GE_EHV1B
ID GE_EHV1B Reviewed; 550 AA.
AC Q6S6V7; P18552;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 02-JUN-2021, entry version 84.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE; OrderedLocusNames=74;
OS Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=31520;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT "The DNA sequence of equine herpesvirus-1.";
RL Virology 189:304-316(1992).
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; AY665713; AAT67331.1; -; Genomic_DNA.
DR PIR; B36803; VGBEG5.
DR RefSeq; YP_053118.1; NC_001491.2.
DR SMR; Q6S6V7; -.
DR PRIDE; Q6S6V7; -.
DR GeneID; 2948576; -.
DR KEGG; vg:2948576; -.
DR Proteomes; UP000001189; 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; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Virion.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..550
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038229"
FT TOPO_DOM 24..408
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 409..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 426..550
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 65..91
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 468..482
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 471..513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 449..452
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 241
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 247..273
FT /evidence="ECO:0000250"
FT DISULFID 256..265
FT /evidence="ECO:0000250"
FT DISULFID 292..303
FT /evidence="ECO:0000250"
SQ SEQUENCE 550 AA; 61183 MW; 2114D833555EE2BD CRC64;
MELLAASRAC IFFGLVTVLD AWGVQQVELS EGAWAMIDGR DVLTPTNTTT RVTKAWTFLE
TPPGCAGDIS VKKVCVSHSL CEDNIIIGKH CNLLTGEHGI ALAEFNVVNG SLRRTDDVYF
VNGTVFPILA ETRSVLQIHR ATPSIAGVYT LHVSIDGMMK HSVVLLTVKK PPKQPQPRLR
VKTPPPVTVP QVPVKTHTDF VVHGYHSRVY ADGESFELSV NLESHIVEPS FSAEIQWYYM
NTSSSSCDLF RVFETCIFHP TAMACLHPEQ HTCSFTSPIR ATKILHRVYG NCSDHGNSWP
SRCHSTLLGN RLYFIQPAQN RVDLLFKDTP ASATGLYVFV LLYNGHPEAW TYTLLSTANH
FMNVLTDVTR PRLGEHFYTD LGHKIITPHP SVATTEELGA WTRHYLAFLL VIICTCAALL
VALVVWGCIL YIRSNRKPYE VLNPFETVYT SVPSNDPSDE VLVFERLASD SDDSFDSDSD
EELEYPPPPK PAPQLPPYQF VDGGDAPSGR SGFKVWFRDT PEASPVPLHK PTLQGPDYSR
VASKLKSILK
