BST2_CRIGR
ID BST2_CRIGR Reviewed; 203 AA.
AC Q6WRU0;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Bone marrow stromal antigen 2;
DE Short=BST-2;
DE AltName: Full=Luminal membrane-associated protein GREG;
DE AltName: CD_antigen=CD317;
DE Flags: Precursor;
GN Name=Bst2;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, SUBUNIT, AND GPI-ANCHOR
RP AT SER-183.
RX PubMed=17251550; DOI=10.1091/mbc.e06-03-0236;
RA Li X., Kaloyanova D., van Eijk M., Eerland R., van der Goot G.,
RA Oorschot V., Klumperman J., Lottspeich F., Starkuviene V., Wieland F.T.,
RA Helms J.B.;
RT "Involvement of a Golgi-resident GPI-anchored protein in maintenance of the
RT Golgi structure.";
RL Mol. Biol. Cell 18:1261-1271(2007).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: 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). Parallel
CC homodimer; disulfide-linked. May form homotetramers under reducing
CC conditions. Dimerization is essential for its antiviral activity.
CC {ECO:0000250, ECO:0000269|PubMed:17251550}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
CC {ECO:0000269|PubMed:17251550}. Cell membrane
CC {ECO:0000269|PubMed:17251550}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:17251550}. Cell membrane
CC {ECO:0000269|PubMed:17251550}; Lipid-anchor, GPI-anchor
CC {ECO:0000269|PubMed:17251550}. Late endosome {ECO:0000250}. Membrane
CC raft {ECO:0000250}. Cytoplasm {ECO:0000250}. Apical cell membrane
CC {ECO:0000250}. Note=Shuttles between the cell membrane, where it is
CC present predominantly in membrane/lipid rafts, and the trans-Golgi
CC network. Forms a complex with MMP14 and localizes to the cytoplasm (By
CC similarity). {ECO:0000250}.
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: The GPI anchor is essential for its antiviral activity.
CC {ECO:0000250}.
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DR EMBL; AY272060; AAQ16301.1; -; mRNA.
DR RefSeq; NP_001231044.1; NM_001244115.1.
DR AlphaFoldDB; Q6WRU0; -.
DR SMR; Q6WRU0; -.
DR STRING; 10029.NP_001231044.1; -.
DR Ensembl; ENSCGRT00001016649; ENSCGRP00001012415; ENSCGRG00001013835.
DR GeneID; 100689092; -.
DR KEGG; cge:100689092; -.
DR CTD; 684; -.
DR eggNOG; ENOG502TB0V; Eukaryota.
DR GeneTree; ENSGT00390000013782; -.
DR OMA; TSHRYSR; -.
DR OrthoDB; 1579815at2759; -.
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; ISS:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005770; C:late endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0008191; F:metalloendopeptidase inhibitor activity; ISS:UniProtKB.
DR GO; GO:0051607; P:defense response to virus; IEA:InterPro.
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; 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; 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 Lipoprotein; Membrane; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..183
FT /note="Bone marrow stromal antigen 2"
FT /id="PRO_0000253550"
FT PROPEP 184..203
FT /note="Removed in mature form"
FT /evidence="ECO:0000255"
FT /id="PRO_0000253551"
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..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT COILED 66..178
FT /evidence="ECO:0000255"
FT LIPID 183
FT /note="GPI-anchor amidated serine"
FT /evidence="ECO:0000269|PubMed:17251550"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 54
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 64
FT /note="Interchain"
FT /evidence="ECO:0000250"
FT DISULFID 92
FT /note="Interchain"
FT /evidence="ECO:0000250"
SQ SEQUENCE 203 AA; 22826 MW; 83D82F6B26504B94 CRC64;
MAPTFYHYHP LPMDQKEPGC GIRWRCLAAA SVLILVALVI PLIIFAVKAN SEACRDGLRA
QEECSNTTRL LQRQLTRSQD NLAQAEAQAS TCNRTVVTLQ DSLEKKVSQI QEKQALIQEQ
EAQIKEQEAQ IKEQEAQIKE QKAHIQEQQV RIQKLEGEVE EFEQKLKKLR TAEEASITSK
QNSAGSMAVS SLLVLAVPLF LLF
