ID Q9IKB9_9ALPH Unreviewed; 598 AA.
AC Q9IKB9;
DT 01-OCT-2000, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2000, sequence version 1.
DT 24-JAN-2024, entry version 52.
DE RecName: Full=Envelope glycoprotein E {ECO:0000256|ARBA:ARBA00013988};
OS Bovine alphaherpesvirus 5.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC Varicellovirus bovinealpha5.
OX NCBI_TaxID=35244 {ECO:0000313|EMBL:AAF34744.1};
RN [1] {ECO:0000313|EMBL:AAF34744.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=TX 89 {ECO:0000313|EMBL:AAF34744.1};
RX PubMed=10666239; DOI=10.1128/JVI.74.5.2094-2106.2000;
RA Chowdhury S.I., Lee B.J., Ozkul A., Weiss M.L.;
RT "Bovine herpesvirus 5 glycoprotein E is important for neuroinvasiveness and
RT neurovirulence in the olfactory pathway of the rabbit.";
RL J. Virol. 74:2094-2106(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.
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; AF208294; AAF34744.1; -; Genomic_DNA.
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 450..475
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 64..183
FT /note="Envelope glycoprotein E N-terminal"
FT /evidence="ECO:0000259|Pfam:PF20418"
FT DOMAIN 244..417
FT /note="Envelope glycoprotein E Fc-binding"
FT /evidence="ECO:0000259|Pfam:PF02480"
FT REGION 190..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..442
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 514..561
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..238
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..536
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 598 AA; 63300 MW; 82D99624ECB92ED7 CRC64;
MRATAPPRPR LLPLLLPLLL PPSLLGLPVG AGLGPSPSPE ADTGAKAPAG AVFTARVGAP
VFLPGPDPRP ETRAVRGWSV LASDCPPPEP TPVCLDDREC FADVALDAAC LRTARMAPLA
IAELTERPDP AGDREFVVPD PRVSARLGRN ATGVQIADVT EEDGGVYFLY DRAAGDAGDE
ETQSALTLRV EPADAWDPAG QGEGGEGEGG KGGRGAAKPT PTPAPSPPRP TPARPAPPPR
RRHGARFRVQ PYRSHVYTPG DSFTLSVRLQ SEFFDEAPFS ASIDWYFLRP AGDCALVRIY
ETCIFHPEAP ACLHPVDARC AFASPYRSET AYSRLYERCR PASADRWPRE CEGAAYEAPV
AHLRPANNSV DLVFDGAPAS ASGLYVFVLQ YNGHVEALGL QPWSSPRTAL VRAVTDHTRP
AAADAPEPSP PPADGPADAP GRGARGPAPW LVVLGGALGL AGLIGVAALA VWVCARRAGQ
KRTYDILNPF GPVYTSLPTN EPLDVVSVSD DEFFPDEDSS FAEDGSDADD ELADEPPATA
AYDLAGPARE AGGPARPSRS GFKVWFRDPL EDDDVAPARP QTAPDYTVVA ARLKSILR
//
