ID G9IXZ6_HHV3 Unreviewed; 623 AA.
AC G9IXZ6;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Envelope glycoprotein E {ECO:0000256|ARBA:ARBA00013988};
GN ORFNames=HHV3gp69 {ECO:0000313|EMBL:AEW89412.1};
OS Human herpesvirus 3 (HHV-3) (Varicella-zoster virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus humanalpha3.
OX NCBI_TaxID=10335 {ECO:0000313|EMBL:AEW89412.1, ECO:0000313|Proteomes:UP000118042};
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1] {ECO:0000313|EMBL:AEW89412.1, ECO:0000313|Proteomes:UP000118042}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VZVi/Jena.GER/37.05/V[VIII] {ECO:0000313|EMBL:AEW89412.1};
RX PubMed=22130537; DOI=10.1128/JVI.06233-11;
RA Zell R., Taudien S., Pfaff F., Wutzler P., Platzer M., Sauerbrei A.;
RT "Sequencing of 21 varicella-zoster virus genomes reveals two novel
RT genotypes and evidence of recombination.";
RL J. Virol. 86:1608-1622(2012).
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.
CC {ECO:0000256|ARBA:ARBA00025134}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
CC Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I
CC membrane protein {ECO:0000256|ARBA:ARBA00004251}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004190}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004190}. Host Golgi apparatus membrane
CC {ECO:0000256|ARBA:ARBA00004152}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004152}. Host cell junction
CC {ECO:0000256|ARBA:ARBA00004315}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402}. Host endosome membrane
CC {ECO:0000256|ARBA:ARBA00004235}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004235}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Membrane
CC {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004479}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004563}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004563}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000256|ARBA:ARBA00008101}.
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DR EMBL; JN704709; AEW89412.1; -; Genomic_DNA.
DR Proteomes; UP000118042; Genome.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-SubCell.
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:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; Immunoglobulins; 1.
DR InterPro; IPR046463; Herpes_gE_N.
DR InterPro; IPR003404; Herpes_glycopE_Fc.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF02480; Herpes_gE; 1.
DR Pfam; PF20418; Herpes_gE_N; 1.
DR SUPFAM; SSF48726; Immunoglobulin; 1.
PE 3: Inferred from homology;
KW Host cell junction {ECO:0000256|ARBA:ARBA00023081};
KW Host cell membrane {ECO:0000256|ARBA:ARBA00022511};
KW Host endosome {ECO:0000256|ARBA:ARBA00023046};
KW Host Golgi apparatus {ECO:0000256|ARBA:ARBA00022812};
KW Host membrane {ECO:0000256|ARBA:ARBA00022870};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius};
KW Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 538..560
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..321
FT /note="Envelope glycoprotein E N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20418"
FT DOMAIN 337..511
FT /note="Envelope glycoprotein E Fc-binding"
FT /evidence="ECO:0000259|Pfam:PF02480"
SQ SEQUENCE 623 AA; 70011 MW; C7301A791146A4B3 CRC64;
MGTVNKPVVG VLMGFGIITG TLRITNPVRA SVLRYDDFHI DEDKLDTNSV YEPYYHSDHA
ESSWVNRGES SRKAYDHNSP YIWPRNDYDG FLENAHEHHG VYNQGRGIDS GERLMQPTQM
SAQEDLGDDT GIHVIPTLNG DDRHKIVNVD QRQYGDVFKG DRNPKPQGQR LIEVSVEENH
PFTLRAPIQR IYGVRYTETW SFLPSLTCTG DAAPAIQHIC LKHTTCFQDV VVDVDCAENT
KEDQLAEISY RFQGKKEADQ PWIVVNTSTL FDELELDPPE IEPGVLKVLR TEKQYLGVYI
WNMRGSDGTS TYATFLVTWK GDEKTRNPTP AVTPQPRGAE FHMWNYHSHV FSVGDTFSLA
MHLQYKIHEA PFDLLLEWLY VPIDPTCQPM RLYSTCLYHP NAPQCLSHMN SGCTFTSPHL
AQRVASTVYQ NCEHADNYTA YCLGISHMEP SFGLILHDGG TTLKFVDTPE SLSGLYVFVV
YFNGHVEAVA YTVVSTVDHF VNAIEERGFP PTAGQPPATT KPKEITPVNP GTSPLLRYAA
WTGGLAAVVL LCLVIFLICT AKRMRVKAYR VDKSPYNQSM YYAGLPVDDF EDSESTDTEE
EFGNAIGGSH GGSSYTVYID KTR
//
