ID   GI_CHV9D                Reviewed;         353 AA.
AC   Q04547;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   02-JUN-2021, entry version 76.
DE   RecName: Full=Envelope glycoprotein I;
DE   AltName: Full=Membrane glycoprotein 1;
DE   Flags: Precursor;
GN   Name=gI; Synonyms=US3;
OS   Cercopithecine herpesvirus 9 (strain DHV) (CeHV-9) (Simian varicella
OS   virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=36348;
OH   NCBI_TaxID=9534; Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8384754; DOI=10.1006/viro.1993.1185;
RA   Fletcher T.M. III, Gray W.L.;
RT   "DNA sequence and genetic organization of the unique short (US) region of
RT   the simian varicella virus genome.";
RL   Virology 193:762-773(1993).
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; L07067; AAA47888.1; -; Genomic_DNA.
DR   PIR; C46113; C46113.
DR   RefSeq; NP_077481.1; NC_002686.2.
DR   GeneID; 920526; -.
DR   KEGG; vg:920526; -.
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..353
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000038261"
FT   TOPO_DOM        21..274
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        294..353
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          303..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..324
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        40
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        138
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        252
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   353 AA;  40471 MW;  E0314F7B5B0E4AA2 CRC64;
     MLLWYTTASI MRYLMVFMLF GIQCAAAIIY RGNYISLYVN SSATSIFLKG NNNDASIRGR
     FLFIGDQFPV TNTYNVTVEL LHVNQTTLCL QPLYRVMYGE CPRIRTGAII ACRVKRSWHY
     ENATQLTDPN VEIIFKMNNT KVEDAGIYLL VVQLDYTSLF DIFFVSLNVY PKQDTSNEDV
     NYFPPVYSPS HILNTFKICH KFPVHNGMEQ SILQHIVTSD VDTETENLSW QKDDLGSTQK
     PRKNFNPDVK VNVTHETRKT LMESSADVFM IAVPITASLL VILAIIIVVT VGIYRRRSSE
     KRKIYRPKRT KEQASTEKRE RSESDVLLEA AVARLETIQE ENPPHSVINP FTK