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P10185 (GL_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Envelope glycoprotein L

Short name=gL
Gene names
Name:gL
ORF Names:UL1
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length224 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding of gD to one of its receptors, membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. Ref.7

Subunit structure

Interacts with glycoprotein H (gH); this interaction is necessary for the correct processing and cell surface expression of gH. The heterodimer gH/gL seems to interact with gB trimers during fusion. Associates with the gB-gH/gL-gD complex By similarity. Ref.5 Ref.8

Subcellular location

Virion membrane; Peripheral membrane protein; Extracellular side. Host cell membrane; Peripheral membrane protein; Extracellular side By similarity. Note: gL is not anchored to the viral envelope, but associates with the extravirion surface through its binding to gH. During virion morphogenesis, this protein probably accumulates in the 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) By similarity. A fraction of gL has also been found associated to the cell surface in the absence of gH, suggesting incomplete cleavage of the signal peptide or presence of a cell surface receptor for secreted gL. Ref.6 Ref.8

Post-translational modification

N-glycosylated, O-glycosylated, and sialylated By similarity.

Sequence similarities

Belongs to the herpesviridae glycoprotein L family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 224205Envelope glycoprotein L
PRO_0000038264

Regions

Region20 – 161142Interaction with gL
Compositional bias215 – 2184Poly-Arg

Amino acid modifications

Glycosylation1701N-linked (GlcNAc...); by host Probable

Natural variations

Natural variant901K → R in strain: Nonneuroinvasive mutant HF10.
Natural variant1001V → G in strain: Nonneuroinvasive mutant HF10.
Natural variant1091Y → H in strain: Nonneuroinvasive mutant HF10.
Natural variant1151N → D in strain: Nonneuroinvasive mutant HF10.
Natural variant1681P → L in strain: Nonneuroinvasive mutant HF10.
Natural variant1711G → R in strain: Nonneuroinvasive mutant HF10.
Natural variant1811P → S in strain: Nonneuroinvasive mutant HF10.
Natural variant1961P → S in strain: Nonneuroinvasive mutant HF10.
Natural variant2241L → I in strain: Nonneuroinvasive mutant HF10.

Sequences

Sequence LengthMass (Da)Tools
P10185 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: CED51D2FC1D7777F

FASTA22424,934
        10         20         30         40         50         60 
MGILGWVGLI AVGVLCVRGG LPSTEYVIRS RVAREVGDIL KVPCVPLPSD DLDWRYETPS 

        70         80         90        100        110        120 
AINYALIDGI FLRYHCPGLD TVLWDRHAQK AYWVNPFLFV AGFLEDLSYP AFPANTQETE 

       130        140        150        160        170        180 
TRLALYKEIR QALDSRKQAA SHTPVKAGCV NFDYSRTRRC VGRQDLGPTN GTSGRTPVLP 

       190        200        210        220 
PDDEAGLQPK PLTTPPPIIA TSDPTPRRDA ATKSRRRRPH SRRL 

« Hide

References

« Hide 'large scale' references
[1]"The complete DNA sequence of the long unique region in the genome of herpes simplex virus type 1."
McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D., Perry L.J., Scott J.E., Taylor P.
J. Gen. Virol. 69:1531-1574(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[2]"The DNA sequences of the long repeat region and adjoining parts of the long unique region in the genome of herpes simplex virus type 1."
Perry L.J., McGeoch D.J.
J. Gen. Virol. 69:2831-2846(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Determination and analysis of the DNA sequence of highly attenuated herpes simplex virus type 1 mutant HF10, a potential oncolytic virus."
Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.
Microbes Infect. 9:142-149(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Nonneuroinvasive mutant HF10.
[4]"Herpes simplex virus type 1 bacterial artificial chromosome."
Cunningham C., Davison A.J.
Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 17 syn+.
[5]"Structure-function analysis of herpes simplex virus type 1 gD and gH-gL: clues from gDgH chimeras."
Cairns T.M., Milne R.S., Ponce-de-Leon M., Tobin D.K., Cohen G.H., Eisenberg R.J.
J. Virol. 77:6731-6742(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GH.
[6]"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.
Strain: F.
[7]"Herpes simplex virus gD forms distinct complexes with fusion executors gB and gH/gL in part through the C-terminal profusion domain."
Gianni T., Amasio M., Campadelli-Fiume G.
J. Biol. Chem. 284:17370-17382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: F.
[8]"Insertional mutations in herpes simplex virus 1 gL identify functional domains for association with gH and for membrane fusion."
Fan Q., Lin E., Spear P.G.
J. Virol. 83:11607-11615(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GH, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X14112 Genomic DNA. Translation: CAA32337.1.
D00373 Genomic DNA. Translation: BAA00272.1.
DQ889502 Genomic DNA. Translation: ABI63463.1.
FJ593289 Genomic DNA. Translation: ACM62223.1.
PIRWMBEX1. A28133.
RefSeqNP_044602.1. NC_001806.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2364696.

Protein family/group databases

TCDB1.G.10.1.1. the herpes simplex virus membrane fusion complex (hsv-mfc) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703393.

Family and domain databases

InterProIPR022200. Herpes_gL_C.
IPR007923. Herpes_gL_N.
[Graphical view]
PfamPF12524. GlyL_C. 1 hit.
PF05259. Herpes_UL1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGL_HHV11
AccessionPrimary (citable) accession number: P10185
Secondary accession number(s): Q09ID2, Q76WT7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: May 14, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families