GN_EHV1V
ID GN_EHV1V Reviewed; 100 AA.
AC P84449; Q6S6R1;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
DE Flags: Precursor;
GN Name=gN {ECO:0000255|HAMAP-Rule:MF_04037}; OrderedLocusNames=10;
OS Equine herpesvirus 1 (strain V592) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=310273;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAS45894.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Davis-Poynter N., Nugent J., Birch-Machin I., Allen G.P.;
RL Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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; AY464052; AAS45894.1; -; Genomic_DNA.
DR RefSeq; YP_053055.1; NC_001491.2.
DR SMR; P84449; -.
DR GeneID; 1487565; -.
DR KEGG; vg:1487565; -.
DR Proteomes; UP000008296; 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; IPR008647; GN_domain.
DR InterPro; IPR034707; HSV_GN.
DR Pfam; PF05702; Herpes_UL49_5; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Host Golgi apparatus; Host membrane; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 28..100
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000116164"
FT TOPO_DOM 28..63
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 64..84
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 85..100
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 51
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 100 AA; 10802 MW; B53A8AC6F24BB4C7 CRC64;
MLSTRFVTLA ILACLLVVLG LARGAGGDPG VKQRIDVARE EERRDFWHAA CSGHGFPITT
PSTAAILFYV SLLAVGVAVA CQAYRAVLRI VTLEMLQHLH
