ID   GI_GAHVM                Reviewed;         355 AA.
AC   Q9E6L5;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   23-FEB-2022, entry version 60.
DE   RecName: Full=Envelope glycoprotein I;
DE   Flags: Precursor;
GN   Name=gI; ORFNames=MDV095;
OS   Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987) (GaHV-2) (Marek's
OS   disease herpesvirus type 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Mardivirus.
OX   NCBI_TaxID=10389;
OH   NCBI_TaxID=9031; Gallus gallus (Chicken).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10933706; DOI=10.1128/jvi.74.17.7980-7988.2000;
RA   Tulman E.R., Afonso C.L., Lu Z., Zsak L., Rock D.L., Kutish G.F.;
RT   "The genome of a very virulent Marek's disease virus.";
RL   J. Virol. 74:7980-7988(2000).
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   -!- 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; AF243438; AAG14269.1; -; Genomic_DNA.
DR   RefSeq; YP_001034012.1; NC_002229.3.
DR   GeneID; 4811454; -.
DR   KEGG; vg:4811454; -.
DR   Proteomes; UP000008072; 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..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..355
FT                   /note="Envelope glycoprotein I"
FT                   /id="PRO_0000406555"
FT   TOPO_DOM        19..268
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        269..289
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        290..355
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        147
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        167
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        245
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        253
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   355 AA;  40569 MW;  D23A6DA126ACDB00 CRC64;
     MYLLQLLFWI RLFRGIWSIV YTGTSVTLST DQSALVAFCG LDKMVNVRGQ LLFLGDQTRT
     SSYTGTTEIL KWDEEYKCYS VLHATSYMDC PAIDATVFRG CRDAVVYAQP HDRVQPFPEK
     GTLLRIVEPR VSDTGSYYIR VALAGRNMSD IFRMAVIIRS SKSWACNHSA SSFQAHKCIR
     YVDRMAFENY LIGHVGNLLD SDSELHAIYN ITPQSISTDI NIITTPFYDN SGTIYSPTVF
     NLFNNNSHVD AMNSTGMWNT VLKYTLPRLI YFSTMIVLCI IALAIYLVCE RCRSPHRRIY
     IGEPRSDEAP LITSAVNESF QYDYNVKETP SDVIEKELME KLKKKVELLE REECV