ID   GE_EHV4                 Reviewed;         255 AA.
AC   P18345;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   23-FEB-2022, entry version 70.
DE   RecName: Full=Envelope glycoprotein E;
DE            Short=gE;
DE   Flags: Fragment;
GN   Name=gE;
OS   Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10333;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839595; DOI=10.1099/0022-1317-69-7-1575;
RA   Cullinane A.A., Rixon F.J., Davison A.J.;
RT   "Characterization of the genome of equine herpesvirus 1 subtype 2.";
RL   J. Gen. Virol. 69:1575-1590(1988).
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   -!- SUBUNIT: Interacts with gI. {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   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC       {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D00318; BAA00218.1; -; Genomic_DNA.
DR   SMR; P18345; -.
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   Glycoprotein; Host cell junction; Host cell membrane; Host endosome;
KW   Host Golgi apparatus; Host membrane; Membrane; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   CHAIN           <1..255
FT                   /note="Envelope glycoprotein E"
FT                   /id="PRO_0000115766"
FT   TOPO_DOM        <1..110
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        111..131
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        132..255
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          173..187
FT                   /note="Acidic"
FT                   /evidence="ECO:0000250"
FT   REGION          176..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          223..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           154..157
FT                   /note="Internalization motif"
FT                   /evidence="ECO:0000255"
FT   NON_TER         1
SQ   SEQUENCE   255 AA;  28680 MW;  06D7E643A54A330A CRC64;
     GSTWPSRCHS TLLGDRPHFI QPAPNRVDLL FKDIPESATG LYVFVLLYNG HPEAWTYTLL
     STANHFMNVL TDRTRPRLGE HFYTDHGHQL FTPHPSEATT QELGAWTRHY LAFLLIIICT
     CAALLIALVV WGCILYIRSN RKPYEVLNPF ETVYTSVPSN DPTDEVLVFE RLASDSDDSF
     DSSSDEELEL PQPPPAAQLQ PYSSLESADA SRGRSGFKVW FRDTPEASPE PLHRPTPPVG
     PDYSKVASKL RSILK