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P06477

- GH_HHV11

UniProt

P06477 - GH_HHV11

Protein

Envelope glycoprotein H

Gene

gH

Organism
Human herpesvirus 1 (strain 17) (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 75 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    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. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis.1 Publication

    GO - Biological processi

    1. fusion of virus membrane with host plasma membrane Source: UniProtKB-KW

    Keywords - Biological processi

    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

    Keywords - Ligandi

    Sialic acid

    Protein family/group databases

    TCDBi1.G.10.1.1. the herpes simplex virus membrane fusion complex (hsv-mfc) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Envelope glycoprotein H
    Short name:
    gH
    Gene namesi
    Name:gH
    ORF Names:UL22
    OrganismiHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
    Taxonomic identifieri10299 [NCBI]
    Taxonomic lineageiVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
    Virus hostiHomo sapiens (Human) [TaxID: 9606]
    ProteomesiUP000009294: Genome

    Subcellular locationi

    Virion membrane By similarity; Single-pass type I membrane protein By similarity. Host cell membrane By similarity; Single-pass type I membrane protein By similarity. Host endosome 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. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN) By similarity.By similarity

    GO - Cellular componenti

    1. host cell endosome membrane Source: UniProtKB-SubCell
    2. host cell plasma membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. viral envelope Source: UniProtKB-KW
    5. virion membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Host cell membrane, Host endosome, Host membrane, Membrane, Viral envelope protein, Virion

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 838818Envelope glycoprotein HPRO_0000038235Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi73 – 731N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi120 – 1201N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi216 – 2161N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi332 – 3321N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi437 – 4371N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi670 – 6701N-linked (GlcNAc...); by hostSequence Analysis
    Glycosylationi784 – 7841N-linked (GlcNAc...); by hostSequence Analysis

    Post-translational modificationi

    N-glycosylated, O-glycosylated, and sialylated.1 Publication

    Keywords - PTMi

    Glycoprotein

    Interactioni

    Subunit structurei

    Interacts with glycoprotein L (gL); 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 Probable. Associates with the gB-gH/gL-gD complex Probable. Interacts with VP16.5 PublicationsCurated

    Structurei

    Secondary structure

    1
    838
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi627 – 6337
    Helixi634 – 6363
    Helixi638 – 6414

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2LQYNMR-A625-644[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini21 – 803783Virion surfaceSequence AnalysisAdd
    BLAST
    Topological domaini825 – 83814IntravirionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei804 – 82421HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni259 – 32365Interaction with gLAdd
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Family and domain databases

    InterProiIPR003493. Herpes_gH.
    [Graphical view]
    PfamiPF02489. Herpes_glycop_H. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P06477-1 [UniParc]FASTAAdd to Basket

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    MGNGLWFVGV IILGVAWGQV HDWTEQTDPW FLDGLGMDRM YWRDTNTGRL    50
    WLPNTPDPQK PPRGFLAPPD ELNLTTASLP LLRWYEERFC FVLVTTAEFP 100
    RDPGQLLYIP KTYLLGRPPN ASLPAPTTVE PTAQPPPSVA PLKGLLHNPA 150
    ASVLLRSRAW VTFSAVPDPE ALTFPRGDNV ATASHPSGPR DTPPPRPPVG 200
    ARRHPTTELD ITHLHNASTT WLATRGLLRS PGRYVYFSPS ASTWPVGIWT 250
    TGELVLGCDA ALVRARYGRE FMGLVISMHD SPPVEVMVVP AGQTLDRVGD 300
    PADENPPGAL PGPPGGPRYR VFVLGSLTRA DNGSALDALR RVGGYPEEGT 350
    NYAQFLSRAY AEFFSGDAGA EQGPRPPLFW RLTGLLATSG FAFVNAAHAN 400
    GAVCLSDLLG FLAHSRALAG LAARGAAGCA ADSVFFNVSV LDPTARLQLE 450
    ARLQHLVAEI LEREQSLALH ALGYQLAFVL DSPSAYDAVA PSAAHLIDAL 500
    YAEFLGGRVL TTPVVHRALF YASAVLRQPF LAGVPSAVQR ERARRSLLIA 550
    SALCTSDVAA ATNADLRTAL ARADHQKTLF WLPDHFSPCA ASLRFDLDES 600
    VFILDALAQA TRSETPVEVL AQQTHGLAST LTRWAHYNAL IRAFVPEASH 650
    RCGGQSANVE PRILVPITHN ASYVVTHSPL PRGIGYKLTG VDVRRPLFLT 700
    YLTATCEGST RDIESKRLVR TQNQRDLGLV GAVFMRYTPA GEVMSVLLVD 750
    TDNTQQQIAA GPTEGAPSVF SSDVPSTALL LFPNGTVIHL LAFDTQPVAA 800
    IAPGFLAASA LGVVMITAAL AGILKVLRTS VPFFWRRE 838
    Length:838
    Mass (Da):90,366
    Last modified:January 1, 1988 - v1
    Checksum:i9AFDE1E690BD498F
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti15 – 151V → A in strain: Nonneuroinvasive mutant HF10.
    Natural varianti138 – 1381S → A in strain: Nonneuroinvasive mutant HF10.
    Natural varianti150 – 1501A → T in strain: Nonneuroinvasive mutant HF10.
    Natural varianti284 – 2841V → A in strain: Nonneuroinvasive mutant HF10.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03896 Genomic DNA. Translation: CAA27534.1.
    X14112 Genomic DNA. Translation: CAA32335.1.
    DQ889502 Genomic DNA. Translation: ABI63484.1.
    FJ593289 Genomic DNA. Translation: ACM62244.1.
    PIRiA24018. VGBEG1.
    RefSeqiNP_044623.1. NC_001806.1.

    Genome annotation databases

    GeneIDi2703373.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03896 Genomic DNA. Translation: CAA27534.1 .
    X14112 Genomic DNA. Translation: CAA32335.1 .
    DQ889502 Genomic DNA. Translation: ABI63484.1 .
    FJ593289 Genomic DNA. Translation: ACM62244.1 .
    PIRi A24018. VGBEG1.
    RefSeqi NP_044623.1. NC_001806.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2LQY NMR - A 625-644 [» ]
    ModBasei Search...
    MobiDBi Search...

    Chemistry

    ChEMBLi CHEMBL2364696.

    Protein family/group databases

    TCDBi 1.G.10.1.1. the herpes simplex virus membrane fusion complex (hsv-mfc) family.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 2703373.

    Family and domain databases

    InterProi IPR003493. Herpes_gH.
    [Graphical view ]
    Pfami PF02489. Herpes_glycop_H. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "DNA sequence of the herpes simplex virus type 1 gene encoding glycoprotein gH, and identification of homologues in the genomes of varicella-zoster virus and Epstein-Barr virus."
      McGeoch D.J., Davison A.J.
      Nucleic Acids Res. 14:4281-4292(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "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].
    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. "Structural and antigenic analysis of a truncated form of the herpes simplex virus glycoprotein gH-gL complex."
      Peng T., Ponce de Leon M., Novotny M.J., Jiang H., Lambris J.D., Dubin G., Spear P.G., Cohen G.H., Eisenberg R.J.
      J. Virol. 72:6092-6103(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GL, GLYCOSYLATION.
      Strain: KOS.
    6. "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 GL.
    7. "The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the tegument protein VP16 in vitro and in vivo."
      Gross S.T., Harley C.A., Wilson D.W.
      Virology 317:1-12(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH VP16.
      Strain: SC16.
    8. "Herpes simplex virus glycoproteins gB and gH function in fusion between the virion envelope and the outer nuclear membrane."
      Farnsworth A., Wisner T.W., Webb M., Roller R.J., Cohen G.H., Eisenberg R.J., Johnson D.C.
      Proc. Natl. Acad. Sci. U.S.A. 104:10187-10192(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Complexes between herpes simplex virus glycoproteins gD, gB, and gH detected in cells by complementation of split enhanced green fluorescent protein."
      Avitabile E., Forghieri C., Campadelli-Fiume G.
      J. Virol. 81:11532-11537(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH GB AND GD.
    10. "Bimolecular complementation reveals that glycoproteins gB and gH/gL of herpes simplex virus interact with each other during cell fusion."
      Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H., Eisenberg R.J.
      Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION OF GH/GL HETERODIMER WITH GB.
      Strain: KOS.

    Entry informationi

    Entry nameiGH_HHV11
    AccessioniPrimary (citable) accession number: P06477
    Secondary accession number(s): B9VQE9, Q09IB1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 75 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programViral Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3