ID   GN_VZVD                 Reviewed;          87 AA.
AC   Q65ZG0;
DT   10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, 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}; ORFNames=9A;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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; X04370; CAH19068.1; -; Genomic_DNA.
DR   IntAct; Q65ZG0; 7.
DR   MINT; Q65ZG0; -.
DR   PRIDE; Q65ZG0; -.
DR   Proteomes; UP000002602; 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; IPR008647; GN_domain.
DR   InterPro; IPR034707; HSV_GN.
DR   Pfam; PF05702; Herpes_UL49_5; 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..87
FT                   /note="Envelope glycoprotein N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT                   /id="PRO_0000339176"
FT   TOPO_DOM        25..48
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TRANSMEM        49..69
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TOPO_DOM        70..87
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   DISULFID        38
FT                   /note="Interchain (with gM)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ   SEQUENCE   87 AA;  9762 MW;  96669F5AA8D668A8 CRC64;
     MGSITASFIL ITMQILFFCE DSSGEPNFAE RNFWHASCSA RGVYIDGSMI TTLFFYASLL
     GVCVALISLA YHACFRLFTR SVLRSTW