ID   GN_EBVA8                Reviewed;         102 AA.
AC   P0C6Z3; Q777F2;
DT   26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
DE   Flags: Precursor;
GN   Name=gN {ECO:0000255|HAMAP-Rule:MF_04037}; ORFNames=BLRF1;
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: Envelope glycoprotein necessary for proper maturation of gM
CC       and modulation of its membrane fusion activity. Also plays a critical
CC       role in virion morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- SUBUNIT: Interacts (via N-terminus) with gM (via N-terminus). The gM-gN
CC       heterodimer forms the gCII complex. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04037}. Host membrane {ECO:0000255|HAMAP-Rule:MF_04037};
CC       Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04037}.
CC       Host Golgi apparatus, host trans-Golgi network {ECO:0000255|HAMAP-
CC       Rule:MF_04037}. Note=When coexpressed with gM, localizes in the host
CC       trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04037}.
CC   -!- PTM: O-glycosylated. Contains alpha 2,6-sialic acid residues.
CC       {ECO:0000250|UniProtKB:P03196}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC       {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR   EMBL; DQ279927; ABB89240.1; -; Genomic_DNA.
DR   RefSeq; YP_001129460.1; NC_009334.1.
DR   RefSeq; YP_401665.1; NC_007605.1.
DR   DNASU; 3783716; -.
DR   GeneID; 3783716; -.
DR   GeneID; 5176229; -.
DR   KEGG; vg:3783716; -.
DR   KEGG; vg:5176229; -.
DR   Proteomes; UP000007639; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
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.
DR   HAMAP; MF_04037; HSV_GN; 1.
DR   InterPro; IPR005211; Herpes_glycoprotein_N_domain.
DR   InterPro; IPR034707; HSV_GN.
DR   Pfam; PF03554; Herpes_UL73; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Host Golgi apparatus; Host membrane; Membrane;
KW   Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW   Viral envelope protein; Virion.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   CHAIN           33..102
FT                   /note="Envelope glycoprotein N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT                   /id="PRO_0000375951"
FT   TOPO_DOM        33..69
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TOPO_DOM        91..102
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   DISULFID        55
FT                   /note="Interchain (with gM)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ   SEQUENCE   102 AA;  10944 MW;  DF40CC9B30B060B3 CRC64;
     MGKVLRKPFA KAVPLLFLAA TWLLTGVLPA GASSPTNAAA ASLTEAQDQF YSYTCNADTF
     SPSLTSFASI WALLTLVLVI IASAIYLMYV CFNKFVNTLL TD