ID   GN_HHV8P                Reviewed;         110 AA.
AC   F5HFQ0;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   28-JUN-2011, sequence version 1.
DT   03-AUG-2022, entry version 32.
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=ORF53;
OS   Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS   sarcoma-associated herpesvirus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX   NCBI_TaxID=868565;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA   Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT   "Identification of a spliced gene from Kaposi's sarcoma-associated
RT   herpesvirus encoding a protein with similarities to latent membrane
RT   proteins 1 and 2A of Epstein-Barr virus.";
RL   J. Virol. 73:6953-6963(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA   Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT   "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL   J. Gen. Virol. 87:1781-1804(2006).
RN   [3]
RP   FUNCTION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND INTERACTION WITH GM.
RX   PubMed=12771417; DOI=10.1099/vir.0.18941-0;
RA   Koyano S., Mar E.C., Stamey F.R., Inoue N.;
RT   "Glycoproteins M and N of human herpesvirus 8 form a complex and inhibit
RT   cell fusion.";
RL   J. Gen. Virol. 84:1485-1491(2003).
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:12771417}.
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       ECO:0000269|PubMed:12771417}.
CC   -!- INTERACTION:
CC       F5HFQ0; P88927: gM; Xeno; NbExp=2; IntAct=EBI-8841815, EBI-7931480;
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04037,
CC       ECO:0000269|PubMed:12771417}; Single-pass type I membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04037, ECO:0000269|PubMed:12771417}. Host
CC       membrane {ECO:0000255|HAMAP-Rule:MF_04037}; Single-pass type I membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_04037, ECO:0000269|PubMed:12771417}.
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 (By similarity). Contains alpha 2,6-sialic acid
CC       residues (By similarity). N-glycosylated. {ECO:0000250,
CC       ECO:0000269|PubMed:12771417}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC       {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR   EMBL; AF148805; ABD28904.1; -; Genomic_DNA.
DR   RefSeq; YP_001129406.1; NC_009333.1.
DR   SMR; F5HFQ0; -.
DR   IntAct; F5HFQ0; 1.
DR   PRIDE; F5HFQ0; -.
DR   DNASU; 4961468; -.
DR   GeneID; 4961468; -.
DR   KEGG; vg:4961468; -.
DR   Proteomes; UP000000942; 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..17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   CHAIN           18..110
FT                   /note="Envelope glycoprotein N"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT                   /id="PRO_0000423791"
FT   TOPO_DOM        18..80
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TRANSMEM        81..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   TOPO_DOM        102..110
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT   REGION          28..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        63
FT                   /note="Interchain (with gM)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ   SEQUENCE   110 AA;  11466 MW;  468877D25B4B0173 CRC64;
     MTASTVALAL FVASILGHCW VTANSTGVAS STERSSPSTA GLSARPSPGP TSVTTPGFYD
     VACSADSFSP SLSSFSSVWA LINALLVVVA TFFYLVYLCF FKFVDEVVHA