ID   GI_VZVO                 Reviewed;         354 AA.
AC   Q77NN4;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 68.
DE   RecName: Full=Envelope glycoprotein I;
DE            Short=gI;
DE   AltName: Full=Glycoprotein IV;
DE            Short=GPIV;
DE   Flags: Precursor;
GN   Name=gI; ORFNames=ORF67;
OS   Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=341980;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=10720545; DOI=10.1086/315335;
RA   Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
RA   Krause P.R.;
RT   "Nucleotide sequences that distinguish Oka vaccine from parental Oka and
RT   other varicella-zoster virus isolates.";
RL   J. Infect. Dis. 181:1153-1157(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=11162813; DOI=10.1006/viro.2000.0775;
RA   Faga B., Maury W., Bruckner D.A., Grose C.;
RT   "Identification and mapping of single nucleotide polymorphisms in the
RT   varicella-zoster virus genome.";
RL   Virology 280:1-6(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC   Oka varicella vaccine Biken (V-Oka-Biken);
RX   PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA   Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT   "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT   its parental virus.";
RL   J. Virol. 76:11447-11459(2002).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC   Oka varicella vaccine Varivax (V-Oka-Merk);
RX   PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA   Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA   Vassilev V.;
RT   "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL   J. Virol. 82:11023-11044(2008).
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 (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: The heterodimer gE/gI serves as a receptor for the Fc part of
CC       human IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus
CC       be involved in anti-VZV antibodies bipolar bridging, followed by
CC       intracellular endocytosis and degradation, thereby interfering with
CC       host Ig-mediated immune responses (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with gE; this interaction enhances the Fc receptor
CC       function of gE. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q77NN4; Q9J3M8: gE; NbExp=3; IntAct=EBI-2533019, EBI-2532305;
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; AF206304; AAF61668.1; -; Genomic_DNA.
DR   EMBL; AY016450; AAK19945.1; -; Genomic_DNA.
DR   EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; DQ008354; AAY57676.1; -; Genomic_DNA.
DR   EMBL; DQ008355; AAY57747.1; -; Genomic_DNA.
DR   RefSeq; NP_040189.1; NC_001348.1.
DR   DIP; DIP-45062N; -.
DR   IntAct; Q77NN4; 9.
DR   MINT; Q77NN4; -.
DR   GeneID; 1487689; -.
DR   KEGG; vg:1487689; -.
DR   Proteomes; UP000002603; Genome.
DR   Proteomes; UP000008504; Genome.
DR   Proteomes; UP000008505; Genome.
DR   Proteomes; UP000008506; 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   1: Evidence at protein level;
KW   Glycoprotein; Host cell junction; Host cell membrane; Host Golgi apparatus;
KW   Host membrane; Host-virus interaction; Membrane; Phosphoprotein; Signal;
KW   Transmembrane; Transmembrane helix; Viral envelope protein;
KW   Viral immunoevasion; Virion.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..354
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000385500"
FT   TOPO_DOM        21..274
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        275..295
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        296..354
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         343
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        33
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        47
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        67
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        116
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   354 AA;  39364 MW;  E52B0B60BF52E666 CRC64;
     MFLIQCLISA VIFYIQVTNA LIFKGDHVSL QVNSSLTSIL IPMQNDNYTE IKGQLVFIGE
     QLPTGTNYSG TLELLYADTV AFCFRSVQVI RYDGCPRIRT SAFISCRYKH SWHYGNSTDR
     ISTEPDAGVM LKITKPGIND AGVYVLLVRL DHSRSTDGFI LGVNVYTAGS HHNIHGVIYT
     SPSLQNGYST RALFQQARLC DLPATPKGSG TSLFQHMLDL RAGKSLEDNP WLHEDVVTTE
     TKSVVKEGIE NHVYPTDMST LPEKSLNDPP ENLLIIIPIV ASVMILTAMV IVIVISVKRR
     RIKKHPIYRP NTKTRRGIQN ATPESDVMLE AAIAQLATIR EESPPHSVVN PFVK