ID   GI_HHV11                Reviewed;         390 AA.
AC   P06487; B9VQK1; Q09I70;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Envelope glycoprotein I;
DE            Short=gI;
DE   Flags: Precursor;
GN   Name=gI; ORFNames=US7;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2984429; DOI=10.1016/0022-2836(85)90320-1;
RA   McGeoch D.J., Dolan A., Donald S., Rixon F.J.;
RT   "Sequence determination and genetic content of the short unique region in
RT   the genome of herpes simplex virus type 1.";
RL   J. Mol. Biol. 181:1-13(1985).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated herpes
RT   simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   FUNCTION, AND INTERACTION WITH GLYCOPROTEIN E.
RC   STRAIN=17 syn+, and F;
RX   PubMed=2831396; DOI=10.1128/jvi.62.4.1347-1354.1988;
RA   Johnson D.C., Frame M.C., Ligas M.W., Cross A.M., Stow N.D.;
RT   "Herpes simplex virus immunoglobulin G Fc receptor activity depends on a
RT   complex of two viral glycoproteins, gE and gI.";
RL   J. Virol. 62:1347-1354(1988).
RN   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=11134295; DOI=10.1128/jvi.75.2.821-833.2001;
RA   Johnson D.C., Webb M., Wisner T.W., Brunetti C.;
RT   "Herpes simplex virus gE/gI sorts nascent virions to epithelial cell
RT   junctions, promoting virus spread.";
RL   J. Virol. 75:821-833(2001).
RN   [6]
RP   FUNCTION.
RC   STRAIN=KOS;
RX   PubMed=14734541; DOI=10.1074/jbc.m313281200;
RA   Sprague E.R., Martin W.L., Bjorkman P.J.;
RT   "pH dependence and stoichiometry of binding to the Fc region of IgG by the
RT   herpes simplex virus Fc receptor gE-gI.";
RL   J. Biol. Chem. 279:14184-14193(2004).
RN   [7]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=F;
RX   PubMed=16537585; DOI=10.1128/jvi.80.7.3167-3179.2006;
RA   Farnsworth A., Johnson D.C.;
RT   "Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at
RT   early times and then redistribute to cell junctions to promote cell-cell
RT   spread.";
RL   J. Virol. 80:3167-3179(2006).
RN   [8]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=F;
RX   PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA   Loret S., Guay G., Lippe R.;
RT   "Comprehensive characterization of extracellular herpes simplex virus type
RT   1 virions.";
RL   J. Virol. 82:8605-8618(2008).
CC   -!- FUNCTION: In epithelial cells, the heterodimer gE/gI is required for
CC       the cell-to-cell spread of the virus, by sorting nascent virions to
CC       cell junctions. Once the virus reaches the cell junctions, virus
CC       particles can spread to adjacent cells extremely rapidly through
CC       interactions with cellular receptors that accumulate at these
CC       junctions. Implicated in basolateral spread in polarized cells. In
CC       neuronal cells, gE/gI is essential for the anterograde spread of the
CC       infection throughout the host nervous system. Together with US9, the
CC       heterodimer gE/gI is involved in the sorting and transport of viral
CC       structural components toward axon tips. {ECO:0000269|PubMed:11134295,
CC       ECO:0000269|PubMed:14734541, ECO:0000269|PubMed:2831396}.
CC   -!- FUNCTION: The heterodimer gE/gI serves as a receptor for the Fc part of
CC       human IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus
CC       be involved in anti-HSV antibodies bipolar bridging, followed by
CC       intracellular endocytosis and degradation, thereby interfering with
CC       host Ig-mediated immune responses.
CC   -!- SUBUNIT: Interacts with gE; this interaction enhances the Fc receptor
CC       function of gE. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:18596102};
CC       Single-pass membrane protein {ECO:0000255}. Host cell membrane
CC       {ECO:0000269|PubMed:16537585}; Single-pass type I membrane protein
CC       {ECO:0000255}. Host cell junction {ECO:0000269|PubMed:11134295,
CC       ECO:0000269|PubMed:16537585}. Host Golgi apparatus, host trans-Golgi
CC       network {ECO:0000269|PubMed:16537585}. Note=During virion
CC       morphogenesis, this protein probably accumulates in the trans-Golgi
CC       where secondary envelopment occurs. The heterodimer gE/gI then
CC       redistributes to cell junctions to promote cell-cell spread later in
CC       the infection. {ECO:0000269|PubMed:11134295}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family.
CC       {ECO:0000305}.
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DR   EMBL; X14112; CAA32284.1; -; Genomic_DNA.
DR   EMBL; X02138; CAA26061.1; -; Genomic_DNA.
DR   EMBL; L00036; AAA96681.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63525.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62296.1; -; Genomic_DNA.
DR   PIR; A05243; QQBE77.
DR   RefSeq; YP_009137142.1; NC_001806.2.
DR   ChEMBL; CHEMBL2364696; -.
DR   DrugCentral; P06487; -.
DR   GlyCosmos; P06487; 3 sites, No reported glycans.
DR   DNASU; 2703446; -.
DR   GeneID; 2703446; -.
DR   KEGG; vg:2703446; -.
DR   PRO; PR:P06487; -.
DR   Proteomes; UP000009294; Genome.
DR   Proteomes; UP000180652; Genome.
DR   GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0044156; C:host cell junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C: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:0019049; P:virus-mediated perturbation of host defense response; IEA:UniProtKB-KW.
DR   InterPro; IPR002874; Herpes_gI.
DR   Pfam; PF01688; Herpes_gI; 1.
PE   1: Evidence at protein level;
KW   Glycoprotein; Host cell junction; Host cell membrane; Host Golgi apparatus;
KW   Host membrane; Host-virus interaction; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral immunoevasion; Virion.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..390
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000115770"
FT   TOPO_DOM        21..276
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        298..390
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          200..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          334..390
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        201..235
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        236..252
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        372..390
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        156
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        175
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        257
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   VARIANT         73
FT                   /note="G -> V (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         165
FT                   /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         225..231
FT                   /note="Missing (in strain: Nonneuroinvasive mutant HF10)"
SQ   SEQUENCE   390 AA;  41370 MW;  39381B1D6B5F08C8 CRC64;
     MPCRPLQGLV LVGLWVCATS LVVRGPTVSL VSNSFVDAGA LGPDGVVEED LLILGELRFV
     GDQVPHTTYY DGGVELWHYP MGHKCPRVVH VVTVTACPRR PAVAFALCRA TDSTHSPAYP
     TLELNLAQQP LLRVQRATRD YAGVYVLRVW VGDAPNASLF VLGMAIAAEG TLAYNGSAYG
     SCDPKLLPSS APRLAPASVY QPAPNQASTP STTTSTPSTT IPAPSTTIPA PQASTTPFPT
     GDPKPQPPGV NHEPPSNATR ATRDSRYALT VTQIIQIAIP ASIIALVFLG SCICFIHRCQ
     RRYRRSRRPI YSPQMPTGIS CAVNEAAMAR LGAELKSHPS TPPKSRRRSS RTPMPSLTAI
     AEESEPAGAA GLPTPPVDPT TPTPTPPLLV
//