GI_VZVD
ID GI_VZVD Reviewed; 354 AA.
AC P09258;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 90.
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 Dumas) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10338;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA Davison A.J., Scott J.E.;
RT "The complete DNA sequence of varicella-zoster virus.";
RL J. Gen. Virol. 67:1759-1816(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6321154; DOI=10.1002/j.1460-2075.1983.tb01724.x;
RA Davison A.J.;
RT "DNA sequence of the US component of the varicella-zoster virus genome.";
RL EMBO J. 2:2203-2209(1983).
RN [3]
RP MUTAGENESIS, AND PHOSPHORYLATION AT SER-343.
RX PubMed=8207795; DOI=10.1128/jvi.68.7.4204-4211.1994;
RA Yao Z., Grose C.;
RT "Unusual phosphorylation sequence in the gpIV (gI) component of the
RT varicella-zoster virus gpI-gpIV glycoprotein complex (VZV gE-gI complex).";
RL J. Virol. 68:4204-4211(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 (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 -!- 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; X04370; CAA27950.1; -; Genomic_DNA.
DR EMBL; X00208; CAA25032.1; -; Genomic_DNA.
DR PIR; F27345; VGBE67.
DR RefSeq; NP_040189.1; NC_001348.1.
DR iPTMnet; P09258; -.
DR PRIDE; P09258; -.
DR GeneID; 1487689; -.
DR KEGG; vg:1487689; -.
DR Proteomes; UP000002602; 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;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral immunoevasion; Virion.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..354
FT /note="Envelope glycoprotein I"
FT /id="PRO_0000038262"
FT TOPO_DOM 18..295
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 296..312
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 313..354
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:8207795"
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"
FT MUTAGEN 338
FT /note="T->A: No effect on phosphorylation."
FT /evidence="ECO:0000269|PubMed:8207795"
FT MUTAGEN 341..342
FT /note="EE->AA: Moderate decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:8207795"
FT MUTAGEN 343
FT /note="S->A: Marked decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:8207795"
FT MUTAGEN 344
FT /note="P->A: Marked decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:8207795"
FT MUTAGEN 345
FT /note="P->A: Decrease in phosphorylation."
FT /evidence="ECO:0000269|PubMed:8207795"
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
