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Database: UniProt
Entry: H9DUH9_9ALPH
LinkDB: H9DUH9_9ALPH
Original site: H9DUH9_9ALPH 
ID   H9DUH9_9ALPH            Unreviewed;       140 AA.
AC   H9DUH9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Envelope glycoprotein E {ECO:0000256|ARBA:ARBA00013988};
DE   Flags: Fragment;
GN   Name=US8 {ECO:0000313|EMBL:AFD50683.1};
OS   Suid alphaherpesvirus 1.
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Varicellovirus;
OC   Varicellovirus suidalpha1.
OX   NCBI_TaxID=10345 {ECO:0000313|EMBL:AFD50683.1};
RN   [1] {ECO:0000313|EMBL:AFD50683.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=A/swine/Italy/2945/2001 {ECO:0000313|EMBL:AFD50683.1};
RX   PubMed=23331342;
RA   Sozzi E., Moreno A., Lelli D., Cinotti S., Alborali G.L., Nigrelli A.,
RA   Luppi A., Bresaola M., Catella A., Cordioli P.;
RT   "Genomic Characterization of Pseudorabies Virus Strains Isolated in
RT   Italy.";
RL   Transbound. Emerg. Dis. 0:0-0(2013).
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       Endosome membrane {ECO:0000256|ARBA:ARBA00004190}; Single-pass membrane
CC       protein {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}. 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; JQ619759; AFD50683.1; -; 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:0016020; C: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; IPR003404; Herpes_glycopE_Fc.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   Pfam; PF02480; Herpes_gE; 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|ARBA:ARBA00022989};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW   Viral envelope protein {ECO:0000256|ARBA:ARBA00022879};
KW   Virion {ECO:0000256|ARBA:ARBA00022844}.
FT   DOMAIN          10..105
FT                   /note="Envelope glycoprotein E Fc-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02480"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFD50683.1"
FT   NON_TER         140
FT                   /evidence="ECO:0000313|EMBL:AFD50683.1"
SQ   SEQUENCE   140 AA;  15780 MW;  C962F23C1C11D252 CRC64;
     VGPARHEPRF HALGFHSQLF SPGDTFDLMP RLVSDMGDSR ENFTATLDWY YARAPTRCLL
     YYVYEPCIYH PRAPECLRPV DPACSFTSPA RARLVARRAY ASCSPLLGDR WLTACPFDAF
     GEEVHTNATA DESGLYVLVM
//
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