BMRF2_EBVB9
ID BMRF2_EBVB9 Reviewed; 357 AA.
AC P03192; Q777F8;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 89.
DE RecName: Full=Protein BMRF2;
GN ORFNames=BMRF2;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2441081; DOI=10.1128/jvi.61.9.2943-2946.1987;
RA Pfitzner A.J., Strominger J.L., Speck S.H.;
RT "Characterization of a cDNA clone corresponding to a transcript from the
RT Epstein-Barr virus BamHI M fragment: evidence for overlapping mRNAs.";
RL J. Virol. 61:2943-2946(1987).
RN [3]
RP IDENTIFICATION, AND SUBCELLULAR LOCATION.
RX PubMed=1333758; DOI=10.1007/bf01309601;
RA Modrow S., Hoflacher B., Wolf H.;
RT "Identification of a protein encoded in the EB-viral open reading frame
RT BMRF2.";
RL Arch. Virol. 127:379-386(1992).
RN [4]
RP INTERACTION WITH HOST BETA1 INTEGRIN FAMILY.
RX PubMed=12592401; DOI=10.1038/nm830;
RA Tugizov S.M., Berline J.W., Palefsky J.M.;
RT "Epstein-Barr virus infection of polarized tongue and nasopharyngeal
RT epithelial cells.";
RL Nat. Med. 9:307-314(2003).
RN [5]
RP CHARACTERIZATION, AND SUBCELLULAR LOCATION.
RX PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA Illanes D., Sarracino D., Kieff E.;
RT "Proteins of purified Epstein-Barr virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN [6]
RP FUNCTION.
RX PubMed=18350146; DOI=10.1371/journal.pone.0001808;
RA Gill M.B., Edgar R., May J.S., Stevenson P.G.;
RT "A gamma-herpesvirus glycoprotein complex manipulates actin to promote
RT viral spread.";
RL PLoS ONE 3:E1808-E1808(2008).
RN [7]
RP CHARACTERIZATION, AND GLYCOSYLATION.
RX PubMed=17081581; DOI=10.1016/j.virol.2006.09.047;
RA Xiao J., Palefsky J.M., Herrera R., Tugizov S.M.;
RT "Characterization of the Epstein-Barr virus glycoprotein BMRF-2.";
RL Virology 359:382-396(2007).
RN [8]
RP FUNCTION.
RX PubMed=17945327; DOI=10.1016/j.virol.2007.09.012;
RA Xiao J., Palefsky J.M., Herrera R., Berline J., Tugizov S.M.;
RT "The Epstein-Barr virus BMRF-2 protein facilitates virus attachment to oral
RT epithelial cells.";
RL Virology 370:430-442(2008).
RN [9]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BDLF2.
RX PubMed=18995876; DOI=10.1016/j.virol.2008.10.010;
RA Gore M., Hutt-Fletcher L.M.;
RT "The BDLF2 protein of Epstein-Barr virus is a type II glycosylated envelope
RT protein whose processing is dependent on coexpression with the BMRF2
RT protein.";
RL Virology 383:162-167(2009).
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.
CC {ECO:0000269|PubMed:17945327, ECO:0000269|PubMed:18350146}.
CC -!- SUBUNIT: Interacts with BDLF2. Interacts with host beta1 integrin
CC family. {ECO:0000269|PubMed:12592401, ECO:0000269|PubMed:18995876}.
CC -!- INTERACTION:
CC P03192; P05556: ITGB1; Xeno; NbExp=2; IntAct=EBI-9348955, EBI-703066;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:15534216};
CC Multi-pass membrane protein {ECO:0000255}. Host cell membrane
CC {ECO:0000269|PubMed:18995876}; Multi-pass membrane protein
CC {ECO:0000255}. Note=In EBV-infected polarized oral epithelial cells, is
CC transported to the basolateral membranes and colocalizes with beta1
CC integrin. {ECO:0000269|PubMed:17945327}.
CC -!- DOMAIN: The RGD motif presumably is the main binding site to host beta1
CC integrins.
CC -!- PTM: Extensively glycosylated by O-linked oligosaccharides.
CC {ECO:0000269|PubMed:17081581}.
CC -!- SIMILARITY: Belongs to the herpesviridae BMRF2 family. {ECO:0000305}.
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DR EMBL; V01555; CAA24845.1; -; Genomic_DNA.
DR EMBL; M17322; AAA45878.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53408.1; -; Genomic_DNA.
DR PIR; C43041; QQBE14.
DR RefSeq; YP_401658.1; NC_007605.1.
DR IntAct; P03192; 4.
DR MINT; P03192; -.
DR DNASU; 3783719; -.
DR GeneID; 3783719; -.
DR KEGG; vg:3783719; -.
DR Proteomes; UP000153037; 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 1: Evidence at protein level;
KW Early protein; Glycoprotein; Host cell membrane; Host membrane;
KW Host-virus interaction; Membrane; Reference proteome; Transmembrane;
KW Viral attachment to host cell; Virion; Virus entry into host cell.
FT CHAIN 1..357
FT /note="Protein BMRF2"
FT /id="PRO_0000116254"
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="Virion surface"
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="Virion surface"
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="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..217
FT /note="Virion surface"
FT TRANSMEM 218..238
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..240
FT /note="Virion surface"
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="Virion surface"
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="Virion surface"
FT /evidence="ECO:0000255"
FT MOTIF 199..201
FT /note="Integrin binding site"
FT /evidence="ECO:0000255"
SQ SEQUENCE 357 AA; 39516 MW; BDB101894C5980F5 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 TSVVVYFLHE TLGPLGKTVL
FISIFVYYFS GVAALSAAMR YKLKKFVNGP LVHLRVVYMC CFVFTFCEYL LVTFIKS
