GE_CHV9D
ID GE_CHV9D Reviewed; 604 AA.
AC Q04548;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 12-AUG-2020, entry version 71.
DE RecName: Full=Envelope glycoprotein E;
DE AltName: Full=Membrane glycoprotein 2;
DE Short=gE;
DE Flags: Precursor;
GN Name=gE; ORFNames=ORF68;
OS Cercopithecine herpesvirus 9 (strain DHV) (CeHV-9) (Simian varicella
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=36348;
OH NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8384754; DOI=10.1006/viro.1993.1185;
RA Fletcher T.M. III, Gray W.L.;
RT "DNA sequence and genetic organization of the unique short (US) region of
RT the simian varicella virus genome.";
RL Virology 193:762-773(1993).
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 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000305}.
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DR EMBL; L07067; AAA47889.1; -; Genomic_DNA.
DR PIR; D46113; D46113.
DR RefSeq; NP_077482.1; NC_002686.2.
DR SMR; Q04548; -.
DR GeneID; 920503; -.
DR KEGG; vg:920503; -.
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..24
FT /evidence="ECO:0000255"
FT CHAIN 25..604
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000038232"
FT TOPO_DOM 25..526
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..544
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 545..604
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 192..219
FT /note="Interaction with gI"
FT /evidence="ECO:0000250"
FT REGION 574..586
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT MOTIF 568..571
FT /note="Internalization motif"
FT /evidence="ECO:0000255"
FT CARBOHYD 117
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 303
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 419
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 370..396
FT /evidence="ECO:0000250"
FT DISULFID 379..388
FT /evidence="ECO:0000250"
FT DISULFID 415..424
FT /evidence="ECO:0000250"
SQ SEQUENCE 604 AA; 67583 MW; 396192E07F2F0C1F CRC64;
MRMTVVKHVM LTLICGTLSW GVQINTLAYA SAIKSEDGFD MDEDGVYGDD IQDYINAAYT
HERPFIQDKS KHKMETYTQS LLHTDLETDS QISRERGNYI NAQELGDGNN EHVDLVNRTM
TKNVLMKHGH RNFMDASILY KSVHGITHLH AHQRPTEVSV AENQQLLLKV HIPQENEHTY
TERWSFLPAA PCKLTPPSIQ QVCIKHGACI HDVVVDVDCI AESMEHTLVE IGYVVHASKA
VHPTWTVVNI TEDFANYGFD TPDVKPGVLK FEHMNAHHAG VYIWNLQGTH GENMYVTFLV
KLNNSIENHI DLPAVTPKPK GAEFHTWHYH SHVFSVGETF SLPMHLQYKI HDTPFDLLLE
WLYVPINPTC QPMRLYSACV YHETVPSCLS PENPECTFAS PHIARRVANT VYQNCEHVNY
TADCLAVSHV EPGSGLEIQN GGSALLFVNA AESMSGLYVF IIHFNGHVET VAYTVVSTIE
NFVNAIEEHG FPPEIHNVPS PSSPNVTANN DVISETNTFP FKTYAGITGG FAVLALVCLA
LALVCTKRKF GHRSYWSDKA AYGQSTYYAG VPVDDFEDDT EVEVDEGAEC GGSGYTVYID
KRTR
