GI_HHV11
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 03-AUG-2022, entry version 91.
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; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
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 PRIDE; P06487; -.
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: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 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
