BARF1_EBVG
ID BARF1_EBVG Reviewed; 221 AA.
AC P0CW72; Q777A5;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 02-JUN-2021, entry version 41.
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 GD1) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10376;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16306603; DOI=10.1128/jvi.79.24.15323-15330.2005;
RA Zeng M.-S., Li D.-J., Liu Q.-L., Song L.-B., Li M.-Z., Zhang R.-H.,
RA Yu X.-J., Wang H.-M., Ernberg I., Zeng Y.-X.;
RT "Genomic sequence analysis of Epstein-Barr virus strain GD1 from a
RT nasopharyngeal carcinoma patient.";
RL J. Virol. 79:15323-15330(2005).
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 -!- INTERACTION:
CC P0CW72; P0CW72: BARF1; NbExp=2; IntAct=EBI-2620133, EBI-2620133;
CC P0CW72; P09603: CSF1; Xeno; NbExp=3; IntAct=EBI-2620133, EBI-2872294;
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; AY961628; AAY41158.1; -; Genomic_DNA.
DR RefSeq; YP_401719.1; NC_007605.1.
DR PDB; 4FA8; X-ray; 2.20 A; A/B/D=19-221.
DR PDBsum; 4FA8; -.
DR SMR; P0CW72; -.
DR DIP; DIP-60066N; -.
DR IntAct; P0CW72; 5.
DR DNASU; 3783772; -.
DR GeneID; 3783772; -.
DR KEGG; vg:3783772; -.
DR Proteomes; UP000007641; 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; Repeat; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..221
FT /note="Secreted protein BARF1"
FT /id="PRO_0000408390"
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 DISULFID 146..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 29..34
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:4FA8"
FT TURN 53..55
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:4FA8"
FT HELIX 72..74
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 86..93
FT /evidence="ECO:0007829|PDB:4FA8"
FT HELIX 96..98
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 100..108
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 111..133
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 142..152
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 183..191
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 199..207
FT /evidence="ECO:0007829|PDB:4FA8"
FT STRAND 209..216
FT /evidence="ECO:0007829|PDB:4FA8"
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