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P06477

- GH_HHV11

UniProt

P06477 - GH_HHV11

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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

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini21 – 803783Virion surfaceSequence AnalysisAdd
BLAST
Transmembranei804 – 82421HelicalSequence AnalysisAdd
BLAST
Topological domaini825 – 83814IntravirionSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. host cell endosome Source: UniProtKB-KW
  2. host cell plasma membrane Source: UniProtKB-KW
  3. integral component of membrane Source: UniProtKB-KW
  4. viral envelope Source: UniProtKB-KW
Complete GO annotation...

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 – 6337Combined sources
Helixi634 – 6363Combined sources
Helixi638 – 6414Combined sources

3D structure databases

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

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

« Hide

        10         20         30         40         50
MGNGLWFVGV IILGVAWGQV HDWTEQTDPW FLDGLGMDRM YWRDTNTGRL
60 70 80 90 100
WLPNTPDPQK PPRGFLAPPD ELNLTTASLP LLRWYEERFC FVLVTTAEFP
110 120 130 140 150
RDPGQLLYIP KTYLLGRPPN ASLPAPTTVE PTAQPPPSVA PLKGLLHNPA
160 170 180 190 200
ASVLLRSRAW VTFSAVPDPE ALTFPRGDNV ATASHPSGPR DTPPPRPPVG
210 220 230 240 250
ARRHPTTELD ITHLHNASTT WLATRGLLRS PGRYVYFSPS ASTWPVGIWT
260 270 280 290 300
TGELVLGCDA ALVRARYGRE FMGLVISMHD SPPVEVMVVP AGQTLDRVGD
310 320 330 340 350
PADENPPGAL PGPPGGPRYR VFVLGSLTRA DNGSALDALR RVGGYPEEGT
360 370 380 390 400
NYAQFLSRAY AEFFSGDAGA EQGPRPPLFW RLTGLLATSG FAFVNAAHAN
410 420 430 440 450
GAVCLSDLLG FLAHSRALAG LAARGAAGCA ADSVFFNVSV LDPTARLQLE
460 470 480 490 500
ARLQHLVAEI LEREQSLALH ALGYQLAFVL DSPSAYDAVA PSAAHLIDAL
510 520 530 540 550
YAEFLGGRVL TTPVVHRALF YASAVLRQPF LAGVPSAVQR ERARRSLLIA
560 570 580 590 600
SALCTSDVAA ATNADLRTAL ARADHQKTLF WLPDHFSPCA ASLRFDLDES
610 620 630 640 650
VFILDALAQA TRSETPVEVL AQQTHGLAST LTRWAHYNAL IRAFVPEASH
660 670 680 690 700
RCGGQSANVE PRILVPITHN ASYVVTHSPL PRGIGYKLTG VDVRRPLFLT
710 720 730 740 750
YLTATCEGST RDIESKRLVR TQNQRDLGLV GAVFMRYTPA GEVMSVLLVD
760 770 780 790 800
TDNTQQQIAA GPTEGAPSVF SSDVPSTALL LFPNGTVIHL LAFDTQPVAA
810 820 830
IAPGFLAASA LGVVMITAAL AGILKVLRTS VPFFWRRE
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 77 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