ID   GN_HCMVM                Reviewed;         135 AA.
AC   F5HHQ0;
DT   21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 27.
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=UL73;
OS   Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=295027;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA   Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA   Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA   Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT   "Genetic content of wild-type human cytomegalovirus.";
RL   J. Gen. Virol. 85:1301-1312(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   -!- 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. {ECO:0000250|UniProtKB:P16795}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC       {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR   EMBL; AY446894; AAR31725.1; -; Genomic_DNA.
DR   RefSeq; YP_081521.1; NC_006273.2.
DR   PRIDE; F5HHQ0; -.
DR   DNASU; 3077417; -.
DR   GeneID; 3077417; -.
DR   KEGG; vg:3077417; -.
DR   Reactome; R-HSA-9609690; HCMV Early Events.
DR   Reactome; R-HSA-9610379; HCMV Late Events.
DR   Proteomes; UP000000938; 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:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0019031; C:viral envelope; TAS:Reactome.
DR   GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR   HAMAP; MF_04037; HSV_GN; 1.
DR   InterPro; IPR021003; Cytomegalovirus_glycopN_N.
DR   InterPro; IPR005211; Herpes_glycoprotein_N_domain.
DR   InterPro; IPR034707; HSV_GN.
DR   Pfam; PF03554; Herpes_UL73; 1.
DR   Pfam; PF12522; UL73_N; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   CHAIN           20..135
FT                   /note="Envelope glycoprotein N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT                   /id="PRO_0000416451"
FT   TOPO_DOM        20..98
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TOPO_DOM        120..135
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   REGION          21..73
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        87
FT                   /note="Interchain (with gM)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ   SEQUENCE   135 AA;  14469 MW;  72FFFE83D5DD676C CRC64;
     MEWNTLVLGL LVLSVVASSN NTSTASTPRP SSSTHASTTV KATTVATTST TTATSTSSTT
     SAKPGSTTHD PNVMRPHAHN DFYNAHCTSH MYELSLSSFA AWWTMLNALI LMGAFCIVLR
     HCCFQNFTAT TTKGY