GE_BHV1S
ID GE_BHV1S Reviewed; 575 AA.
AC Q08101;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 02-JUN-2021, entry version 71.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE;
OS Bovine herpesvirus 1.2 (strain ST) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=45407;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8122370; DOI=10.1006/viro.1994.1139;
RA Leung-Tack P., Audonnet J.F., Riviere M.;
RT "The complete DNA sequence and the genetic organization of the short unique
RT region (US) of the bovine herpesvirus type 1 (ST strain).";
RL Virology 199:409-421(1994).
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 EMBL; Z23068; CAA80606.1; -; Genomic_DNA.
DR PIR; S35786; S35786.
DR SMR; Q08101; -.
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..26
FT /evidence="ECO:0000255"
FT CHAIN 27..575
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038231"
FT TOPO_DOM 27..423
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 424..444
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 445..575
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 76..101
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 186..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..416
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..502
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 491..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 467..470
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT CARBOHYD 141
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 270..296
FT /evidence="ECO:0000250"
FT DISULFID 279..288
FT /evidence="ECO:0000250"
FT DISULFID 315..327
FT /evidence="ECO:0000250"
SQ SEQUENCE 575 AA; 61168 MW; AF734AA3812E4D09 CRC64;
MQPTAPPRRR LLPLLLPQLL LFGLMAEAEP ATETPGSASV DTVFTARAGA PVFLPGPAAR
PDVRAVRGWS VLAGACSPPV PEPVCLDDRE CFTDVALDAA CLRTARVAPL AIAELAERPD
STGDKEFVLA DPHVSAQLGR NATGVLIAAA AEEDGGVYFL YDRLIGDAGD EETQLALTLQ
VATAGAQGAA RDEEREPATG PTPGPPPHRT TTRAPPRRHG ARFRVLPYHS HVYTPGDSFL
LSVRLQSEFF DEAPFSASID WYFLRTAGDC ALIRIYETCI FHPEAPACLH PADAQCSFAS
PYRSETVYSR LYEQCRPDPA GRWPHECEGA AYAAPVAHLR PANNSVDLVF DDAPAAASGL
YVFVLQYNGH VEAWDYSLVV TSDRLVRAVT DHTRPEAAAA DAPEPGPPLT SEPAGAPTGP
APWLVVLVGA LGLAGLVGIA ALAVRVCARR ASQKRTYDIL NPFGPVYTSL PTNEPLDVVV
PVSDDEFSLD EDSFADDDSD DDGPASNPPA DAYDLAGAPE PTSGFARAPA NGTRSSRSGF
KVWFRDPPED DAAPARAPAA PDYTVVAARL KSILR
