ID   GI_SUHVR                Reviewed;         350 AA.
AC   P07646;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   23-FEB-2022, entry version 68.
DE   RecName: Full=Envelope glycoprotein I;
DE   AltName: Full=Glycoprotein GP63;
DE   Flags: Precursor;
GN   Name=gI;
OS   Suid herpesvirus 1 (strain Rice) (SuHV-1) (Pseudorabies virus (strain
OS   Rice)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10350;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3018284; DOI=10.1128/jvi.60.1.185-193.1986;
RA   Petrovskis E.A., Timmins J.G., Post L.E.;
RT   "Use of lambda gt11 to isolate genes for two pseudorabies virus
RT   glycoproteins with homology to herpes simplex virus and varicella-zoster
RT   virus glycoproteins.";
RL   J. Virol. 60:185-193(1986).
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; M14336; AAC35204.1; -; Genomic_DNA.
DR   PIR; A29012; VGBE63.
DR   PRIDE; P07646; -.
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..31
FT                   /evidence="ECO:0000255"
FT   CHAIN           32..350
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000038263"
FT   TOPO_DOM        32..285
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        309..350
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          202..253
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..225
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..350
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        73
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        153
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        256
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        262
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        275
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   350 AA;  36773 MW;  66AF2229EC21BEDA CRC64;
     MMMVARDVTR LPAGLLLAAL TLAALTPRVG GVLFRGAGVS VHVAGSAVLV PGDAPNLTID
     GTLLFLEGPS PSNYSGRVEL LRLDPKRACY TREYAAEYDL CPRVHHEAFR GCLRKREPLA
     RRASAAVEAR RLLFVSRPAP PDAGSYVLRV RVNGTTDLFV LTALVPPRGR PHHPTPSSAD
     ECRPVVGSWH DSLRVVDPAE DAVFTTPPPI EPEPPTTPAP PRGTGATPEP RSDEEEEDEE
     GATTAMTPVP GTLDANGTMV LNASVVSRVL LAAANATAGA RGPGKIAMVL GPTIVVLLIF
     LGGVACAARR CARGIASTGR DPGAARRSTR RPRGARPPTP SPGRPSPSPR