BDLF2_EBVG
ID BDLF2_EBVG Reviewed; 420 AA.
AC Q3KSQ7;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 23-FEB-2022, entry version 34.
DE RecName: Full=Protein BDLF2;
GN ORFNames=BDLF2;
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: 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 (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with BMRF2. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type
CC II membrane protein {ECO:0000250}.
CC -!- DOMAIN: Plasma membrane remodeling is mediated by the cytoplasmic tail.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae BDLF2 family. {ECO:0000305}.
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DR EMBL; AY961628; AAY41142.1; -; Genomic_DNA.
DR IntAct; Q3KSQ7; 17.
DR MINT; Q3KSQ7; -.
DR Proteomes; UP000007641; 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 3: Inferred from homology;
KW Glycoprotein; Late protein; Membrane; Signal-anchor; Transmembrane;
KW Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..420
FT /note="Protein BDLF2"
FT /id="PRO_0000408270"
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 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; 46072 MW; 965016C138376ADD CRC64;
MVDEQVAVEH GTVSHTISRE EDGVVHERRV LASGERVEVF YKAPAPRPRE GRASTFHDFT
VPAAAAVPGP EPEPEPHPAM PIHANGGGET KTNTQDQNQN QTTRARTNAK AEERTAEMDD
TMASSGGQRG APISADLLSL SSLTGRMAAM APSWMKSEVC GERMRFKEDV YDGEAETLAE
PPRCFMLSFV FIYYCCYLAF LALLAFGFNP LFLPSFMPVG AKVLRGKGRD FGVPLSYGCP
TNPFCKVYTL IPAVVINNVT YYPNNTDSLG GHGGFEAAAL HVAALFESGC PNLQAVTNRN
RTFNVTRASG RVERRLVQDM QRVLASAVVV MHHHCHYETY YVFDGVGPEF GTIPTPSFKD
VLAFRPSLVT NCTAPLKTSV KGPNWSGAAG GMKRKQCRVD RLTDRSFPAY LEEVMYVMVQ
