GE_EHV1D
ID GE_EHV1D Reviewed; 552 AA.
AC P24380;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 02-JUN-2021, entry version 78.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE;
OS Equine herpesvirus 1 (strain Kentucky D) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10330;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2177089; DOI=10.1099/0022-1317-71-12-2969;
RA Audonnet J.-C., Winslow J., Allen G., Paoletti E.;
RT "Equine herpesvirus type 1 unique short fragment encodes glycoproteins with
RT homology to herpes simplex virus type 1 gD, gI and gE.";
RL J. Gen. Virol. 71:2969-2978(1990).
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}.
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DR PIR; D36646; VGBEKD.
DR SMR; P24380; -.
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; Membrane; Signal;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..552
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038230"
FT TOPO_DOM 24..410
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..427
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 428..552
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 65..91
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 470..478
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 473..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 451..454
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT CARBOHYD 47
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 109
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 243
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 293
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 249..275
FT /evidence="ECO:0000250"
FT DISULFID 258..267
FT /evidence="ECO:0000250"
FT DISULFID 294..305
FT /evidence="ECO:0000250"
SQ SEQUENCE 552 AA; 61493 MW; 2CD6EFB9927F7382 CRC64;
MELLAASRAC IFFGLVTVLD AWGVQQVELS EGAWAMIDGR DVLTPTNTTT RVTKAWTFLE
TPPGCAGDIS VKKVCVSHSL CEDNIIIGKH CNLLTGEHGI ALAEFNVVNG SLRRTDDVYF
VNGTVFPILA ETRSVLQIHR ATPSIAGVYT LHVSIDGMMK HSVVLLTVKK PPKQPQPQPR
LRVKTPPPVT VPQVPVKTHT DFVVHGYHSR VYRDGESFEL SVNLESHIVE PSFSAEIQWY
YMNTSSSSCD LFRVFETCIF HPTAMACLHP EQHTCSFTSP IRATKILHRV YGNCSDHGNS
WPSRCHSTLL GNRLYFIQPA QNRVDLLFKD TPASATGLYV FVLLYNGHPE AWTYTLLSTA
NHFMNVLTDV TRPRLGEHFY TDLGHKIITP HPSVATTEEL GAWTRHYLAF LLVIICTCAA
LLVALVVWGC ILYIRSNRKP YEVLNPFETV YTSVPSNDPS DEVLVFERLA SDSDDSFDSD
SDEELEYPPP PKPAPQLPPY QFVDGGDAPS GRSGFKVWFR DTPEASPVPL HKPTLQGPDY
SRVASKLKSI LK
