISTTVQV NSGGSVVVSS LLVLVAVLFL HF
