ID GI_HHV2H Reviewed; 372 AA.
AC P13291;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=Envelope glycoprotein I;
DE Short=gI;
DE Flags: Precursor;
GN Name=gI; ORFNames=US7;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC Simplexvirus humanalpha2; Human herpesvirus 2.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027242; DOI=10.1099/0022-1317-68-1-19;
RA McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT "DNA sequence and genetic content of the HindIII l region in the short
RT unique component of the herpes simplex virus type 2 genome: identification
RT of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL J. Gen. Virol. 68:19-38(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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.
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:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host cell junction
CC {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass
CC type I membrane protein {ECO:0000250}. Note=During virion
CC morphogenesis, this protein probably accumulates in the endosomes and
CC trans-Golgi where secondary envelopment occurs. It is probably
CC transported to the cell surface from where it is endocytosed and
CC directed to the trans-Golgi network (TGN). The heterodimer gE/gI then
CC redistribute to cell junctions to promote cell-cell spread later in the
CC infection (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family.
CC {ECO:0000305}.
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DR EMBL; X04798; CAA28485.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06714.1; -; Genomic_DNA.
DR PIR; F43674; F43674.
DR RefSeq; YP_009137219.1; NC_001798.2.
DR GlyCosmos; P13291; 4 sites, No reported glycans.
DR DNASU; 1487359; -.
DR GeneID; 1487359; -.
DR KEGG; vg:1487359; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0044178; C:host cell Golgi membrane; 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 3: Inferred from homology;
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..372
FT /note="Envelope glycoprotein I"
FT /id="PRO_0000115771"
FT TOPO_DOM 21..262
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..372
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 198..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..372
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..229
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..344
FT /note="Polar 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 169
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 243
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 372 AA; 39558 MW; C0D4A22CAB16E8D7 CRC64;
MPGRSLQGLA ILGLWVCATG LVVRGPTVSL VSDSLVDAGA VGPQGFVEED LRVFGELHFV
GAQVPHTNYY DGIIELFHYP LGNHCPRVVH VVTLTACPRR PAVAFTLCRS THHAHSPAYP
TLELGLARQP LLRVRTATRD YAGLYVLRVW VGSATNASRF VLGVALSANG TFVYNGSDYG
SCDPAQLPFS APRLGPSSVY TPGASRPTPP RTTTPPSSPR DPTPAPGDTG TPAPASGEIA
PPNSTRSASE SRHRLTVAQV IQIAIPASII AFVFLGSCIC FIHRCQRRYR RPRGQIYNPG
GVSCAVNEAA MARLGAELRS HPNTPPKPRR RSSSSTTMPS LTSIAEESEP GPVVLLSVSP
RPRSGPTAPQ EV
//
