BDLF2_EBVB9
ID BDLF2_EBVB9 Reviewed; 420 AA.
AC P03225; Q777C4;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 68.
DE RecName: Full=Protein BDLF2;
GN ORFNames=BDLF2;
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, 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 [3]
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 [4]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH BMRF2.
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: Rearranges cellular actin to increase intercellular contacts
CC and thereby promote virus cell-to-cell spreading. Induce the outgrowth
CC of long, branched plasma membrane fronds to create intercellular
CC network for virion traffic. The fronds are actin based and RhoA-
CC dependent. {ECO:0000269|PubMed:18350146}.
CC -!- SUBUNIT: Interacts with BMRF2. {ECO:0000269|PubMed:18995876}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:15534216,
CC ECO:0000269|PubMed:18995876}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15534216, ECO:0000269|PubMed:18995876}.
CC -!- DOMAIN: Plasma membrane remodeling is mediated by the cytoplasmic tail.
CC -!- SIMILARITY: Belongs to the herpesviridae BDLF2 family. {ECO:0000305}.
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DR EMBL; V01555; CAA24836.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53445.1; -; Genomic_DNA.
DR PIR; G43044; QQBE44.
DR RefSeq; YP_401695.1; NC_007605.1.
DR IntAct; P03225; 79.
DR MINT; P03225; -.
DR PRIDE; P03225; -.
DR DNASU; 3783693; -.
DR GeneID; 3783693; -.
DR KEGG; vg:3783693; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
PE 1: Evidence at protein level;
KW Glycoprotein; Late protein; Membrane; Reference proteome; Signal-anchor;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..420
FT /note="Protein BDLF2"
FT /id="PRO_0000116267"
FT TOPO_DOM 1..184
FT /note="Intravirion"
FT TRANSMEM 185..205
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..420
FT /note="Virion surface"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 64..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 264
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 300
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 304
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 420 AA; 46168 MW; 4CA5C00D0385E530 CRC64;
MVDEQVAVEH GTVSHTISRE EDGVVHERRV LASGERVEVF YKAPAPRPRE GRASTFHDFT
VPAAAAVPGP EPEPEPHPPM PIHANGGGET KTNTQDQNQN QTTRTRTNAK AEERTAEMDD
TMASSGGQRG APISADLLSL SSLTGRMAAM APSWMKSEVC GERMRFKEDV YDGEAETLAE
PPRCFMLSFV FIYYCCYLAF LALLAFGFNP LFLPSFMPVG AKVLRGKGRD FGVPLSYGCP
TNPFCKVYTL IPAVVINNVT YYPNNTDSHG GHGGFEAAAL HVAALFESGC PNLQAVTNRN
RTFNVTRASG RVERRLVQDM QRVLASAVVV MHHHCHYETY YVFDGVGPEF GTIPTPCFKD
VLAFRPSLVT NCTAPLKTSV KGPNWSGAAG GMKRKQCRVD RLTDRSFPAY LEEVMYVMVQ
