ID   GN_EBVB9                Reviewed;         102 AA.
AC   P03196; Q777F2;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   21-JUL-1986, sequence version 1.
DT   03-AUG-2022, entry version 91.
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 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   INTERACTION WITH GM, AND GLYCOSYLATION.
RX   PubMed=9621013; DOI=10.1128/jvi.72.7.5559-5564.1998;
RA   Lake C.M., Molesworth S.J., Hutt-Fletcher L.M.;
RT   "The Epstein-Barr virus (EBV) gN homolog BLRF1 encodes a 15-kilodalton
RT   glycoprotein that cannot be authentically processed unless it is
RT   coexpressed with the EBV gM homolog BBRF3.";
RL   J. Virol. 72:5559-5564(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=11070013; DOI=10.1128/jvi.74.23.11162-11172.2000;
RA   Lake C.M., Hutt-Fletcher L.M.;
RT   "Epstein-Barr virus that lacks glycoprotein gN is impaired in assembly and
RT   infection.";
RL   J. Virol. 74:11162-11172(2000).
RN   [4]
RP   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).
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       ECO:0000269|PubMed:11070013}.
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 (Probable). Contains alpha 2,6-sialic acid
CC       residues. {ECO:0000269|PubMed:9621013}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC       {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR   EMBL; V01555; CAA24851.1; -; Genomic_DNA.
DR   EMBL; AJ507799; CAD53415.1; -; Genomic_DNA.
DR   PIR; F43041; QQBE18.
DR   RefSeq; YP_401665.1; NC_007605.1.
DR   BioGRID; 971758; 1.
DR   IntAct; P03196; 4.
DR   MINT; P03196; -.
DR   PRIDE; P03196; -.
DR   DNASU; 3783716; -.
DR   GeneID; 3783716; -.
DR   KEGG; vg:3783716; -.
DR   Proteomes; UP000153037; 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   1: Evidence at protein level;
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_0000116218"
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