GN_GAHVM
ID GN_GAHVM Reviewed; 95 AA.
AC Q77MR4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, 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=MDV064;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14244.1; -; Genomic_DNA.
DR RefSeq; YP_001033979.1; NC_002229.3.
DR GeneID; 4811524; -.
DR KEGG; vg:4811524; -.
DR Proteomes; UP000008072; 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;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT SIGNAL 1..26
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 27..95
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000406579"
FT TOPO_DOM 27..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..95
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 46
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 95 AA; 10160 MW; 35F4FC80CA223064 CRC64;
MGLMDIHNAV CSLVIGVAIL IATSQATFVD WGSSITSMGD FWESTCSAVG VSIAFSSGFS
VLFYMGLVAV ISALLAGSYH ACFRLFTADM FKEEW
