GE_PSHV1
ID GE_PSHV1 Reviewed; 568 AA.
AC Q6UDF4;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 23-FEB-2022, entry version 59.
DE RecName: Full=Envelope glycoprotein E;
DE Short=gE;
DE Flags: Precursor;
GN Name=US8;
OS Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997) (PsHV-1)
OS (Pacheco's disease virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=670426;
OH NCBI_TaxID=152276; Amazona oratrix (yellow-headed parrot).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16873243; DOI=10.1128/jvi.00134-06;
RA Thureen D.R., Keeler C.L. Jr.;
RT "Psittacid herpesvirus 1 and infectious laryngotracheitis virus:
RT Comparative genome sequence analysis of two avian alphaherpesviruses.";
RL J. Virol. 80:7863-7872(2006).
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 gI. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250};
CC Single-pass type I membrane protein {ECO:0000250}. Host cell junction
CC {ECO:0000250}. Host Golgi apparatus membrane {ECO:0000250}; Single-pass
CC membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000250};
CC Single-pass 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), maybe through an interaction
CC with PACS-1 sorting protein. The heterodimer gE/gI then redistributes
CC to cell junctions to promote cell-cell spread later in the infection
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on serines within the acidic cluster.
CC Phosphorylation determines whether endocytosed viral gE traffics to the
CC trans-Golgi network or recycles to the cell membrane. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein E family.
CC {ECO:0000305}.
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DR EMBL; AY372243; AAQ73756.1; -; Genomic_DNA.
DR RefSeq; NP_944450.1; NC_005264.1.
DR SMR; Q6UDF4; -.
DR GeneID; 2656958; -.
DR KEGG; vg:2656958; -.
DR Proteomes; UP000006840; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
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 GO; GO:0075509; P:endocytosis involved in viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
DR InterPro; IPR003404; Herpes_glycopE.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR Pfam; PF02480; Herpes_gE; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell junction; Host cell membrane;
KW Host endosome; Host Golgi apparatus; Host membrane; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus endocytosis by host; Virus entry into host cell.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..568
FT /note="Envelope glycoprotein E"
FT /id="PRO_0000406829"
FT TOPO_DOM 21..422
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 423..443
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 444..568
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 470..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 482..497
FT /note="Acidic"
FT /evidence="ECO:0000250"
FT MOTIF 465..468
FT /note="Internalization motif"
FT /evidence="ECO:0000250"
FT COMPBIAS 486..500
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..534
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 88
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 179
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 248
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 271..280
FT /evidence="ECO:0000250"
SQ SEQUENCE 568 AA; 61667 MW; 4154C2F7135DB35C CRC64;
MMPATLAGLA LAVTVATMFA QRVDSTTIHH VSGLKGKPLL FGPSLRRTLP AGGTFKWVLV
LSDPCAPKPT EICVSVGHCF YDLVSSDNDS ECANKDRRVL TLALLTKSKT GELRVIGPMA
ASSALVGDAG ELEQLRRRVS AGMGLTDDGD ISFAAADKVN EGLYGVRVMG SGDSYTFFNV
TVATETAGDD RDLATVRHVD IAHNIVPSED RDHVFVSMPR MHVAWPHGTT VLHPKMIIAA
ASWRPEYNFT YEWYAVPYDG YCATMRLFEA CLYHPSAPAC LDPAGHRGCV VGTMTHDDLV
GRVLMARCRG SDLRTCEPHV IHIKQKPMVS LGRAVPELRV ESAAHIPSLY ILVVKIDDSV
AGWAYTELMA EGSSPRVVID IHMPRPTSAQ GGIAALREIE NDDSAPSLGS NEGGGPGNSK
RRAAVLGAAV WIALTLLILG GLGAYVAVNK KCLRDKRQWL RGSRKPTLET HAHTYTSLPV
GGDLSLEQDA EDEDEDEEEL LYERERRRSS SGSKKSSRSP SRRSSRRNSF GPTLSANALS
RFDKTVKLAM AEVAGRLLAN KTFPSQRY
