BARF1_EBVB9
ID BARF1_EBVB9 Reviewed; 221 AA.
AC P03228; Q777A5;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 02-JUN-2021, entry version 91.
DE RecName: Full=Secreted protein BARF1;
DE AltName: Full=33 kDa early protein;
DE AltName: Full=p33;
DE Flags: Precursor;
GN ORFNames=BARF1;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [2]
RP IDENTIFICATION OF PROTEIN.
RX PubMed=2555151; DOI=10.1002/j.1460-2075.1989.tb08438.x;
RA Wei M.X., Ooka T.;
RT "A transforming function of the BARF1 gene encoded by Epstein-Barr virus.";
RL EMBO J. 8:2897-2903(1989).
RN [3]
RP INTERACTION WITH HUMAN CSF1.
RX PubMed=9557689; DOI=10.1128/jvi.72.5.4015-4021.1998;
RA Strockbine L.D., Cohen J.I., Farrah T., Lyman S.D., Wagener F.,
RA DuBose R.F., Armitage R.J., Spriggs M.K.;
RT "The Epstein-Barr virus BARF1 gene encodes a novel, soluble colony-
RT stimulating factor-1 receptor.";
RL J. Virol. 72:4015-4021(1998).
RN [4]
RP FUNCTION.
RX PubMed=15064715; DOI=10.1038/sj.onc.1207607;
RA Sall A., Caserta S., Jolicoeur P., Franqueville L., de Turenne-Tessier M.,
RA Ooka T.;
RT "Mitogenic activity of Epstein-Barr virus-encoded BARF1 protein.";
RL Oncogene 23:4938-4944(2004).
RN [5]
RP FUNCTION.
RX PubMed=15778977; DOI=10.1002/jmv.20327;
RA Seto E., Yang L., Middeldorp J., Sheen T.S., Chen J.Y., Fukayama M.,
RA Eizuru Y., Ooka T., Takada K.;
RT "Epstein-Barr virus (EBV)-encoded BARF1 gene is expressed in nasopharyngeal
RT carcinoma and EBV-associated gastric carcinoma tissues in the absence of
RT lytic gene expression.";
RL J. Med. Virol. 76:82-88(2005).
RN [6]
RP FUNCTION.
RX PubMed=16054293; DOI=10.1016/j.canlet.2005.06.023;
RA Wang Q., Tsao S.W., Ooka T., Nicholls J.M., Cheung H.W., Fu S., Wong Y.C.,
RA Wang X.;
RT "Anti-apoptotic role of BARF1 in gastric cancer cells.";
RL Cancer Lett. 238:90-103(2006).
RN [7]
RP IDENTIFICATION.
RX PubMed=16518412; DOI=10.1038/sj.onc.1209458;
RA Wang L., Tam J.P., Liu D.X.;
RT "Biochemical and functional characterization of Epstein-Barr virus-encoded
RT BARF1 protein: interaction with human hTid1 protein facilitates its
RT maturation and secretion.";
RL Oncogene 25:4320-4331(2006).
RN [8]
RP POST-TRANSLATIONAL MODIFICATIONS.
RX PubMed=17872516; DOI=10.1099/vir.0.83058-0;
RA de Turenne-Tessier M., Ooka T.;
RT "Post-translational modifications of Epstein Barr virus BARF1 oncogene-
RT encoded polypeptide.";
RL J. Gen. Virol. 88:2656-2661(2007).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=18533018; DOI=10.1186/1743-422x-5-70;
RA Fiorini S., Ooka T.;
RT "Secretion of Epstein-Barr virus-encoded BARF1 oncoprotein from latently
RT infected B cells.";
RL Virol. J. 5:70-70(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 21-221, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-95.
RX PubMed=16647084; DOI=10.1016/j.jmb.2006.03.056;
RA Tarbouriech N., Ruggiero F., de Turenne-Tessier M., Ooka T.,
RA Burmeister W.P.;
RT "Structure of the Epstein-Barr virus oncogene BARF1.";
RL J. Mol. Biol. 359:667-678(2006).
CC -!- FUNCTION: Plays diverse functions in immunomodulation and oncogenicity,
CC maybe by acting as a functional receptor for human CSF1. May inhibit
CC interferon secretion from mononuclear cells. Exhibits oncogenic
CC activity in vitro. {ECO:0000269|PubMed:15064715,
CC ECO:0000269|PubMed:15778977, ECO:0000269|PubMed:16054293}.
CC -!- SUBUNIT: Homohexamer. Interacts with human CSF1.
CC {ECO:0000269|PubMed:9557689}.
CC -!- INTERACTION:
CC P03228; P03228: BARF1; NbExp=3; IntAct=EBI-16007073, EBI-16007073;
CC P03228; P07141: Csf1; Xeno; NbExp=8; IntAct=EBI-16007073, EBI-777188;
CC P03228; P09603: CSF1; Xeno; NbExp=9; IntAct=EBI-16007073, EBI-2872294;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:18533018}.
CC Note=Massively secreted in the serum of EBV-induced nasophyryngeal
CC carcinoma patients.
CC -!- PTM: Phosphorylated on serine and threonine by host.
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DR EMBL; V01555; CAA24809.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53469.1; -; Genomic_DNA.
DR PIR; B43045; QQBE48.
DR RefSeq; YP_401719.1; NC_007605.1.
DR PDB; 2CH8; X-ray; 2.30 A; A/B/C/D=21-221.
DR PDB; 3UEZ; X-ray; 3.41 A; A/B/C/D=21-221.
DR PDB; 4ADF; X-ray; 4.40 A; A/B/C/D/E/F/M/N/O/P/Q/R=21-221.
DR PDB; 4ADQ; X-ray; 4.50 A; A/B/C/D=21-221.
DR PDBsum; 2CH8; -.
DR PDBsum; 3UEZ; -.
DR PDBsum; 4ADF; -.
DR PDBsum; 4ADQ; -.
DR SMR; P03228; -.
DR DIP; DIP-47684N; -.
DR IntAct; P03228; 3.
DR iPTMnet; P03228; -.
DR DNASU; 3783772; -.
DR GeneID; 3783772; -.
DR KEGG; vg:3783772; -.
DR EvolutionaryTrace; P03228; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR SUPFAM; SSF48726; SSF48726; 2.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Early protein; Glycoprotein;
KW Immunoglobulin domain; Oncogene; Reference proteome; Repeat; Secreted;
KW Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..221
FT /note="Secreted protein BARF1"
FT /id="PRO_0000408391"
FT DOMAIN 21..120
FT /note="Ig-like 1"
FT DOMAIN 124..220
FT /note="Ig-like 2"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:16647084"
FT DISULFID 146..201
FT /evidence="ECO:0000269|PubMed:16647084"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:2CH8"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2CH8"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:3UEZ"
FT STRAND 57..64
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2CH8"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:2CH8"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 111..133
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:3UEZ"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 198..205
FT /evidence="ECO:0007829|PDB:2CH8"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:2CH8"
SQ SEQUENCE 221 AA; 24471 MW; CA5A24D1EA28758E CRC64;
MARFIAQLLL LASCVAAGQA VTAFLGERVT LTSYWRRVSL GPEIEVSWFK LGPGEEQVLI
GRMHHDVIFI EWPFRGFFDI HRSANTFFLV VTAANISHDG NYLCRMKLGE TEVTKQEHLS
VVKPLTLSVH SERSQFPDFS VLTVTCTVNA FPHPHVQWLM PEGVEPAPTA ANGGVMKEKD
GSLSVAVDLS LPKPWHLPVT CVGKNDKEEA HGVYVSGYLS Q
