GI_EHV1D
ID GI_EHV1D Reviewed; 424 AA.
AC P68329; P18553;
DT 09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 09-NOV-2004, sequence version 1.
DT 02-JUN-2021, entry version 48.
DE RecName: Full=Envelope glycoprotein I;
DE Short=gI;
DE Flags: Precursor;
GN Name=gI;
OS Equine herpesvirus 1 (strain Kentucky D) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10330;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2177089; DOI=10.1099/0022-1317-71-12-2969;
RA Audonnet J.-C., Winslow J., Allen G., Paoletti E.;
RT "Equine herpesvirus type 1 unique short fragment encodes glycoproteins with
RT homology to herpes simplex virus type 1 gD, gI and gE.";
RL J. Gen. Virol. 71:2969-2978(1990).
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 PIR; C36646; VGBEE9.
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..22
FT /evidence="ECO:0000255"
FT CHAIN 23..424
FT /note="Envelope glycoprotein I"
FT /id="PRO_0000038260"
FT TOPO_DOM 23..319
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 341..424
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 192..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 377..408
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..399
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 35
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 78
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 236
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 424 AA; 46393 MW; EE9BEF7DAA895806 CRC64;
MAKLTGMFSA AILLSMAICS TAIIYRGEHM SMYLNASSEF AVYPTDQSLV LVGHLLFLDG
QRLPTTNYSG LIELIHYNYS SVCYTVIQTI SYESCPRVAN NAFRSCLHKT SKHYHDYFRV
NASVETNVLL NITKPQPTDS GAYILRVKLD HAPTADVFGV SAFVYDLKSK TVPDPMPTTQ
TVEPTTSYVS TPTYDYTDDV TTETESTSTS TQQAMTSTQT PSATWGTQLT TELPTNETVV
IGQEALLCHW FQPSTRVPTL YLHLLGRTGN LPEDVLLVED SEFLRTTSPA HRPSASPADG
DDFKQTNSTS LKARNKIVAM VVIPTACVLM LLLVVVGAII NGAVRKHLLS CASRRIYRSG
QGGASAAERR RLTCGPTLAA SSESLADDTT SSPPTPKPSK KTKLETDPLM EQLNRKLEAI
KEES
