P10185 (GL_HHV11) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 66.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Envelope glycoprotein L Short name=gL | ||||
| Gene names |
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| Organism | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome] | ||||
| Taxonomic identifier | 10299 [NCBI] | ||||
| Taxonomic lineage | Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › ![]() | ||||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 224 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 | 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. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Fusion of virus membrane with host cell membrane Fusion of virus membrane with host membrane Viral penetration into host cytoplasm Virus entry into host cell |
| Cellular component | Host cell membrane Host membrane Membrane Viral envelope protein Virion |
| Domain | Signal |
| Ligand | Sialic acid |
| PTM | Glycoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | viral entry into host cell via membrane fusion with the plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell viral envelopeInferred from electronic annotation. Source: UniProtKB-KW virion membraneInferred 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 – 19 | 19 | Potential | ||||||
| Chain | 20 – 224 | 205 | Envelope glycoprotein L | PRO_0000038264 | |||||
Regions | |||||||||
| Region | 20 – 161 | 142 | Interaction with gL | ||||||
| Compositional bias | 215 – 218 | 4 | Poly-Arg | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 170 | 1 | N-linked (GlcNAc...); by host Probable | ||||||
Natural variations | |||||||||
| Natural variant | 90 | 1 | K → R in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 100 | 1 | V → G in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 109 | 1 | Y → H in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 115 | 1 | N → D in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 168 | 1 | P → L in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 171 | 1 | G → R in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 181 | 1 | P → S in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 196 | 1 | P → S in strain: Nonneuroinvasive mutant HF10. | ||||||
| Natural variant | 224 | 1 | L → I in strain: Nonneuroinvasive mutant HF10. | ||||||
Sequences
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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. |
| PIR | WMBEX1. A28133. |
| RefSeq | NP_044602.1. NC_001806.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 2703393. |
Phylogenomic databases | |
| ProtClustDB | PHA3301. |
Family and domain databases | |
| InterPro | IPR022200. Herpes_gL_C. IPR007923. Herpes_gL_N. [Graphical view] |
| Pfam | PF12524. GlyL_C. 1 hit. PF05259. Herpes_UL1. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GL_HHV11 | ||||||||
| Accession | Primary (citable) accession number: P10185 Secondary accession number(s): Q09ID2, Q76WT7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
