ID   GP42_EBVA8              Reviewed;         223 AA.
AC   Q1HVG2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   29-SEP-2021, entry version 57.
DE   RecName: Full=Glycoprotein 42;
DE            Short=gp42;
GN   ORFNames=BZLF2;
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: 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   -!- 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; DQ279927; ABB89246.1; -; Genomic_DNA.
DR   RefSeq; YP_001129466.1; NC_009334.1.
DR   SMR; Q1HVG2; -.
DR   BindingDB; Q1HVG2; -.
DR   PRIDE; Q1HVG2; -.
DR   GeneID; 5176170; -.
DR   KEGG; vg:5176170; -.
DR   PRO; PR:Q1HVG2; -.
DR   Proteomes; UP000007639; 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   3: Inferred from homology;
KW   Disulfide bond; Host-virus interaction; Lectin; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..223
FT                   /note="Glycoprotein 42"
FT                   /id="PRO_0000375942"
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   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"
SQ   SEQUENCE   223 AA;  25412 MW;  B01D300F8CC82055 CRC64;
     MVSFKQVRVP LFTAIALVIV LLLAYFLPPR VRGGGRVSAA AITWVPKPNV EVWPVDPPPP
     VNFNKTAEQE YGDKEIKLPH WTPTLHTFQV PKNYTKANCT YCNTREYTFS YKERCFYFTK
     KKHTWNGCFQ ACAELYPCTY FYGPTPDILP VVTRNLNAIE SLWVGVYRVG EGNWTSLDGG
     TFKVYQIFGS HCTYVSKFST VPVSHHECSF LKPCLCVSQR SNS