ID G9CUK4_9ALPH Unreviewed; 369 AA.
AC G9CUK4;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=Envelope glycoprotein I {ECO:0000256|ARBA:ARBA00013983};
GN Name=US7 {ECO:0000313|EMBL:AEV55069.1};
OS Gallid herpesvirus 2 strain 814.
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Mardivirus;
OC Mardivirus gallidalpha2; Gallid alphaherpesvirus 2.
OX NCBI_TaxID=1123959 {ECO:0000313|EMBL:AEV55069.1, ECO:0000313|Proteomes:UP000108473};
RN [1] {ECO:0000313|EMBL:AEV55069.1, ECO:0000313|Proteomes:UP000108473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=814 {ECO:0000313|EMBL:AEV55069.1};
RX PubMed=21984218; DOI=10.1007/s00705-011-1131-8;
RA Zhang F., Liu C.J., Zhang Y.P., Li Z.J., Liu A.L., Yan F.H., Cong F.,
RA Cheng Y.;
RT "Comparative full-length sequence analysis of Marek's disease virus vaccine
RT strain 814.";
RL Arch. Virol. 157:177-183(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 Host cell junction {ECO:0000256|ARBA:ARBA00004315}. Host cell membrane
CC {ECO:0000256|ARBA:ARBA00004402}; Single-pass type I membrane protein
CC {ECO:0000256|ARBA:ARBA00004402}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}. Virion membrane
CC {ECO:0000256|ARBA:ARBA00004381}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004381}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family.
CC {ECO:0000256|ARBA:ARBA00005825}.
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DR EMBL; JF742597; AEV55069.1; -; Genomic_DNA.
DR Proteomes; UP000108473; Genome.
DR GO; GO:0070161; C:anchoring junction; 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:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR InterPro; IPR002874; Herpes_gI.
DR Pfam; PF01688; Herpes_gI; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Virion {ECO:0000256|ARBA:ARBA00022844}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 283..302
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 369 AA; 42032 MW; 3ADD5A28AA8C0E8A CRC64;
MTLYSFFGTA CVIAMYVLQL LFWIRLFRGI WSIVYTGTSV TLSTDQSALV AFCGLDKMVN
VRGQLLFLGD QTRTSSYTGT TEILKWDEEY KCYSVLHATS YMDCPAIDAT VFRGCRDAVV
YAQPHGRVQP FPEKGTLLRI VEPRVSDTGS YYIRVSLAGR NMSDIFRMVV IIRSSKSWAC
NHSASSFQAH KCIRYVDRMA FENYLIGHVG NLLDSDSELH AIYNITPQSI STDINIVTTP
FYDNSGTIYS PTVFNLFNNN SHVDAMNSTG MWNTVLKYTL PRLIYFSTMI VLCIIALAIY
LVCERCRSPH RRIYIGEPRS DEAPLITSAV NESFQYDYNV KETPSDVIEK ELMEKLKKKV
ELLEREECV
//
