GN_MUHVS
ID GN_MUHVS Reviewed; 139 AA.
AC Q69150;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 2.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Envelope glycoprotein N {ECO:0000255|HAMAP-Rule:MF_04037};
GN Name=gN {ECO:0000255|HAMAP-Rule:MF_04037}; ORFNames=UL73;
OS Murid herpesvirus 1 (strain Smith) (MuHV-1) (Mouse cytomegalovirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Muromegalovirus.
OX NCBI_TaxID=10367;
OH NCBI_TaxID=10090; Mus musculus (Mouse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7483291; DOI=10.1007/bf01724298;
RA Messerle M., Rapp M., Lucin P., Koszinowski U.H.;
RT "Characterization of a conserved gene block in the murine cytomegalovirus
RT genome.";
RL Virus Genes 10:73-80(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=8971012; DOI=10.1128/jvi.70.12.8833-8849.1996;
RA Rawlinson W.D., Farrell H.E., Barrell B.G.;
RT "Analysis of the complete DNA sequence of murine cytomegalovirus.";
RL J. Virol. 70:8833-8849(1996).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA96662.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; L07319; AAA96662.1; ALT_FRAME; Genomic_DNA.
DR EMBL; U68299; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR Proteomes; UP000008774; 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; IPR005211; Herpes_glycoprotein_N_domain.
DR InterPro; IPR034707; HSV_GN.
DR Pfam; PF03554; Herpes_UL73; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Host Golgi apparatus; Host membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT CHAIN 1..139
FT /note="Envelope glycoprotein N"
FT /id="PRO_0000116221"
FT TOPO_DOM 1..100
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 101..121
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 122..139
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 91
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 139 AA; 14963 MW; 98943A0B64F686F2 CRC64;
MACGKTESGD DSGRFGRTGA GMFGFIMPGF VGIFRLSFFL LLSFAMASGS SSPASVPVSV
AASVPDTTVN KIVISDGSEA HNINEFYDVK CHSHFYGLSV SSFASIWMMV NAIVFICAFG
VFMRHWCYKA FTSDTAKGY
