ID   BMRF2_EBVA8             Reviewed;         357 AA.
AC   Q1HVH3;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   02-JUN-2021, entry version 37.
DE   RecName: Full=Protein BMRF2;
GN   ORFNames=BMRF2;
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: Facilitates virus attachment to oral epithelial cells by
CC       binding to host beta1 integrin family. Participates in rearrangement of
CC       cellular actin to increase intercellular contacts by binding BDLF2 and
CC       thereby promote virus cell-to-cell spreading (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with BDLF2. Interacts with host beta1 integrin
CC       family (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane; Multi-pass membrane protein.
CC       Host cell membrane. Note=In EBV-infected polarized oral epithelial
CC       cells, is transported to the basolateral membranes and colocalizes with
CC       beta1 integrin. {ECO:0000250}.
CC   -!- DOMAIN: The RGD motif presumably is the main binding site to host beta1
CC       integrins. {ECO:0000250}.
CC   -!- PTM: Extensively glycosylated by O-linked oligosaccharides.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the herpesviridae BMRF2 family. {ECO:0000305}.
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DR   EMBL; DQ279927; ABB89235.1; -; Genomic_DNA.
DR   RefSeq; YP_001129455.1; NC_009334.1.
DR   PRIDE; Q1HVH3; -.
DR   GeneID; 5176179; -.
DR   KEGG; vg:5176179; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR   GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW.
DR   InterPro; IPR006727; Herpes_BMRF2.
DR   Pfam; PF04633; Herpes_BMRF2; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell membrane; Host membrane; Host-virus interaction;
KW   Membrane; Reference proteome; Transmembrane; Viral attachment to host cell;
KW   Virion; Virus entry into host cell.
FT   CHAIN           1..357
FT                   /note="Protein BMRF2"
FT                   /id="PRO_0000408277"
FT   TOPO_DOM        1..11
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        12..32
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        33..46
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        47..67
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        68..70
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        71..91
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        92..98
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..121
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        122..133
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        134..154
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        155..158
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        180..217
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..240
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        241..261
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        262..267
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        289..298
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        299..319
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        320..335
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        336..356
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        357
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   MOTIF           199..201
FT                   /note="Integrin binding site"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   357 AA;  39502 MW;  18E151894A845BF3 CRC64;
     MFSCKQHLSL GACVFCLGLL ASTPFIWCFV FANLLSLEIF SPWQTHVYRL GFPTACLMAV
     LWTLVPAKHA VRAVTPAIML NIASALIFFS LRVYSTSTWV SAPCLFLANL PLLCLWPRLA
     IEIVYICPAI HQRFFELGLL LACTIFALSV VSRALEVSAV FMSPFFIFLA LGSGSLAGAR
     RNQIYTSGLE RRRSIFCARG DHSVASLKET LHKCPWDLLA ISALTVLVVC VMIVLHVHAE
     VFFGLSRYLP LFLCGAMASG GLYLGHSSII ACVMATLCTL SSVVVYFLHE TLGPLGKTVL
     FISIFVYYFS GVAALSAAMR YKLKKFVNGP LVHLRVVYMC CFVFTFCEYL LVTFIKS