ID   GI_PSHV1                Reviewed;         408 AA.
AC   Q6UDF5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   02-JUN-2021, entry version 41.
DE   RecName: Full=Envelope glycoprotein I;
DE   Flags: Precursor;
GN   Name=gI; ORFNames=US7;
OS   Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS   (Pacheco's disease virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX   NCBI_TaxID=670426;
OH   NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA   Thureen D.R., Keeler C.L. Jr.;
RT   "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT   Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL   J. Virol. 80:7863-7872(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AY372243; AAQ73755.1; -; Genomic_DNA.
DR   RefSeq; NP_944449.1; NC_005264.1.
DR   SMR; Q6UDF5; -.
DR   GeneID; 2656995; -.
DR   KEGG; vg:2656995; -.
DR   Proteomes; UP000006840; Genome.
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; Reference proteome; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein; Virion.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..408
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000406866"
FT   TOPO_DOM        24..311
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        312..332
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        333..408
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          172..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          357..376
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          388..408
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        93
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        96
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        286
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        294
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   408 AA;  43470 MW;  A486BC0EE63CEFAC CRC64;
     MRAKISSQAA VAIFLALVTC CLGTVIKGLG VSGVFEDTLV VFEKVETEDV GARLVFLGDQ
     RPKNPYGGTV RVLFQPGESG TCSIPLLQVR YSNCTNTSAA VFSGCYRTDT EFSVPRANRG
     TSPGFVSLRT PTMLDSGDIY VTVHLDHLPR PDAFRIKFVS LYTGNETVRI STKDRAGRDR
     DSYGGASSPV GGRDSNRRTA SRNDDGDLPL ALYGPCRPCG KNCKNLREYL LTEESWHEWT
     SVFAPTTVAP TTTVATTAMR STTVSFATMT AEVITSTGTV SMEPHNTTTA DMVNLTAADP
     PPSEPVPALN ALAIGLVVGG TVASLVFLSV ILGGLISCCA RRRSARRLLT RSNSAREMED
     LAPSSEDART SRMSPDVVEL SELVNGAPLS HRNDIGGDDL TSISSASG