GE_CHV1
ID GE_CHV1 Reviewed; 539 AA.
AC P30816; Q8V722;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 2.
DT 02-JUN-2021, entry version 71.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE; ORFNames=US8;
OS Cercopithecine herpesvirus 1 (CeHV-1) (Simian herpes B virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10325;
OH NCBI_TaxID=9606; Homo sapiens (Human).
OH NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH NCBI_TaxID=90387; Macaca leonina (Northern pig-tailed macaque) (Macaca nemestrina leonina).
OH NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH NCBI_TaxID=9545; Macaca nemestrina (Pig-tailed macaque).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=E2490;
RX PubMed=11773425; DOI=10.1128/jvi.76.3.1516-1520.2002;
RA Ohsawa K., Black D.H., Sato H., Eberle R.;
RT "Sequence and genetic arrangement of the U(S) region of the monkey B virus
RT (cercopithecine herpesvirus 1) genome and comparison with the U(S) regions
RT of other primate herpesviruses.";
RL J. Virol. 76:1516-1520(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2490;
RX PubMed=12743273; DOI=10.1128/jvi.77.11.6167-6177.2003;
RA Perelygina L., Zhu L., Zurkuhlen H., Mills R., Borodovsky M.,
RA Hilliard J.K.;
RT "Complete sequence and comparative analysis of the genome of herpes B virus
RT (Cercopithecine herpesvirus 1) from a rhesus monkey.";
RL J. Virol. 77:6167-6177(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 467-539.
RX PubMed=1309859; DOI=10.1099/0022-1317-73-1-195;
RA Killeen A.M., Harrington L., Wall L.V.M., Kelly D.C.;
RT "Nucleotide sequence analysis of a homologue of herpes simplex virus type 1
RT gene US9 found in the genome of simian herpes B virus.";
RL J. Gen. Virol. 73:195-199(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; AB074432; BAB83755.1; -; Genomic_DNA.
DR EMBL; AF533768; AAP41485.1; -; Genomic_DNA.
DR EMBL; S75996; AAB21001.1; ALT_SEQ; Genomic_DNA.
DR PIR; PQ0277; PQ0277.
DR RefSeq; NP_851927.1; NC_004812.1.
DR SMR; P30816; -.
DR GeneID; 1487461; -.
DR KEGG; vg:1487461; -.
DR Proteomes; UP000110594; 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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..539
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000115765"
FT TOPO_DOM 25..410
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 432..539
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 66..91
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 168..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..497
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..480
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT REGION 517..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 452..455
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT COMPBIAS 381..400
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 262..288
FT /evidence="ECO:0000250"
FT DISULFID 271..280
FT /evidence="ECO:0000250"
FT DISULFID 305..314
FT /evidence="ECO:0000250"
SQ SEQUENCE 539 AA; 57992 MW; C9134146FDE33C65 CRC64;
MRPPVRASLG LLVAWAIGAC VCAAAIETTW KHASAGDEVR LFALPAARPG APPAKVVWEL
DPMAACGSLR PSWVSLRPPG QVLDTVVDAE CVSEPVLLAA WYERRDGGSE VPAPFWGPDG
APPQRGNVTN GTLVLREARV GDSGMHVLSV FHPPNATAAR HVVFLKVAPR RPEPAGGTPP
PRDDEEGGTE EPATPAPPPH PHPIAEVAHV RGVTVSLRTQ TAILFAPGDT VHTDVSVMPI
AHDDDPYVME VVWVRFDVPE ECGEMRIYEP CLYHPQLPEC RSPADAPCAA SVWTERLAVR
RYGPCSRGVP PPRCPSDAAM ESRAGLGWYG HTVNLQLRDA SEASGGLYVC VVYVNGHVHA
WGHVVISTAS RYRNAVVERS PPRYRPPPVE PTPSAQPTGP RPAAPRAARL VGVLGAAVGL
AVAGLSVWAC VTCRRARAWR AVKRRDLMAP TYIRLADDEL YGDLSSYGDS DDSEYDSDSD
RLPGTDPAPK RGSGFQILSG AKADPWSAGA RQHGHLITFR ADDTSRYRDP SSPDPPHRR
