GE_SUHVR
ID GE_SUHVR Reviewed; 577 AA.
AC P08354;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 02-JUN-2021, entry version 72.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE;
OS Suid herpesvirus 1 (strain Rice) (SuHV-1) (Pseudorabies virus (strain
OS Rice)).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10350;
OH NCBI_TaxID=9823; Sus scrofa (Pig).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3018284; DOI=10.1128/jvi.60.1.185-193.1986;
RA Petrovskis E.A., Timmins J.G., Post L.E.;
RT "Use of lambda gt11 to isolate genes for two pseudorabies virus
RT glycoproteins with homology to herpes simplex virus and varicella-zoster
RT virus glycoproteins.";
RL J. Virol. 60:185-193(1986).
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 within the acidic cluster. Phosphorylation
CC determines whether endocytosed viral gE traffics to the trans-Golgi
CC 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 EMBL; M14336; AAC35205.1; -; Genomic_DNA.
DR PIR; B29012; VGBEGI.
DR SMR; P08354; -.
DR PRIDE; P08354; -.
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..20
FT /evidence="ECO:0000255"
FT CHAIN 21..577
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038234"
FT TOPO_DOM 21..428
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..577
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 117..141
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 481..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..496
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT MOTIF 478..481
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 185
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 258
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 343
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 274..300
FT /evidence="ECO:0000250"
FT DISULFID 283..292
FT /evidence="ECO:0000250"
FT DISULFID 319..331
FT /evidence="ECO:0000250"
SQ SEQUENCE 577 AA; 62326 MW; AD91F9CCBB0EDA69 CRC64;
MRPFLLRAAQ LLALLALALS TEAPSLSAET TPGPVTEVPS PSAEVWDLST EAGDDDLDGD
LNGDDRRAGF GSALASLREA PPAHLVNVSE GANFTLDARG DGAVVAGIWT FLPVRGCDAV
AVTMVCFETA CHPDLVLGRA CVPEAPERGI GDYLPPEVPR LQREPPIVTP ERWSPHLTVR
RATPNDTGLY TLHDASGPRA VFFVAVGDRP PAPLAPVGPA RHEPRFHALG FHSQLFSPGD
TFDLMPRVVS DMGDSRENFT ATLDWYYARA PPRCLLYYVY EPCIYHPRAP ECLRPVDPAC
SFTSPARAAL VARRAYASCS PLLGDRWLTA CPFDAFGEEV HTNATADESG LYVLVMTHNG
HVATWDYTLV ATAAEYVTVI KELTAPARAP GTPWGPGGGD DAIYVDGVTT PAPPARPWNP
YGRTTPGRLF VLALGSFVMT CVVGGAVWLC VLCSRRRAAS RPFRVPTRAG TRMLSPVYTS
LPTHEDYYDG DDDDEEAGDA RRRPSSPGGD SGYEGPYVSL DAEDEFSSDE DDGLYVRPEE
APRSGFDVWF RDPEKPEVTN GPNYGVTASR LLNARPA
