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 24-JAN-2024, entry version 79. 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; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus; OC Simplexvirus humanalpha1; Human herpesvirus 1. 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 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:0016020; C: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 //