GE_HHV1F
ID GE_HHV1F Reviewed; 552 AA.
AC Q703F0; Q86624;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE AltName: Full=gE-1;
DE Flags: Precursor;
GN Name=gE; ORFNames=US8;
OS Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=15367642; DOI=10.1128/jvi.78.19.10755-10764.2004;
RA Norberg P.R., Bergstroem T., Kekabdar E., Lindh M., Liljeqvist J.-A.;
RT "Phylogenetic analysis of clinical herpes simplex virus type 1 isolates
RT identified three genetic groups and recombinant viruses.";
RL J. Virol. 78:10755-10764(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-552.
RX PubMed=8389914; DOI=10.1128/jvi.67.7.3961-3968.1993;
RA Georgopoulou U., Michaelidou A., Roizman B., Mavromara-Nazos P.;
RT "Identification of a new transcriptional unit that yields a gene product
RT within the unique sequences of the short component of the herpes simplex
RT virus 1 genome.";
RL J. Virol. 67:3961-3968(1993).
RN [3]
RP FUNCTION, AND INTERACTION WITH GLYCOPROTEIN I.
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 [4]
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION.
RX PubMed=18753205; DOI=10.1128/jvi.01241-08;
RA Snyder A., Polcicova K., Johnson D.C.;
RT "Herpes simplex virus gE/gI and US9 proteins promote transport of both
RT capsids and virion glycoproteins in neuronal axons.";
RL J. Virol. 82:10613-10624(2008).
RN [7]
RP SUBCELLULAR LOCATION.
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:16537585, ECO:0000269|PubMed:18753205,
CC ECO:0000269|PubMed:2831396}.
CC -!- FUNCTION: The heterodimer gE/gI serves as a receptor for the Fc part of
CC host 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 IgG-mediated immune responses (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with gI; this interaction enhances the Fc receptor
CC function of gE. The heterodimer gE/gI interacts with the Fc part of
CC host IgG. Interacts (via C-terminus) with VP22 tegument protein; this
CC interaction is necessary for the recruitment of VP22 to the Golgi and
CC its packaging into virions. Interacts (via C-terminus) with UL11
CC tegument protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:18596102};
CC Single-pass type I 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 host 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 -!- PTM: Phosphorylated on serines within the acidic cluster.
CC Phosphorylation determines whether endocytosed viral gE traffics to the
CC trans-Golgi network or recycles to the cell membrane. {ECO:0000305}.
CC -!- PTM: N-glycosylated, and sulfated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000305}.
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DR EMBL; AJ626469; CAF24756.1; -; Genomic_DNA.
DR EMBL; S62895; AAB27080.1; -; Genomic_DNA.
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 Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003404; Herpes_glycopE.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF02480; Herpes_gE; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; Glycoprotein; Host cell junction; Host cell membrane;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Phosphoprotein; Signal; Sulfation; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral immunoevasion; Virion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..552
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038226"
FT TOPO_DOM 21..421
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 443..552
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 63..88
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 162..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 237..382
FT /note="Fc-binding"
FT /evidence="ECO:0000250"
FT REGION 393..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..497
FT /note="Interaction with VP22 and UL11"
FT /evidence="ECO:0000250"
FT REGION 478..486
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 484..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 465..468
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT MOTIF 474..477
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 175..189
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 176
FT /note="Sulfotyrosine; by host"
FT /evidence="ECO:0000255"
FT MOD_RES 478
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 479
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 505
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 124
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 245
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 273..299
FT /evidence="ECO:0000250"
FT DISULFID 282..291
FT /evidence="ECO:0000250"
FT DISULFID 316..325
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 59313 MW; 8F689BF77BE07BB7 CRC64;
MDRGAVVGFL LGVCVVSCLA GTPKTSWRRV SVGEDVSLLP APGPTGRGPT QKLLWAVEPL
DGCGPLHPSW XSLMPPKQVP ETVVDAACMR APVPLAMAYA PPAPSATGGL RTDFVWQERA
AVVNRSLVIY GVRETDSGLY TLSVGDIKDP ARQVASVVLV VQPAPVPTPP PTPADYDEDD
NDEGEGEDES LAGTPASGTP RLPPPPAPPR SWPSAPEVSH VRGVTVRMET PEAILFSPGE
AFSTNVSIHA IAHDDQTYTM DVVWLRFDVP TSCAEMRIYE SCLYHPQLPE CLSPADAPCA
ASTWTSRLAV RSYAGCSRTN PPPRCSAEAH MEPVPGLAWQ AASVNLEFRD ASPQHSGLYL
CVVYVNDHIH AWGHITISTA AXYRNAVVEQ PLPQRGADLA EPTHPHVGAP PHAPPTHGAL
RLGAVMGAAL LLSVLGLSVW ACMTCWRRRA WRAVKSRASG KGPTYIRVAD SELYADWSSD
SEGERDQVPW LAPPERPDSP STNGSGFEIL SPTAPSVYPR SDGHQSRRQL TTFGSGRPDR
RYSQASDSSV FW
