ID   GP42_EBVG               Reviewed;         223 AA.
AC   P0C6Z5; Q777E6;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   23-FEB-2022, entry version 56.
DE   RecName: Full=Glycoprotein 42;
DE            Short=gp42;
DE   Contains:
DE     RecName: Full=Soluble gp42;
GN   ORFNames=BZLF2;
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 a role in virion attachment to host B-lymphocytes,
CC       through binding to leukocyte antigen (HLA) class II and subsequently
CC       participates in fusion of the virion with host membranes. May act as a
CC       tropism switch that directs fusion with B-lymphocytes and inhibits
CC       fusion with epithelial cells (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Forms a complex with gp25 and gp85 via its N-terminus; this
CC       complex is used for invasion of B-lymphocytes. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P0C6Z5; P0C734: BTRF1; NbExp=2; IntAct=EBI-2621381, EBI-2621388;
CC   -!- SUBCELLULAR LOCATION: Virion membrane. Note=virions synthesized in B-
CC       lymphocytes contain a lower amount of gp42 due to sequestration by
CC       cellular HLA class II protein, whereas virions made from epithelial
CC       cells has a higher amount of gp42. Membrane; Single-pass membrane
CC       protein (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The C-lectin type domain is essential for virion-induced
CC       membrane fusion.
CC   -!- SIMILARITY: Belongs to the epstein barr virus gp42 family.
CC       {ECO:0000305}.
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DR   EMBL; AY961628; AAY41121.1; -; Genomic_DNA.
DR   RefSeq; YP_401672.1; NC_007605.1.
DR   PDB; 5T1D; X-ray; 3.10 A; C=33-223.
DR   PDB; 6C5V; EM; 4.80 A; C=33-223.
DR   PDBsum; 5T1D; -.
DR   PDBsum; 6C5V; -.
DR   SMR; P0C6Z5; -.
DR   BioGRID; 971787; 1.
DR   IntAct; P0C6Z5; 4.
DR   MINT; P0C6Z5; -.
DR   DNASU; 3783745; -.
DR   GeneID; 3783745; -.
DR   KEGG; vg:3783745; -.
DR   Proteomes; UP000007641; Genome.
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:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   SUPFAM; SSF56436; SSF56436; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Disulfide bond; Host-virus interaction; Lectin; Membrane;
KW   Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..223
FT                   /note="Glycoprotein 42"
FT                   /id="PRO_0000375941"
FT   CHAIN           34..223
FT                   /note="Soluble gp42"
FT                   /id="PRO_0000433227"
FT   TOPO_DOM        1..8
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..223
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          111..217
FT                   /note="C-type lectin"
FT   SITE            33..34
FT                   /note="Potential cleavage"
FT                   /evidence="ECO:0000305"
FT   DISULFID        99..138
FT                   /evidence="ECO:0000250"
FT   DISULFID        102..115
FT                   /evidence="ECO:0000250"
FT   DISULFID        128..214
FT                   /evidence="ECO:0000250"
FT   DISULFID        132..216
FT                   /evidence="ECO:0000250"
FT   DISULFID        192..208
FT                   /evidence="ECO:0000250"
FT   HELIX           67..70
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          92..94
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          104..106
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          108..111
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          114..118
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   HELIX           128..133
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          136..138
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   TURN            146..148
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   HELIX           149..154
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          169..172
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          193..195
FT                   /evidence="ECO:0007829|PDB:5T1D"
FT   STRAND          214..218
FT                   /evidence="ECO:0007829|PDB:5T1D"
SQ   SEQUENCE   223 AA;  25257 MW;  F87541F6CEC26D74 CRC64;
     MVSFKQVRVP LFTAIALVIV LLLAYFLPPR VRGGGRVAAA AITWVPKPNV EVWPVDPPPP
     VNFNKTAEQE YGDKEVKLPH WTPTLHTFQV PQNYTKANCT YCNTREYTFS YKGCCFYFTK
     KKHTWNGCFQ ACAELYPCTY FYGPTPDILP VVTRNLNAIE SLWVGVYRVG EGNWTSLDGG
     TFKVYQIFGS HCTYVSKFST VPVSHHECSF LKPCLCVSQR SNS