GE_VZVD
ID GE_VZVD Reviewed; 623 AA.
AC P09259;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE; ORFNames=ORF68;
OS Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6321154; DOI=10.1002/j.1460-2075.1983.tb01724.x;
RA Davison A.J.;
RT "DNA sequence of the US component of the varicella-zoster virus genome.";
RL EMBO J. 2:2203-2209(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [3]
RP INTERNALIZATION MOTIF, AND SUBCELLULAR LOCATION.
RX PubMed=9094682; DOI=10.1128/jvi.71.5.4042-4054.1997;
RA Olson J.K., Grose C.;
RT "Endocytosis and recycling of varicella-zoster virus Fc receptor
RT glycoprotein gE: internalization mediated by a YXXL motif in the
RT cytoplasmic tail.";
RL J. Virol. 71:4042-4054(1997).
RN [4]
RP SUBCELLULAR LOCATION.
RC STRAIN=VZV-32;
RX PubMed=15613328; DOI=10.1128/jvi.79.2.997-1007.2005;
RA Maresova L., Pasieka T.J., Homan E., Gerday E., Grose C.;
RT "Incorporation of three endocytosed varicella-zoster virus glycoproteins,
RT gE, gH, and gB, into the virion envelope.";
RL J. Virol. 79:997-1007(2005).
RN [5]
RP INTERACTION WITH HUMAN IDE RECEPTOR AND GLYCOPROTEIN I.
RX PubMed=17553876; DOI=10.1128/jvi.00286-07;
RA Li Q., Krogmann T., Ali M.A., Tang W.-J., Cohen J.I.;
RT "The amino terminus of varicella-zoster virus (VZV) glycoprotein E is
RT required for binding to insulin-degrading enzyme, a VZV receptor.";
RL J. Virol. 81:8525-8532(2007).
CC -!- FUNCTION: Envelope glycoprotein that binds to the potential host cell
CC entry receptor IDE.
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 (By similarity). {ECO:0000250}.
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-VZV 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 (via N-terminus) with host receptor IDE (via N-
CC terminus). Interacts with gI; this interaction enhances the Fc receptor
CC function of gE (By similarity). The heterodimer gE/gI interacts with
CC the Fc part of host IgG. {ECO:0000250, ECO:0000269|PubMed:17553876}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Host cell junction
CC {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250};
CC Single-pass 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), maybe through an interaction
CC with PACS-1 sorting protein. The heterodimer gE/gI then redistributes
CC to cell junctions to promote cell-cell spread later in the infection
CC (By similarity). {ECO:0000250}.
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 -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA25033.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X04370; CAA27951.1; -; Genomic_DNA.
DR EMBL; X00208; CAA25034.1; -; Genomic_DNA.
DR EMBL; X00208; CAA25033.1; ALT_INIT; Genomic_DNA.
DR PIR; G27345; VGBE68.
DR RefSeq; NP_040190.1; NC_001348.1.
DR SMR; P09259; -.
DR PRIDE; P09259; -.
DR DNASU; 1487709; -.
DR GeneID; 1487709; -.
DR KEGG; vg:1487709; -.
DR Proteomes; UP000002602; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
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: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 GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
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 endosome; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Phosphoprotein; Reference proteome; Signal; Sulfation;
KW Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein;
KW Viral immunoevasion; Virion; Virus entry into host cell.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..623
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038233"
FT TOPO_DOM 31..538
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 539..559
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 560..623
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 24..71
FT /note="Interaction with host receptor IDE"
FT REGION 208..236
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 352..499
FT /note="Fc-binding"
FT /evidence="ECO:0000250"
FT REGION 588..601
FT /note="Acidic"
FT MOTIF 582..585
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT MOD_RES 438
FT /note="Sulfotyrosine; by host"
FT /evidence="ECO:0000255"
FT MOD_RES 441
FT /note="Sulfotyrosine; by host"
FT /evidence="ECO:0000255"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 595
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT MOD_RES 596
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT MOD_RES 598
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 266
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 387..413
FT /evidence="ECO:0000250"
FT DISULFID 396..405
FT /evidence="ECO:0000250"
FT DISULFID 432..442
FT /evidence="ECO:0000250"
SQ SEQUENCE 623 AA; 69956 MW; 4C44B4EB65E89A18 CRC64;
MGTVNKPVVG VLMGFGIITG TLRITNPVRA SVLRYDDFHT 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
