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P06477 (GH_HHV11) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 H

Short name=gH
Gene names
Name:gH
ORF Names:UL22
OrganismHuman herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]
Taxonomic identifier10299 [NCBI]
Taxonomic lineageVirusesdsDNA viruses, no RNA stageHerpesviralesHerpesviridaeAlphaherpesvirinaeSimplexvirus
Virus hostHomo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length838 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8

Subunit structure

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. Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

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

Post-translational modification

N-glycosylated, O-glycosylated, and sialylated Probable. Ref.5

Sequence similarities

Belongs to the herpesviridae glycoprotein H family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 838818Envelope glycoprotein H
PRO_0000038235

Regions

Topological domain21 – 803783Virion surface Potential
Transmembrane804 – 82421Helical; Potential
Topological domain825 – 83814Intravirion Potential
Region259 – 32365Interaction with gL

Amino acid modifications

Glycosylation731N-linked (GlcNAc...); by host Potential
Glycosylation1201N-linked (GlcNAc...); by host Potential
Glycosylation2161N-linked (GlcNAc...); by host Potential
Glycosylation3321N-linked (GlcNAc...); by host Potential
Glycosylation4371N-linked (GlcNAc...); by host Potential
Glycosylation6701N-linked (GlcNAc...); by host Potential
Glycosylation7841N-linked (GlcNAc...); by host Potential

Natural variations

Natural variant151V → A in strain: Nonneuroinvasive mutant HF10.
Natural variant1381S → A in strain: Nonneuroinvasive mutant HF10.
Natural variant1501A → T in strain: Nonneuroinvasive mutant HF10.
Natural variant2841V → A in strain: Nonneuroinvasive mutant HF10.

Secondary structure

...... 838
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06477 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 9AFDE1E690BD498F

FASTA83890,366
        10         20         30         40         50         60 
MGNGLWFVGV IILGVAWGQV HDWTEQTDPW FLDGLGMDRM YWRDTNTGRL WLPNTPDPQK 

        70         80         90        100        110        120 
PPRGFLAPPD ELNLTTASLP LLRWYEERFC FVLVTTAEFP RDPGQLLYIP KTYLLGRPPN 

       130        140        150        160        170        180 
ASLPAPTTVE PTAQPPPSVA PLKGLLHNPA ASVLLRSRAW VTFSAVPDPE ALTFPRGDNV 

       190        200        210        220        230        240 
ATASHPSGPR DTPPPRPPVG ARRHPTTELD ITHLHNASTT WLATRGLLRS PGRYVYFSPS 

       250        260        270        280        290        300 
ASTWPVGIWT TGELVLGCDA ALVRARYGRE FMGLVISMHD SPPVEVMVVP AGQTLDRVGD 

       310        320        330        340        350        360 
PADENPPGAL PGPPGGPRYR VFVLGSLTRA DNGSALDALR RVGGYPEEGT NYAQFLSRAY 

       370        380        390        400        410        420 
AEFFSGDAGA EQGPRPPLFW RLTGLLATSG FAFVNAAHAN GAVCLSDLLG FLAHSRALAG 

       430        440        450        460        470        480 
LAARGAAGCA ADSVFFNVSV LDPTARLQLE ARLQHLVAEI LEREQSLALH ALGYQLAFVL 

       490        500        510        520        530        540 
DSPSAYDAVA PSAAHLIDAL YAEFLGGRVL TTPVVHRALF YASAVLRQPF LAGVPSAVQR 

       550        560        570        580        590        600 
ERARRSLLIA SALCTSDVAA ATNADLRTAL ARADHQKTLF WLPDHFSPCA ASLRFDLDES 

       610        620        630        640        650        660 
VFILDALAQA TRSETPVEVL AQQTHGLAST LTRWAHYNAL IRAFVPEASH RCGGQSANVE 

       670        680        690        700        710        720 
PRILVPITHN ASYVVTHSPL PRGIGYKLTG VDVRRPLFLT YLTATCEGST RDIESKRLVR 

       730        740        750        760        770        780 
TQNQRDLGLV GAVFMRYTPA GEVMSVLLVD TDNTQQQIAA GPTEGAPSVF SSDVPSTALL 

       790        800        810        820        830 
LFPNGTVIHL LAFDTQPVAA IAPGFLAASA LGVVMITAAL AGILKVLRTS VPFFWRRE 

« Hide

References

« Hide 'large scale' references
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X03896 Genomic DNA. Translation: CAA27534.1.
X14112 Genomic DNA. Translation: CAA32335.1.
DQ889502 Genomic DNA. Translation: ABI63484.1.
FJ593289 Genomic DNA. Translation: ACM62244.1.
PIRVGBEG1. A24018.
RefSeqNP_044623.1. NC_001806.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LQYNMR-A625-644[»]
ModBaseSearch...
MobiDBSearch...

Chemistry

ChEMBLCHEMBL2364696.

Protein family/group databases

TCDB1.G.10.1.1. the herpes simplex virus membrane fusion complex (hsv-mfc) family.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2703373.

Family and domain databases

InterProIPR003493. Herpes_gH.
[Graphical view]
PfamPF02489. Herpes_glycop_H. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGH_HHV11
AccessionPrimary (citable) accession number: P06477
Secondary accession number(s): B9VQE9, Q09IB1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: May 14, 2014
This is version 74 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references