GN_HHV2H
ID GN_HHV2H Reviewed; 87 AA.
AC Q86539; O12513;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
DE Flags: Precursor;
GN Name=gN {ECO:0000255|HAMAP-Rule:MF_04037};
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1322965; DOI=10.1099/0022-1317-73-8-2167;
RA Barnett B.C., Dolan A., Telford E.A., Davison A.J., McGeoch D.J.;
RT "A novel herpes simplex virus gene (UL49A) encodes a putative membrane
RT protein with counterparts in other herpesviruses.";
RL J. Gen. Virol. 73:2167-2171(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06736.1; -; Genomic_DNA.
DR PIR; JQ1683; JQ1683.
DR RefSeq; YP_009137202.1; NC_001798.2.
DR PRIDE; Q86539; -.
DR DNASU; 1487337; -.
DR GeneID; 1487337; -.
DR KEGG; vg:1487337; -.
DR Proteomes; UP000001874; 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; IPR017376; Herpes_UL49A.
DR InterPro; IPR034707; HSV_GN.
DR PIRSF; PIRSF038075; Herpes_UL49A_env; 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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 26..87
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000385483"
FT TOPO_DOM 26..51
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 52..72
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 73..87
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 87 AA; 8782 MW; 6581844686B50296 CRC64;
MTGKPARLGR WVVLLFVALV AGVPGEPPNA AGARGVIGDA QCRGDSAGVV SVPGVLVPFY
LGMTSMGVCM IAHVYQICQR ALAAGSA
