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A1Z0Q5

- GD_HHV1K

UniProt

A1Z0Q5 - GD_HHV1K

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Protein

Envelope glycoprotein D

Gene

gD

Organism
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Zinc 1; shared with dimeric partnerBy similarity
Metal bindingi240 – 2401Zinc 1; shared with dimeric partnerBy similarity

GO - Molecular functioni

  1. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. viral entry into host cell Source: UniProtKB-KW
  2. virion attachment to host cell Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Host-virus interaction, Viral attachment to host cell, Viral attachment to host entry receptor, Virus entry into host cell

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Envelope glycoprotein D
Short name:
gD
Gene namesi
Name:gD
ORF Names:US6
OrganismiHuman herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Taxonomic identifieri10306 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostiHomo sapiens (Human) [TaxID: 9606]

Subcellular locationi

Virion membrane By similarity; 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

GO - Cellular componenti

  1. integral component of membrane Source: UniProtKB-KW
  2. viral envelope Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Viral envelope protein, Virion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 394369Envelope glycoprotein DPRO_5000142086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi91 ↔ 214By similarity
Glycosylationi119 – 1191N-linked (GlcNAc...); by hostSequence Analysis
Disulfide bondi131 ↔ 227By similarity
Disulfide bondi143 ↔ 152By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...); by hostSequence Analysis
Glycosylationi287 – 2871N-linked (GlcNAc...); by hostSequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

MINTiMINT-237377.

Structurei

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini26 – 340315Virion surfaceSequence AnalysisAdd
BLAST
Topological domaini362 – 39433IntravirionSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei341 – 36121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni26 – 5732Interaction with TNFRSF14Add
BLAST
Regioni261 – 30545ProfusionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi269 – 33769Pro-richAdd
BLAST
Compositional biasi365 – 38117Arg/Lys-rich (highly basic; probably serves to anchor the glycoprotein in the membrane)Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Signal, Transmembrane, Transmembrane helix

Family and domain databases

InterProiIPR002896. Herpes_glycop_dom.
[Graphical view]
PfamiPF01537. Herpes_glycop_D. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

A1Z0Q5-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MGGAAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVL
60 70 80 90 100
DQLTDPPGVR RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS
110 120 130 140 150
EAPQIVRGAS EDVRKQPYNL TIAWFRMGGN CAIPITVMEY TECSYNKSLG
160 170 180 190 200
ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA PAFETAGTYL RLVKINDWTE
210 220 230 240 250
ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD SIGMLPRFIP
260 270 280 290 300
ENQRTVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED
310 320 330 340 350
SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS
360 370 380 390
LLAALVICGI VYWMHRRTRK APKRIRLPHI REDDQPSSHQ PLFY
Length:394
Mass (Da):43,317
Last modified:September 22, 2009 - v2
Checksum:i905A0F0F1953CB7F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301A → V in AAA19630. (PubMed:17604805)Curated
Sequence conflicti30 – 301A → V in ABM52980. (PubMed:8116256)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti52 – 521Q → P in strain: Mutant rid1 and Isolate KOSc(AC3,AC6); interference resistant.
Natural varianti52 – 521Q → R in strain: Mutant rid2; interference resistant.

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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

ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-237377.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR002896. Herpes_glycop_dom.
[Graphical view ]
Pfami PF01537. Herpes_glycop_D. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiGD_HHV1K
AccessioniPrimary (citable) accession number: A1Z0Q5
Secondary accession number(s): Q05060, Q69081, Q69082
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 22, 2009
Last modified: October 29, 2014
This is version 33 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3