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Envelope glycoprotein E (gE) (gE-1)

 GE_HHV11                Reviewed;         550 AA.
P04488; B9VQK2; Q09I69;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
25-OCT-2017, entry version 104.
RecName: Full=Envelope glycoprotein E;
Short=gE;
AltName: Full=gE-1;
Flags: Precursor;
Name=gE; ORFNames=US8;
Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus
1).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Simplexvirus.
NCBI_TaxID=10299;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2984429; DOI=10.1016/0022-2836(85)90320-1;
McGeoch D.J., Dolan A., Donald S., Rixon F.J.;
"Sequence determination and genetic content of the short unique region
in the genome of herpes simplex virus type 1.";
J. Mol. Biol. 181:1-13(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Nonneuroinvasive mutant HF10;
PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
"Determination and analysis of the DNA sequence of highly attenuated
herpes simplex virus type 1 mutant HF10, a potential oncolytic
virus.";
Microbes Infect. 9:142-149(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=17 syn+;
Cunningham C., Davison A.J.;
"Herpes simplex virus type 1 bacterial artificial chromosome.";
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
[4]
GLYCOSYLATION, AND SULFATION.
PubMed=6310034; DOI=10.1099/0022-1317-64-9-1943;
Hope R.G., Marsden H.S.;
"Processing of glycoproteins induced by herpes simplex virus type 1:
sulphation and nature of the oligosaccharide linkages.";
J. Gen. Virol. 64:1943-1953(1983).
[5]
FUNCTION, AND INTERACTION WITH GLYCOPROTEIN I.
STRAIN=17 syn+, and F;
PubMed=2831396;
Johnson D.C., Frame M.C., Ligas M.W., Cross A.M., Stow N.D.;
"Herpes simplex virus immunoglobulin G Fc receptor activity depends on
a complex of two viral glycoproteins, gE and gI.";
J. Virol. 62:1347-1354(1988).
[6]
PHOSPHORYLATION AT SER-476 AND SER-477.
PubMed=10725429;
Miriagou V., Stevanato L., Manservigi R., Mavromara P.;
"The C-terminal cytoplasmic tail of herpes simplex virus type 1 gE
protein is phosphorylated in vivo and in vitro by cellular enzymes in
the absence of other viral proteins.";
J. Gen. Virol. 81:1027-1031(2000).
[7]
FUNCTION.
STRAIN=KOS;
PubMed=14734541; DOI=10.1074/jbc.M313281200;
Sprague E.R., Martin W.L., Bjorkman P.J.;
"pH dependence and stoichiometry of binding to the Fc region of IgG by
the herpes simplex virus Fc receptor gE-gI.";
J. Biol. Chem. 279:14184-14193(2004).
[8]
INTERACTION WITH VP22 AND UL11 TEGUMENT PROTEINS.
STRAIN=F;
PubMed=17035313; DOI=10.1128/JVI.01842-06;
Farnsworth A., Wisner T.W., Johnson D.C.;
"Cytoplasmic residues of herpes simplex virus glycoprotein gE required
for secondary envelopment and binding of tegument proteins VP22 and
UL11 to gE and gD.";
J. Virol. 81:319-331(2007).
[9]
INTERACTION WITH VP22 TEGUMENT PROTEIN.
STRAIN=17 syn+;
PubMed=16997344; DOI=10.1016/j.virol.2006.08.024;
O'Regan K.J., Bucks M.A., Murphy M.A., Wills J.W., Courtney R.J.;
"A conserved region of the herpes simplex virus type 1 tegument
protein VP22 facilitates interaction with the cytoplasmic tail of
glycoprotein E (gE).";
Virology 358:192-200(2007).
[10]
INTERACTION WITH VP22 TEGUMENT PROTEIN.
PubMed=19279114; DOI=10.1128/JVI.00069-09;
Stylianou J., Maringer K., Cook R., Bernard E., Elliott G.;
"Virion incorporation of the herpes simplex virus type 1 tegument
protein VP22 occurs via glycoprotein E-specific recruitment to the
late secretory pathway.";
J. Virol. 83:5204-5218(2009).
[11]
X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF 213-390, X-RAY
CRYSTALLOGRAPHY (5.0 ANGSTROMS) OF 21-419 IN COMPLEX WITH HOST FC
RECEPTOR, AND DISULFIDE BONDS.
PubMed=16646632; DOI=10.1371/journal.pbio.0040148;
Sprague E.R., Wang C., Baker D., Bjorkman P.J.;
"Crystal structure of the HSV-1 Fc receptor bound to Fc reveals a
mechanism for antibody bipolar bridging.";
PLoS Biol. 4:E148-E148(2006).
-!- FUNCTION: In epithelial cells, the heterodimer gE/gI is required
for the cell-to-cell spread of the virus, by sorting nascent
virions to cell junctions. Once the virus reaches the cell
junctions, virus particles can spread to adjacent cells extremely
rapidly through interactions with cellular receptors that
accumulate at these junctions. Implicated in basolateral spread in
polarized cells (By similarity). In neuronal cells, gE/gI is
essential for the anterograde spread of the infection throughout
the host nervous system. Together with US9, the heterodimer gE/gI
is involved in the sorting and transport of viral structural
components toward axon tips. {ECO:0000250,
ECO:0000269|PubMed:14734541, ECO:0000269|PubMed:2831396}.
-!- FUNCTION: The heterodimer gE/gI serves as a receptor for the Fc
part of host IgG. Dissociation of gE/gI from IgG occurs at acidic
pH. May thus be involved in anti-HSV antibodies bipolar bridging,
followed by intracellular endocytosis and degradation, thereby
interfering with host IgG-mediated immune responses.
-!- SUBUNIT: Interacts with gI; this interaction enhances the Fc
receptor function of gE (By similarity). The heterodimer gE/gI
interacts with the Fc part of host IgG. Interacts (via C-terminus)
with VP22 tegument protein; this interaction is necessary for the
recruitment of VP22 to the Golgi and its packaging into virions.
Interacts (via C-terminus) with UL11 tegument protein.
{ECO:0000250, ECO:0000269|PubMed:16646632,
ECO:0000269|PubMed:16997344, ECO:0000269|PubMed:17035313,
ECO:0000269|PubMed:19279114, ECO:0000269|PubMed:2831396}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-15581257, EBI-15581257;
P01857:IGHG1 (xeno); NbExp=2; IntAct=EBI-15581257, EBI-356114;
-!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}. Host cell membrane
{ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Host cell junction. Host Golgi apparatus membrane {ECO:0000250};
Single-pass membrane protein {ECO:0000250}. Host endosome membrane
{ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Note=During virion morphogenesis, this protein probably
accumulates in the endosomes and trans-Golgi where secondary
envelopment occurs. It is probably transported to the cell surface
from where it is endocytosed and directed to the trans-Golgi
network (TGN), maybe through an interaction with PACS-1 sorting
protein. The heterodimer gE/gI then redistributes to cell
junctions to promote cell-cell spread later in the infection.
-!- PTM: Phosphorylated on serines within the acidic cluster.
Phosphorylation determines whether endocytosed viral gE traffics
to the trans-Golgi network or recycles to the cell membrane.
{ECO:0000305}.
-!- PTM: N-glycosylated, and sulfated. {ECO:0000269|PubMed:6310034}.
-!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E
family. {ECO:0000305}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; X14112; CAA32272.1; -; Genomic_DNA.
EMBL; X02138; CAA26062.1; -; Genomic_DNA.
EMBL; L00036; AAA96680.1; -; Genomic_DNA.
EMBL; DQ889502; ABI63526.1; -; Genomic_DNA.
EMBL; FJ593289; ACM62297.1; -; Genomic_DNA.
PIR; A03733; VGBE18.
RefSeq; YP_009137143.1; NC_001806.2.
PDB; 2GIY; X-ray; 1.78 A; A/B=213-390.
PDB; 2GJ7; X-ray; 5.00 A; E/F=21-419.
PDBsum; 2GIY; -.
PDBsum; 2GJ7; -.
SMR; P04488; -.
DIP; DIP-29186N; -.
IntAct; P04488; 1.
ChEMBL; CHEMBL2364696; -.
iPTMnet; P04488; -.
PRIDE; P04488; -.
GeneID; 2703448; -.
KEGG; vg:2703448; -.
OrthoDB; VOG0900004S; -.
EvolutionaryTrace; P04488; -.
PRO; PR:P04488; -.
Proteomes; UP000009294; Genome.
Proteomes; UP000180652; Genome.
GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0044156; C:host cell junction; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR003404; Herpes_glycopE.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF02480; Herpes_gE; 1.
SUPFAM; SSF48726; SSF48726; 2.
1: Evidence at protein level;
3D-structure; Complete proteome; Disulfide bond; Glycoprotein;
Host cell junction; Host cell membrane; Host endosome;
Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
Phosphoprotein; Reference proteome; Signal; Sulfation; Transmembrane;
Transmembrane helix; Viral envelope protein; Viral immunoevasion;
Virion.
SIGNAL 1 20 {ECO:0000255}.
CHAIN 21 550 Envelope glycoprotein E.
/FTId=PRO_0000038225.
TOPO_DOM 21 419 Virion surface. {ECO:0000255}.
TRANSMEM 420 440 Helical. {ECO:0000255}.
TOPO_DOM 441 550 Intravirion. {ECO:0000255}.
REGION 63 88 Interaction with gI. {ECO:0000250}.
REGION 235 380 Fc-binding.
REGION 470 495 Interaction with VP22 and UL11.
{ECO:0000269|PubMed:17035313}.
REGION 476 484 Acidic.
MOTIF 463 466 Internalization motif. {ECO:0000255}.
MOTIF 472 475 Internalization motif. {ECO:0000255}.
COMPBIAS 163 214 Pro-rich.
MOD_RES 176 176 Sulfotyrosine; by host. {ECO:0000255}.
MOD_RES 476 476 Phosphoserine; by host CK2.
{ECO:0000305|PubMed:10725429}.
MOD_RES 477 477 Phosphoserine; by host CK2.
{ECO:0000305|PubMed:10725429}.
MOD_RES 503 503 Phosphoserine. {ECO:0000305}.
CARBOHYD 124 124 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 243 243 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 271 297 {ECO:0000269|PubMed:16646632}.
DISULFID 280 289 {ECO:0000269|PubMed:16646632}.
DISULFID 314 323 {ECO:0000269|PubMed:16646632}.
VARIANT 120 120 A -> T (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 130 130 H -> Y (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 143 143 S -> F (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 239 239 T -> A (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 257 257 S -> A (in strain: Nonneuroinvasive
mutant HF10).
VARIANT 432 432 A -> V (in strain: Nonneuroinvasive
mutant HF10).
STRAND 221 227 {ECO:0000244|PDB:2GIY}.
STRAND 230 233 {ECO:0000244|PDB:2GIY}.
STRAND 245 253 {ECO:0000244|PDB:2GIY}.
STRAND 256 265 {ECO:0000244|PDB:2GIY}.
STRAND 272 277 {ECO:0000244|PDB:2GIY}.
HELIX 278 282 {ECO:0000244|PDB:2GIY}.
HELIX 287 290 {ECO:0000244|PDB:2GIY}.
HELIX 295 297 {ECO:0000244|PDB:2GIY}.
STRAND 306 315 {ECO:0000244|PDB:2GIY}.
TURN 320 323 {ECO:0000244|PDB:2GIY}.
STRAND 324 329 {ECO:0000244|PDB:2GIY}.
STRAND 345 348 {ECO:0000244|PDB:2GIY}.
HELIX 351 353 {ECO:0000244|PDB:2GIY}.
STRAND 355 363 {ECO:0000244|PDB:2GIY}.
STRAND 366 376 {ECO:0000244|PDB:2GIY}.
TURN 378 380 {ECO:0000244|PDB:2GIY}.
STRAND 383 387 {ECO:0000244|PDB:2GIY}.
SEQUENCE 550 AA; 59094 MW; BE8271E5B7E34776 CRC64;
MDRGAVVGFL LGVCVVSCLA GTPKTSWRRV SVGEDVSLLP APGPTGRGPT QKLLWAVEPL
DGCGPLHPSW VSLMPPKQVP ETVVDAACMR APVPLAMAYA PPAPSATGGL RTDFVWQERA
AVVNRSLVIH GVRETDSGLY TLSVGDIKDP ARQVASVVLV VQPAPVPTPP PTPADYDEDD
NDEGEDESLA GTPASGTPRL PPPPAPPRSW PSAPEVSHVR GVTVRMETPE AILFSPGETF
STNVSIHAIA HDDQTYSMDV VWLRFDVPTS CAEMRIYESC LYHPQLPECL SPADAPCAAS
TWTSRLAVRS YAGCSRTNPP PRCSAEAHME PVPGLAWQAA SVNLEFRDAS PQHSGLYLCV
VYVNDHIHAW GHITISTAAQ YRNAVVEQPL PQRGADLAEP THPHVGAPPH APPTHGALRL
GAVMGAALLL SALGLSVWAC MTCWRRRAWR AVKSRASGKG PTYIRVADSE LYADWSSDSE
GERDQVPWLA PPERPDSPST NGSGFEILSP TAPSVYPRSD GHQSRRQLTT FGSGRPDRRY
SQASDSSVFW


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