P06477 (GH_HHV11) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Envelope glycoprotein H
Short name=gH

Gene names

Name:	gH
ORF Names:	UL22

Organism

Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) [Reference proteome]

Taxonomic identifier

10299 [NCBI]

Taxonomic lineage

Viruses › dsDNA viruses, no RNA stage › Herpesvirales › Herpesviridae › Alphaherpesvirinae › Simplexvirus › Human herpesvirus 1

Virus host

Homo sapiens (Human) [TaxID: 9606]

Protein attributes

Sequence length	838 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	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
Cellular component	Host cell membrane Host endosome Host membrane Membrane Viral envelope protein Virion
Domain	Signal Transmembrane Transmembrane helix
Ligand	Sialic acid
PTM	Glycoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	viral entry into host cell via membrane fusion with the plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	host cell endosome membrane Inferred from electronic annotation. Source: UniProtKB-SubCell host cell plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW viral envelope Inferred from electronic annotation. Source: UniProtKB-KW virion membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Potential

Chain

21 – 838

818

Envelope glycoprotein H

PRO_0000038235

Regions

Topological domain

21 – 803

783

Virion surface Potential

Transmembrane

804 – 824

21

Helical; Potential

Topological domain

825 – 838

14

Intravirion Potential

Region

259 – 323

65

Interaction with gL

Amino acid modifications

Glycosylation

73

1

N-linked (GlcNAc...); by host Potential

Glycosylation

120

1

N-linked (GlcNAc...); by host Potential

Glycosylation

216

1

N-linked (GlcNAc...); by host Potential

Glycosylation

332

1

N-linked (GlcNAc...); by host Potential

Glycosylation

437

1

N-linked (GlcNAc...); by host Potential

Glycosylation

670

1

N-linked (GlcNAc...); by host Potential

Glycosylation

784

1

N-linked (GlcNAc...); by host Potential

Natural variations

Natural variant

15

1

V → A in strain: Nonneuroinvasive mutant HF10.

Natural variant

138

1

S → A in strain: Nonneuroinvasive mutant HF10.

Natural variant

150

1

A → T in strain: Nonneuroinvasive mutant HF10.

Natural variant

284

1

V → A in strain: Nonneuroinvasive mutant HF10.

Secondary structure

1

.

.

.

.

.

.

838

Helix Strand Turn

Details...

Helix

627 – 633

7

Helix

634 – 636

3

Helix

638 – 641

4

Sequences

	Sequence		Length	Mass (Da)
	P06477 [UniParc]. Last modified January 1, 1988. Version 1. Checksum: 9AFDE1E690BD498F	FASTA	838	90,366
	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

References

	« Hide 'large scale' referencesShow '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.

PIR

VGBEG1. A24018.

RefSeq

NP_044623.1. NC_001806.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2LQY	NMR	-	A	625-644	[»]

ModBase

Search...

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

2703373.

Phylogenomic databases

ProtClustDB

PHA3294.

Family and domain databases

InterPro

IPR003493. Herpes_gH.
[Graphical view]

Pfam

PF02489. Herpes_glycop_H. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

GH_HHV11

Accession

Primary (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:	April 3, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Viral Protein Annotation Program