ID   GI_BHV1S                Reviewed;         380 AA.
AC   Q08102;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   23-FEB-2022, entry version 52.
DE   RecName: Full=Envelope glycoprotein I;
DE            Short=gI;
DE   Flags: Precursor;
GN   Name=gI;
OS   Bovine herpesvirus 1.2 (strain ST) (BoHV-1) (Infectious bovine
OS   rhinotracheitis virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=45407;
OH   NCBI_TaxID=9913; Bos taurus (Bovine).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8122370; DOI=10.1006/viro.1994.1139;
RA   Leung-Tack P., Audonnet J.F., Riviere M.;
RT   "The complete DNA sequence and the genetic organization of the short unique
RT   region (US) of the bovine herpesvirus type 1 (ST strain).";
RL   Virology 199:409-421(1994).
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   -!- SUBUNIT: Interacts with gE. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass
CC       membrane protein {ECO:0000250}. Host cell membrane {ECO:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}. Host cell junction
CC       {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass
CC       type I 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). The heterodimer gE/gI then
CC       redistribute to cell junctions to promote cell-cell spread later in the
CC       infection (By similarity). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein I family.
CC       {ECO:0000305}.
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DR   EMBL; Z23068; CAA80605.1; -; Genomic_DNA.
DR   PIR; S35785; S35785.
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   InterPro; IPR002874; Herpes_gI.
DR   Pfam; PF01688; Herpes_gI; 1.
PE   3: Inferred from homology;
KW   Glycoprotein; Host cell junction; Host cell membrane; Host Golgi apparatus;
KW   Host membrane; Membrane; Phosphoprotein; Signal; Transmembrane;
KW   Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..380
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000115774"
FT   TOPO_DOM        21..293
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        315..380
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          172..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   380 AA;  39911 MW;  AEBE1FB9B430D2BD CRC64;
     MRCLLLWMVV LAARAAPARS LVYRGEAVGL RADGPVAFAV HPTDATLALR GRLIFLEHQL
     PAGRRYNGTV ELLRYHAAGD CFVMLQTTAF ASCPRVANNA FRSCLHADTR PARSERRASA
     AVENHVLFSI ARPRPIDSGL YFLRVGIYGG TAGSERRRDV FPLAAFVHSF GEPGDPEAAA
     RTPAPSRQSR PAASGLTSSA SLYDRALARS PQAPPPRPAP PRAARAGPRR PERVDETTEV
     EAATRAGSAF ALTTPPAGPT ASPAASPSRA FSAAAPAAAA QPAGDTPARF RRQLASILVP
     LCVLVLLLLA LCAATVNCAL RRRLLPCSRR VYKPRTCAAC GSGTCAGRPP CRGAAPSAPA
     TVVALGSRPK APPLATISEE