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A1Z0Q5

- GD_HHV1K

UniProt

A1Z0Q5 - GD_HHV1K

Protein

Envelope glycoprotein D

Gene

gD

Organism
Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 32 (01 Oct 2014)
      Sequence version 2 (22 Sep 2009)
      Previous versions | rss
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    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

    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
    3. virion membrane Source: UniProtKB-SubCell

    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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    MGGAAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVL    50
    DQLTDPPGVR RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS 100
    EAPQIVRGAS EDVRKQPYNL TIAWFRMGGN CAIPITVMEY TECSYNKSLG 150
    ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA PAFETAGTYL RLVKINDWTE 200
    ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD SIGMLPRFIP 250
    ENQRTVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED 300
    SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS 350
    LLAALVICGI VYWMHRRTRK APKRIRLPHI REDDQPSSHQ PLFY 394
    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 1, 2014
    This is version 32 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