GN_BHV1C
ID GN_BHV1C Reviewed; 96 AA.
AC Q77CE4;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 58.
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 Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9010999; DOI=10.1016/s0378-1135(96)01235-7;
RA Schwyzer M., Styger D., Vogt B., Lowery D.E., Simard C., LaBoissiere S.,
RA Misra V., Vlcek C., Paces V.;
RT "Gene contents in a 31-kb segment at the left genome end of bovine
RT herpesvirus-1.";
RL Vet. Microbiol. 53:67-77(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Schwyzer M., Paces V., Letchworth G.J., Misra V., Buhk H.J., Lowery D.E.,
RA Simard C., Bello L.J., Thiry E., Vlcek C.;
RT "Complete DNA sequence of bovine herpesvirus 1.";
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBUNIT, AND DISULFIDE BOND.
RX PubMed=9525625; DOI=10.1128/jvi.72.4.3029-3036.1998;
RA Wu S.X., Zhu X.P., Letchworth G.J.;
RT "Bovine herpesvirus 1 glycoprotein M forms a disulfide-linked heterodimer
RT with the U(L)49.5 protein.";
RL J. Virol. 72:3029-3036(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 -!- INTERACTION:
CC Q77CE4; Q03518: TAP1; Xeno; NbExp=6; IntAct=EBI-11303846, EBI-747259;
CC Q77CE4; P36372: Tap2; Xeno; NbExp=2; IntAct=EBI-11303846, EBI-11304494;
CC Q77CE4; Q03519: TAP2; Xeno; NbExp=2; IntAct=EBI-11303846, EBI-780781;
CC Q77CE4; O15533: TAPBP; Xeno; NbExp=2; IntAct=EBI-11303846, EBI-874801;
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; AJ004801; CAA06084.1; -; Genomic_DNA.
DR RefSeq; NP_045309.1; NC_001847.1.
DR SMR; Q77CE4; -.
DR IntAct; Q77CE4; 5.
DR GeneID; 4783426; -.
DR KEGG; vg:4783426; -.
DR GO; GO:0044165; C:host cell endoplasmic reticulum; IDA:AgBase.
DR GO; GO:0044177; C:host cell Golgi apparatus; IMP:AgBase.
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 GO; GO:0046978; F:TAP1 binding; IPI:AgBase.
DR GO; GO:0046979; F:TAP2 binding; IPI:AgBase.
DR GO; GO:0046980; F:tapasin binding; IPI:AgBase.
DR GO; GO:0045862; P:positive regulation of proteolysis; IMP:AgBase.
DR GO; GO:0090087; P:regulation of peptide transport; IMP:AgBase.
DR GO; GO:0061635; P:regulation of protein complex stability; IMP:AgBase.
DR GO; GO:1903317; P:regulation of protein maturation; IMP:AgBase.
DR GO; GO:0046776; P:suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I; IMP:AgBase.
DR GO; GO:0039657; P:suppression by virus of host gene expression; IMP:AgBase.
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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT CHAIN 22..96
FT /note="Envelope glycoprotein N"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT /id="PRO_0000339174"
FT TOPO_DOM 22..54
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT TOPO_DOM 76..96
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
FT DISULFID 42
FT /note="Interchain (with gM)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04037"
SQ SEQUENCE 96 AA; 10260 MW; 7C96E4FF67386AB9 CRC64;
MPRSPLIVAV VAAALFAIVR GRDPLLDAMR REGAMDFWSA GCYARGVPLS EPPQALVVFY
VALTAVMVAV ALYAYGLCFR LMGASGPNKK ESRGRG
