GN_EBVG
ID GN_EBVG Reviewed; 102 AA.
AC P0C6Z4; 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 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: 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; AY961628; AAY41114.1; -; Genomic_DNA.
DR RefSeq; YP_401665.1; NC_007605.1.
DR BioGRID; 971758; 1.
DR IntAct; P0C6Z4; 3.
DR DNASU; 3783716; -.
DR GeneID; 3783716; -.
DR KEGG; vg:3783716; -.
DR Proteomes; UP000007641; 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; Signal;
KW Transmembrane; Transmembrane helix; 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_0000375952"
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
