Envelope glycoprotein E precursor - Human herpesvirus 1 (strain F) (HHV-1)

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Q703F0 (GE_HHV1F) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 45. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Envelope glycoprotein E
Short name=gE

Alternative name(s):
gE-1

Gene names

Name:	gE
ORF Names:	US8

Organism

Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1)

Taxonomic identifier

10304 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus ›

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	552 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	In epithelial cells, the heterodimer gE/gI is required for the cell-to-cell spread of the virus, by sorting nascent virions to cell junctions. Once the virus reaches the cell junctions, virus particles can spread to adjacent cells extremely rapidly through interactions with cellular receptors that accumulate at these junctions. Implicated in basolateral spread in polarized cells. In neuronal cells, gE/gI is essential for the anterograde spread of the infection throughout the host nervous system. Together with US9, the heterodimer gE/gI is involved in the sorting and transport of viral structural components toward axon tips. Ref.3 Ref.4 Ref.5 Ref.6 The heterodimer gE/gI serves as a receptor for the Fc part of host IgG. Dissociation of gE/gI from IgG occurs at acidic pH. May thus be involved in anti-HSV antibodies bipolar bridging, followed by intracellular endocytosis and degradation, thereby interfering with host IgG-mediated immune responses By similarity. Ref.3 Ref.4 Ref.5 Ref.6
Subunit structure	Interacts with gI; this interaction enhances the Fc receptor function of gE. The heterodimer gE/gI interacts with the Fc part of host IgG. Interacts (via C-terminus) with VP22 tegument protein; this interaction is necessary for the recruitment of VP22 to the Golgi and its packaging into virions. Interacts (via C-terminus) with UL11 tegument protein By similarity. Ref.3
Subcellular location	Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein By similarity. Host cell junction. Host Golgi apparatus membrane; Single-pass membrane protein. Host endosome membrane; Single-pass membrane protein Probable. Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN), maybe through an interaction with PACS-1 sorting protein. The heterodimer gE/gI then redistributes to cell junctions to promote cell-cell spread later in the infection. Ref.4 Ref.5 Ref.7
Post-translational modification	Phosphorylated on serines within the acidic cluster Potential. Phosphorylation determines whether endocytosed viral gE traffics to the trans-Golgi network or recycles to the cell membrane Potential. N-glycosylated, and sulfated By similarity.
Sequence similarities	Belongs to the alphaherpesvirinae glycoprotein E family.

Ontologies

Keywords
Biological process	Host-virus interaction Viral immunoevasion
Cellular component	Host Golgi apparatus Host cell junction Host cell membrane Host endosome Host membrane Membrane Viral envelope protein Virion
Domain	Signal Transmembrane Transmembrane helix
PTM	Disulfide bond Glycoprotein Phosphoprotein Sulfation
Gene Ontology (GO)
Biological_process	evasion or tolerance by virus of host immune response Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell Golgi membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell junction Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

Potential

Chain

21 – 552

532

Envelope glycoprotein E

PRO_0000038226

Regions

Topological domain

21 – 421

401

Virion surface Potential

Transmembrane

422 – 442

Helical; Potential

Topological domain

443 – 552

110

Intravirion Potential

Region

63 – 88

Interaction with gI By similarity

Region

237 – 382

146

Fc-binding By similarity

Region

472 – 497

Interaction with VP22 and UL11 By similarity

Region

478 – 486

Acidic By similarity

Motif

465 – 468

Internalization motif Potential

Motif

474 – 477

Internalization motif Potential

Compositional bias

163 – 216

Pro-rich

Amino acid modifications

Modified residue

176

Sulfotyrosine Potential

Modified residue

478

Phosphoserine; by host CK2 By similarity

Modified residue

479

Phosphoserine; by host CK2 By similarity

Modified residue

505

Phosphoserine By similarity

Glycosylation

124

N-linked (GlcNAc...); by host Potential

Glycosylation

245

N-linked (GlcNAc...); by host Potential

Disulfide bond

273 ↔ 299

By similarity

Disulfide bond

282 ↔ 291

By similarity

Disulfide bond

316 ↔ 325

By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

Q703F0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8F689BF77BE07BB7
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FASTA

552

59,313

        10         20         30         40         50         60 
MDRGAVVGFL LGVCVVSCLA GTPKTSWRRV SVGEDVSLLP APGPTGRGPT QKLLWAVEPL 

        70         80         90        100        110        120 
DGCGPLHPSW XSLMPPKQVP ETVVDAACMR APVPLAMAYA PPAPSATGGL RTDFVWQERA 

       130        140        150        160        170        180 
AVVNRSLVIY GVRETDSGLY TLSVGDIKDP ARQVASVVLV VQPAPVPTPP PTPADYDEDD 

       190        200        210        220        230        240 
NDEGEGEDES LAGTPASGTP RLPPPPAPPR SWPSAPEVSH VRGVTVRMET PEAILFSPGE 

       250        260        270        280        290        300 
AFSTNVSIHA IAHDDQTYTM DVVWLRFDVP TSCAEMRIYE SCLYHPQLPE CLSPADAPCA 

       310        320        330        340        350        360 
ASTWTSRLAV RSYAGCSRTN PPPRCSAEAH MEPVPGLAWQ AASVNLEFRD ASPQHSGLYL 

       370        380        390        400        410        420 
CVVYVNDHIH AWGHITISTA AXYRNAVVEQ PLPQRGADLA EPTHPHVGAP PHAPPTHGAL 

       430        440        450        460        470        480 
RLGAVMGAAL LLSVLGLSVW ACMTCWRRRA WRAVKSRASG KGPTYIRVAD SELYADWSSD 

       490        500        510        520        530        540 
SEGERDQVPW LAPPERPDSP STNGSGFEIL SPTAPSVYPR SDGHQSRRQL TTFGSGRPDR 

       550 
RYSQASDSSV FW

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References

[1]	"Phylogenetic analysis of clinical herpes simplex virus type 1 isolates identified three genetic groups and recombinant viruses." Norberg P.R., Bergstroem T., Kekabdar E., Lindh M., Liljeqvist J.-A. J. Virol. 78:10755-10764(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Identification of a new transcriptional unit that yields a gene product within the unique sequences of the short component of the herpes simplex virus 1 genome." Georgopoulou U., Michaelidou A., Roizman B., Mavromara-Nazos P. J. Virol. 67:3961-3968(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 440-552.
[3]	"Herpes simplex virus immunoglobulin G Fc receptor activity depends on a complex of two viral glycoproteins, gE and gI." Johnson D.C., Frame M.C., Ligas M.W., Cross A.M., Stow N.D. J. Virol. 62:1347-1354(1988) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH GLYCOPROTEIN I.
[4]	"Herpes simplex virus gE/gI sorts nascent virions to epithelial cell junctions, promoting virus spread." Johnson D.C., Webb M., Wisner T.W., Brunetti C. J. Virol. 75:821-833(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[5]	"Herpes simplex virus gE/gI must accumulate in the trans-Golgi network at early times and then redistribute to cell junctions to promote cell-cell spread." Farnsworth A., Johnson D.C. J. Virol. 80:3167-3179(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[6]	"Herpes simplex virus gE/gI and US9 proteins promote transport of both capsids and virion glycoproteins in neuronal axons." Snyder A., Polcicova K., Johnson D.C. J. Virol. 82:10613-10624(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"Comprehensive characterization of extracellular herpes simplex virus type 1 virions." Loret S., Guay G., Lippe R. J. Virol. 82:8605-8618(2008) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ626469 Genomic DNA. Translation: CAF24756.1. S62895 Genomic DNA. Translation: AAB27080.1.
3D structure databases
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Family and domain databases
InterPro	IPR003404. Herpes_glycopE. [Graphical view]
Pfam	PF02480. Herpes_gE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GE_HHV1F

Accession

Primary (citable) accession number: Q703F0
Secondary accession number(s): Q86624

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 7, 2004
Last sequence update:	July 5, 2004
Last modified:	April 3, 2013
This is version 45 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protocols and materials databases

Family and domain databases

Entry information

Relevant documents