GE_HHV2H
ID GE_HHV2H Reviewed; 545 AA.
AC P89475; P13289;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE AltName: Full=gE-2;
DE Flags: Precursor;
GN Name=gE; ORFNames=US8;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-274.
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).
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-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: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 -!- 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; Z86099; CAB06715.1; -; Genomic_DNA.
DR EMBL; X04798; CAA28486.1; -; Genomic_DNA.
DR PIR; G43674; G43674.
DR SMR; P89475; -.
DR PRIDE; P89475; -.
DR Proteomes; UP000001874; 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 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 3: Inferred from homology;
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 envelope protein;
KW Viral immunoevasion; Virion.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..545
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000385498"
FT TOPO_DOM 21..414
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 415..435
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 436..545
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 61..86
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 162..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..375
FT /note="Fc-binding"
FT /evidence="ECO:0000250"
FT REGION 386..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 465..490
FT /note="Interaction with VP22 and UL11"
FT /evidence="ECO:0000250"
FT REGION 470..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..479
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT MOTIF 458..461
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT MOTIF 467..470
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 187..205
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..485
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..503
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..545
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 172
FT /note="Sulfotyrosine; by host"
FT /evidence="ECO:0000250"
FT MOD_RES 471
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 472
FT /note="Phosphoserine; by host CK2"
FT /evidence="ECO:0000250"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 266..292
FT /evidence="ECO:0000250"
FT DISULFID 275..284
FT /evidence="ECO:0000250"
FT DISULFID 309..318
FT /evidence="ECO:0000250"
SQ SEQUENCE 545 AA; 59309 MW; 4A18C3F855501E1E CRC64;
MARGAGLVFF VGVWVVSCLA AAPRTSWKRV TSGEDVVLLP APAERTRAHK LLWAAEPLDA
CGPLRPSWVA LWPPRRVLET VVDAACMRAP EPLAIAYSPP FPAGDEGLYS ELAWRDRVAV
VNESLVIYGA LETDSGLYTL SVVGLSDEAR QVASVVLVVE PAPVPTPTPD DYDEEDDAGV
TNARRSAFPP QPPPRRPPVA PPTHPRVIPE VSHVRGVTVH METLEAILFA PGETFGTNVS
IHAIAHDDGP YAMDVVWMRF DVPSSCADMR IYEACLYHPQ LPECLSPADA PCAVSSWAYR
LAVRSYAGCS RTTPPPRCFA EARMEPVPGL AWLASTVNLE FQHASPQHAG LYLCVVYVDD
HIHAWGHMTI STAAQYRNAV VEQHLPQRQP EPVEPTRPHV RAPHPAPSAR GPLRLGAVLG
AALLLAALGL SAWACMTCWR RRSWRAVKSR ASATGPTYIR VADSELYADW SSDSEGERDG
SLWQDPPERP DSPSTNGSGF EILSPTAPSV YPHSEGRKSR RPLTTFGSGS PGRRHSQASY
PSVLW
