ID   BARF1_EBVA8             Reviewed;         221 AA.
AC   P0C6N0; Q777A5;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
DE   RecName: Full=Secreted protein BARF1;
DE   AltName: Full=33 kDa early protein;
DE   AltName: Full=p33;
DE   Flags: Precursor;
GN   Name=BARF1;
OS   Epstein-Barr virus (strain AG876) (HHV-4) (Human herpesvirus 4).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX   NCBI_TaxID=82830;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA   Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT   "The genome of Epstein-Barr virus type 2 strain AG876.";
RL   Virology 350:164-170(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 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homohexamer. Interacts with human CSF1 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Note=Massively secreted in the serum of
CC       EBV-induced nasophyryngeal carcinoma patients. {ECO:0000250}.
CC   -!- PTM: Phosphorylated on serine and threonine by host. {ECO:0000250}.
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DR   EMBL; DQ279927; ABB89291.1; -; Genomic_DNA.
DR   RefSeq; YP_001129512.1; NC_009334.1.
DR   RefSeq; YP_401719.1; NC_007605.1.
DR   SMR; P0C6N0; -.
DR   DNASU; 3783772; -.
DR   GeneID; 3783772; -.
DR   GeneID; 5176183; -.
DR   KEGG; vg:3783772; -.
DR   KEGG; vg:5176183; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0051781; P:positive regulation of cell division; IDA:CACAO.
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   3: Inferred from homology;
KW   Disulfide bond; Early protein; Glycoprotein; Immunoglobulin domain;
KW   Oncogene; Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..221
FT                   /note="Secreted protein BARF1"
FT                   /id="PRO_0000116200"
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:0000250"
FT   DISULFID        146..201
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
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