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A1Z0Q5 (GD_HHV1K) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 31. 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 D

Short name=gD
Gene names
Name:gD
ORF Names:US6
OrganismHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifier10306 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Envelope glycoprotein that binds to the potential host cell entry receptors TNFRSF14/HVEM, PVRL1 and 3-O-sulfated heparan sulfate. May trigger fusion with host membrane, by recruiting the fusion machinery composed of gB and gH/gL By similarity.

Subunit structure

Homodimer By similarity. Interacts with host receptor TNFRSF14. Interacts with host receptor PVRL1. Mutant Rid1 interacts with host receptor PVRL2. Interacts (via profusion domain) with gB; this interaction occurs in the absence of gH/gL. Interacts (via profusion domain) with gH/gL heterodimer; this interaction occurs in the absence of gB. Associates with the gB-gH/gL-gD complex. Interacts (via C-terminus) with UL11 tegument protein. Interacts (via C-terminus) with VP22 tegument protein; this interaction might be very weak By similarity. Ref.3 Ref.5

Subcellular location

Virion membrane; Single-pass type I membrane protein By similarity. Note: During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs By similarity.

Sequence similarities

Belongs to the herpesviridae glycoprotein D family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential
Chain26 – 394369Envelope glycoprotein D
PRO_5000142086

Regions

Topological domain26 – 340315Virion surface Potential
Transmembrane341 – 36121Helical; Potential
Topological domain362 – 39433Intravirion Potential
Region26 – 5732Interaction with TNFRSF14
Region261 – 30545Profusion By similarity
Compositional bias269 – 33769Pro-rich
Compositional bias365 – 38117Arg/Lys-rich (highly basic; probably serves to anchor the glycoprotein in the membrane)

Sites

Metal binding641Zinc 1; shared with dimeric partner By similarity
Metal binding2401Zinc 1; shared with dimeric partner By similarity

Amino acid modifications

Glycosylation1191N-linked (GlcNAc...); by host Potential
Glycosylation1461N-linked (GlcNAc...); by host Potential
Glycosylation2871N-linked (GlcNAc...); by host Potential
Disulfide bond91 ↔ 214 By similarity
Disulfide bond131 ↔ 227 By similarity
Disulfide bond143 ↔ 152 By similarity

Natural variations

Natural variant521Q → P in strain: Mutant rid1 and Isolate KOSc(AC3,AC6); interference resistant.
Natural variant521Q → R in strain: Mutant rid2; interference resistant.

Experimental info

Sequence conflict301A → V in AAA19630. Ref.1
Sequence conflict301A → V in ABM52980. Ref.2

Sequences

Sequence LengthMass (Da)Tools
A1Z0Q5 [UniParc].

Last modified September 22, 2009. Version 2.
Checksum: 905A0F0F1953CB7F

FASTA39443,317
        10         20         30         40         50         60 
MGGAAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVL DQLTDPPGVR 

        70         80         90        100        110        120 
RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS EAPQIVRGAS EDVRKQPYNL 

       130        140        150        160        170        180 
TIAWFRMGGN CAIPITVMEY TECSYNKSLG ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA 

       190        200        210        220        230        240 
PAFETAGTYL RLVKINDWTE ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD 

       250        260        270        280        290        300 
SIGMLPRFIP ENQRTVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED 

       310        320        330        340        350        360 
SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS LLAALVICGI 

       370        380        390 
VYWMHRRTRK APKRIRLPHI REDDQPSSHQ PLFY 

« Hide

References

[1]"Molecular basis for resistance of herpes simplex virus type 1 mutants to the sulfated oligosaccharide inhibitor PI-88."
Ekblad M., Adamiak B., Bergefall K., Nenonen H., Roth A., Bergstrom T., Ferro V., Trybala E.
Virology 367:244-252(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: Isolate KOSc, Isolate KOSc(AC3,AC6) and Isolate KOSc(AC4).
[2]"Single amino acid substitutions in glycoprotein D of herpes simplex virus type 1 that confer resistance to gD-mediated interference also alter virus infectivity."
Dean H.J., Terhune S.S., Shieh M.-T., Spear P.G.
Virology 199:67-80(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: KOS, Mutant Rid1 and Mutant Rid2.
[3]"Herpes simplex virus glycoprotein D can bind to poliovirus receptor-related protein 1 or herpesvirus entry mediator, two structurally unrelated mediators of virus entry."
Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D., Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.
J. Virol. 72:7064-7074(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HUMAN RECEPTORS PVRL1 AND TNFRSF14.
[4]"A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1 entry."
Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D., Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.
Cell 99:13-22(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: BINDING TO 3-O-SULFATED HEPARAN SULFATE.
[5]"Structural features of nectin-2 (HveB) required for herpes simplex virus entry."
Martinez W.M., Spear P.G.
J. Virol. 75:11185-11195(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF MUTANT RID1 WITH HUMAN PVRL2.
Strain: Mutant Rid1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L09243 Unassigned DNA. Translation: AAA19629.1.
L09244 Unassigned DNA. Translation: AAA19631.1.
L09245 Unassigned DNA. Translation: AAA19630.1.
EF157319 Genomic DNA. Translation: ABM52978.1.
EF157320 Genomic DNA. Translation: ABM52979.1.
EF157321 Genomic DNA. Translation: ABM52980.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-237377.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR002896. Herpes_glycop_dom.
[Graphical view]
PfamPF01537. Herpes_glycop_D. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGD_HHV1K
AccessionPrimary (citable) accession number: A1Z0Q5
Secondary accession number(s): Q05060, Q69081, Q69082
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: March 19, 2014
This is version 31 of the entry and version 2 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