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Envelope glycoprotein E (gE)

 GE_VZVO                 Reviewed;         623 AA.
Q9J3M8;
22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
28-FEB-2018, entry version 68.
RecName: Full=Envelope glycoprotein E;
Short=gE;
Flags: Precursor;
Name=gE; ORFNames=ORF68;
Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus
3).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Alphaherpesvirinae; Varicellovirus.
NCBI_TaxID=341980;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=V-Oka(Biken);
PubMed=10720545; DOI=10.1086/315335;
Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
Krause P.R.;
"Nucleotide sequences that distinguish Oka vaccine from parental Oka
and other varicella-zoster virus isolates.";
J. Infect. Dis. 181:1153-1157(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
PubMed=11162813; DOI=10.1006/viro.2000.0775;
Faga B., Maury W., Bruckner D.A., Grose C.;
"Identification and mapping of single nucleotide polymorphisms in the
varicella-zoster virus genome.";
Virology 280:1-6(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Isolate Human/Japan/P-Oka/1970, and
Oka varicella vaccine Biken (V-Oka-Biken);
PubMed=12388706; DOI=10.1128/JVI.76.22.11447-11459.2002;
Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M.,
Yamanishi K.;
"Comparison of the complete DNA sequences of the Oka varicella vaccine
and its parental virus.";
J. Virol. 76:11447-11459(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
Oka varicella vaccine Varivax (V-Oka-Merk);
PubMed=18787000; DOI=10.1128/JVI.00777-08;
Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
Vassilev V.;
"Complete DNA sequences of two oka strain varicella-zoster virus
genomes.";
J. Virol. 82:11023-11044(2008).
[5]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-593; SER-595; THR-596 AND
THR-598, AND MUTAGENESIS OF 593-SER--THR-598.
STRAIN=R-Oka;
PubMed=12368341; DOI=10.1128/JVI.76.21.10980-10993.2002;
Kenyon T.K., Cohen J.I., Grose C.;
"Phosphorylation by the varicella-zoster virus ORF47 protein serine
kinase determines whether endocytosed viral gE traffics to the trans-
Golgi network or recycles to the cell membrane.";
J. Virol. 76:10980-10993(2002).
[6]
INTERACTION WITH HUMAN IDE RECEPTOR.
STRAIN=R-Oka;
PubMed=17055432; DOI=10.1016/j.cell.2006.08.046;
Li Q., Ali M.A., Cohen J.I.;
"Insulin degrading enzyme is a cellular receptor mediating varicella-
zoster virus infection and cell-to-cell spread.";
Cell 127:305-316(2006).
[7]
INTERACTION WITH VP22.
STRAIN=Isolate Human/Japan/P-Oka/1970;
PubMed=18400847; DOI=10.1128/JVI.00303-08;
Che X., Reichelt M., Sommer M.H., Rajamani J., Zerboni L., Arvin A.M.;
"Functions of the ORF9-to-ORF12 gene cluster in varicella-zoster virus
replication and in the pathogenesis of skin infection.";
J. Virol. 82:5825-5834(2008).
[8]
INTERACTION WITH HUMAN IDE RECEPTOR AND GLYCOPROTEIN I.
STRAIN=Isolate Human/Japan/P-Oka/1970;
PubMed=18945783; DOI=10.1128/JVI.00913-08;
Berarducci B., Rajamani J., Reichelt M., Sommer M.H., Zerboni L.,
Arvin A.M.;
"Deletion of the first cysteine-rich region of the varicella-zoster
virus glycoprotein E ectodomain abolishes the gE and gI interaction
and differentially affects cell-cell spread and viral entry.";
J. Virol. 83:228-240(2009).
-!- FUNCTION: Envelope glycoprotein that binds to the potential host
cell entry receptor IDE.
-!- 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. 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 (By similarity). {ECO:0000250}.
-!- 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-VZV antibodies bipolar bridging,
followed by intracellular endocytosis and degradation, thereby
interfering with host IgG-mediated immune responses (By
similarity). {ECO:0000250}.
-!- SUBUNIT: Interacts (via N-terminus) with host receptor IDE (via N-
terminus). 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 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
Q77NN4:gI; NbExp=3; IntAct=EBI-2532305, EBI-2533019;
P14735-1:IDE (xeno); NbExp=2; IntAct=EBI-2532305, EBI-15607031;
-!- 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 {ECO:0000250}. 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
(By similarity). {ECO:0000250}.
-!- 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}.
-!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E
family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF206304; AAF61669.1; -; Genomic_DNA.
EMBL; AY016450; AAK19946.1; -; Genomic_DNA.
EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; DQ008354; AAY57677.1; -; Genomic_DNA.
EMBL; DQ008355; AAY57748.1; -; Genomic_DNA.
SMR; Q9J3M8; -.
DIP; DIP-56349N; -.
ELM; Q9J3M8; -.
IntAct; Q9J3M8; 19.
OrthoDB; VOG0900004S; -.
Proteomes; UP000002603; Genome.
Proteomes; UP000008504; Genome.
Proteomes; UP000008505; Genome.
Proteomes; UP000008506; 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:0019899; F:enzyme binding; IPI:UniProtKB.
GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; 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; 1.
1: Evidence at protein level;
Complete proteome; Disulfide bond; Glycoprotein; Host cell junction;
Host cell membrane; Host endosome; Host Golgi apparatus;
Host membrane; Host-virus interaction; Membrane; Phosphoprotein;
Signal; Sulfation; Transmembrane; Transmembrane helix;
Viral attachment to host cell;
Viral attachment to host entry receptor; Viral envelope protein;
Viral immunoevasion; Virion; Virus entry into host cell.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 623 Envelope glycoprotein E.
/FTId=PRO_0000385499.
TOPO_DOM 31 538 Virion surface. {ECO:0000255}.
TRANSMEM 539 559 Helical. {ECO:0000255}.
TOPO_DOM 560 623 Intravirion. {ECO:0000255}.
REGION 208 236 Interaction with gI.
REGION 352 499 Fc-binding. {ECO:0000250}.
REGION 588 601 Acidic.
MOTIF 582 585 Internalization motif. {ECO:0000255}.
MOD_RES 438 438 Sulfotyrosine; by host. {ECO:0000255}.
MOD_RES 441 441 Sulfotyrosine; by host. {ECO:0000255}.
MOD_RES 593 593 Phosphoserine. {ECO:0000250}.
MOD_RES 595 595 Phosphoserine. {ECO:0000250}.
MOD_RES 596 596 Phosphothreonine. {ECO:0000250}.
MOD_RES 598 598 Phosphothreonine. {ECO:0000250}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
CARBOHYD 437 437 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
DISULFID 387 413 {ECO:0000250}.
DISULFID 396 405 {ECO:0000250}.
DISULFID 432 442 {ECO:0000250}.
MUTAGEN 593 598 SESTDT->AESADA: Complete loss of
phosphorylation by ORF47 kinase.
{ECO:0000269|PubMed:12368341}.
SEQUENCE 623 AA; 69968 MW; CFC5EF31E4B7D31F CRC64;
MGTVNKPVVG VLMGFGIITG TLRITNPVRA SVLRYDDFHI DEDKLDTNSV YEPYYHSDHA
ESSWVNRGES SRKAYDHNSP YIWPRNDYDG FLENAHEHHG VYNQGRGIDS GERLMQPTQM
SAQEDLGDDT GIHVIPTLNG DDRHKIVNVD QRQYGDVFKG DLNPKPQGQR LIEVSVEENH
PFTLRAPIQR IYGVRYTETW SFLPSLTCTG DAAPAIQHIC LKHTTCFQDV VVDVDCAENT
KEDQLAEISY RFQGKKEADQ PWIVVNTSTL FDELELDPPE IEPGVLKVLR TEKQYLGVYI
WNMRGSDGTS TYATFLVTWK GDEKTRNPTP AVTPQPRGAE FHMWNYHSHV FSVGDTFSLA
MHLQYKIHEA PFDLLLEWLY VPIDPTCQPM RLYSTCLYHP NAPQCLSHMN SGCTFTSPHL
AQRVASTVYQ NCEHADNYTA YCLGISHMEP SFGLILHDGG TTLKFVDTPE SLSGLYVFVV
YFNGHVEAVA YTVVSTVDHF VNAIEERGFP PTAGQPPATT KPKEITPVNP GTSPLLRYAA
WTGGLAAVVL LCLVIFLICT AKRMRVKAYR VDKSPYNQSM YYAGLPVDDF EDSESTDTEE
EFGNAIGGSH GGSSYTVYID KTR


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