GN_HHV11
ID GN_HHV11 Reviewed; 91 AA.
AC O09800; B9VQH8;
DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=UL49.5, UL49A;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17229708; DOI=10.1128/jvi.01463-06;
RA Mach M., Osinski K., Kropff B., Schloetzer-Schrehardt U., Krzyzaniak M.,
RA Britt W.;
RT "The carboxy-terminal domain of glycoprotein N of human cytomegalovirus is
RT required for virion morphogenesis.";
RL J. Virol. 81:5212-5224(2007).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=F;
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
RN [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=25505065; DOI=10.1128/jvi.03041-14;
RA El Kasmi I., Lippe R.;
RT "Herpes simplex virus 1 gN partners with gM to modulate the viral fusion
RT machinery.";
RL J. Virol. 89:2313-2323(2015).
RN [6]
RP FUNCTION, DISULFIDE BOND, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=26999189; DOI=10.3390/v8030083;
RA Striebinger H., Funk C., Raschbichler V., Bailer S.M.;
RT "Subcellular trafficking and functional relationship of the HSV-1
RT glycoproteins N and M.";
RL Viruses 8:83-83(2016).
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:17229708, ECO:0000269|PubMed:25505065,
CC ECO:0000269|PubMed:26999189}.
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:26999189}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04037,
CC ECO:0000269|PubMed:18596102}; Single-pass type I membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_04037}. Host membrane {ECO:0000255|HAMAP-
CC Rule:MF_04037}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04037}. Host Golgi apparatus, host trans-Golgi network
CC {ECO:0000255|HAMAP-Rule:MF_04037, ECO:0000269|PubMed:25505065,
CC ECO:0000269|PubMed:26999189}. Note=When coexpressed with gM, localizes
CC in the host trans-Golgi network. {ECO:0000255|HAMAP-Rule:MF_04037,
CC ECO:0000269|PubMed:25505065}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC {ECO:0000255|HAMAP-Rule:MF_04037}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X14112; CAA32300.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62273.1; -; Genomic_DNA.
DR RefSeq; YP_009137125.1; NC_001806.2.
DR ChEMBL; CHEMBL2364696; -.
DR DrugCentral; O09800; -.
DR PRIDE; O09800; -.
DR GeneID; 2703419; -.
DR KEGG; vg:2703419; -.
DR PRO; PR:O09800; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; 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 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..23
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 24..91
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000116098"
FT TOPO_DOM 24..55
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 77..91
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT REGION 23..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 46
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037,
FT ECO:0000269|PubMed:26999189"
SQ SEQUENCE 91 AA; 9202 MW; 8CF33C769092BB5F CRC64;
MGPPRRVCRA GLLFVLLVAL AAGDAGPRGE PPGEEGGRDG IGGARCETQN TGQMSAPGAL
VPFYVGMASM GVCIIAHVCQ ICQRLLAAGH A
