GN_SUHVK
ID GN_SUHVK Reviewed; 98 AA.
AC Q87088;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 68.
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;
OS Suid herpesvirus 1 (strain Kaplan) (SuHV-1) (Pseudorabies virus (strain
OS Kaplan)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=33703;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND GLYCOSYLATION.
RX PubMed=8551587; DOI=10.1128/jvi.70.2.1237-1241.1996;
RA Joens A., Granzow H., Kuchling R., Mettenleiter T.C.;
RT "The UL49.5 gene of pseudorabies virus codes for an O-glycosylated
RT structural protein of the viral envelope.";
RL J. Virol. 70:1237-1241(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14671123; DOI=10.1128/jvi.78.1.424-440.2004;
RA Klupp B.G., Hengartner C.J., Mettenleiter T.C., Enquist L.W.;
RT "Complete, annotated sequence of the pseudorabies virus genome.";
RL J. Virol. 78:424-440(2004).
RN [3]
RP SUBUNIT, GLYCOSYLATION, AND DISULFIDE BOND.
RX PubMed=9420258; DOI=10.1128/jvi.72.1.550-557.1998;
RA Joens A., Dijkstra J.M., Mettenleiter T.C.;
RT "Glycoproteins M and N of pseudorabies virus form a disulfide-linked
RT complex.";
RL J. Virol. 72:550-557(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 ECO:0000269|PubMed:9420258}.
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 -!- PTM: O-glycosylated. {ECO:0000269|PubMed:8551587,
CC ECO:0000269|PubMed:9420258}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein N family.
CC {ECO:0000255|HAMAP-Rule:MF_04037}.
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DR EMBL; U38547; AAB02854.1; -; Genomic_DNA.
DR EMBL; BK001744; DAA02145.1; -; Genomic_DNA.
DR RefSeq; YP_068325.1; NC_006151.1.
DR TCDB; 8.B.25.1.1; the viral glycoprotein n (gn, ul49,5) tap inhibitor (gn-i) family.
DR GeneID; 2952538; -.
DR KEGG; vg:2952538; -.
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 1: Evidence at protein level;
KW Disulfide bond; Host Golgi apparatus; Host membrane; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..24
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 25..98
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000339175"
FT TOPO_DOM 25..60
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 82..98
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 49
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 98 AA; 10155 MW; B60084221E6C3864 CRC64;
MVSSAGLSLT LVAALCALVA PALSSIVSTE GPLPLLREES RINFWNAACA ARGVPVDQPT
AAAVTFYICL LAVLVVALGY ATRTCTRMLH ASPAGRRV
