GE_GAHVM
ID GE_GAHVM Reviewed; 497 AA.
AC Q77MP7;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 02-JUN-2021, entry version 43.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
GN Name=MDV096;
OS Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS disease herpesvirus type 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX NCBI_TaxID=10389;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT "The genome of a very virulent Marek's disease virus.";
RL J. Virol. 74:7980-7988(2000).
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; AF243438; AAG14270.1; -; Genomic_DNA.
DR RefSeq; YP_001034013.1; NC_002229.3.
DR SMR; Q77MP7; -.
DR GeneID; 4811455; -.
DR KEGG; vg:4811455; -.
DR Proteomes; UP000008072; 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 Glycoprotein; Host cell junction; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT CHAIN 1..497
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000406532"
FT TOPO_DOM 1..398
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 420..497
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 133
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 203
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 277
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 366
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 497 AA; 55676 MW; 5C853014DF2772A2 CRC64;
MCVFQILIIV TTIKVAGTAN INHIDVPAGH SATTTIPRYP PVVDGTLYTE TWTWIPNHCN
ETATGYVCLE SAHCFTDLIL GVSCMRYADE IVLRTDKFIV DAGSIKQIES LSLNGVPNIF
LSTKASNKLE ILNASLQNAG IYIRYSRNGT RTAKLDVVVV GVLGQARDRL PQMSSPMISS
HADIKLSLKN FKALVYHVGD TINVSTAVIL GPSPEIFTLE FRVLFLRYNP TCKFVTIYEP
CIFHPKEPEC ITTAEQSVCH FASNIDILQI AAARSENCST GYRRCIYDTA IDESVQARLT
FIEPGIPSFK MKDVQVDDAG LYVVVALYNG RPSAWTYIYL STVETYLNVY ENYHKPGFGY
KSFLQNSSIV DENEASDWSS SSIKRRNNGT IIYDILLTSL SIGAIIIVIV GGVCIAILIR
RRRRRRTRGL FDEYPKYMTL PGNDLGGMNV PYDNTCSGNQ VEYYQEKSAK MKRMGSGYTA
WLKNDMPKIR KRLDLYH
