GN_EHV2
ID GN_EHV2 Reviewed; 89 AA.
AC Q66655;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 56.
DE RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
DE Flags: Precursor;
GN Name=gN {ECO:0000255|HAMAP-Rule:MF_04037}; Synonyms=53;
OS Equine herpesvirus 2 (strain 86/87) (EHV-2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Percavirus.
OX NCBI_TaxID=82831;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7783207; DOI=10.1006/jmbi.1995.0314;
RA Telford E.A.R., Watson M.S., Aird H.C., Perry J., Davison A.J.;
RT "The DNA sequence of equine herpesvirus 2.";
RL J. Mol. Biol. 249:520-528(1995).
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 -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR EMBL; U20824; AAC13841.1; -; Genomic_DNA.
DR PIR; S55648; S55648.
DR RefSeq; NP_042650.1; NC_001650.2.
DR SMR; Q66655; -.
DR GeneID; 1461050; -.
DR KEGG; vg:1461050; -.
DR Proteomes; UP000007083; 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..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 25..89
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000406056"
FT TOPO_DOM 25..56
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 57..77
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 78..89
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 42
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 89 AA; 9928 MW; E6E33749A267E52B CRC64;
MAPGRGVLLL ICLCLMDNVS QVVCSQNSTT PSKFPTFYSY DCNADTYAPQ LTSFSTIWTL
LNVLVMTIAC VIYLIYMCFN KFVATMTNT
