GH_HHV11
ID GH_HHV11 Reviewed; 838 AA.
AC P06477; B9VQE9; Q09IB1;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Envelope glycoprotein H {ECO:0000255|HAMAP-Rule:MF_04033};
DE Short=gH {ECO:0000255|HAMAP-Rule:MF_04033};
DE Flags: Precursor;
GN Name=gH {ECO:0000255|HAMAP-Rule:MF_04033}; ORFNames=UL22;
OS Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10299;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3012465; DOI=10.1093/nar/14.10.4281;
RA McGeoch D.J., Davison A.J.;
RT "DNA sequence of the herpes simplex virus type 1 gene encoding glycoprotein
RT gH, and identification of homologues in the genomes of varicella-zoster
RT virus and Epstein-Barr virus.";
RL Nucleic Acids Res. 14:4281-4292(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA Perry L.J., Scott J.E., Taylor P.;
RT "The complete DNA sequence of the long unique region in the genome of
RT herpes simplex virus type 1.";
RL J. Gen. Virol. 69:1531-1574(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nonneuroinvasive mutant HF10;
RX PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT "Determination and analysis of the DNA sequence of highly attenuated herpes
RT simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL Microbes Infect. 9:142-149(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17 syn+;
RA Cunningham C., Davison A.J.;
RT "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP INTERACTION WITH GL, AND GLYCOSYLATION.
RC STRAIN=KOS;
RX PubMed=9621073; DOI=10.1128/jvi.72.7.6092-6103.1998;
RA Peng T., Ponce de Leon M., Novotny M.J., Jiang H., Lambris J.D., Dubin G.,
RA Spear P.G., Cohen G.H., Eisenberg R.J.;
RT "Structural and antigenic analysis of a truncated form of the herpes
RT simplex virus glycoprotein gH-gL complex.";
RL J. Virol. 72:6092-6103(1998).
RN [6]
RP INTERACTION WITH GL.
RX PubMed=12767993; DOI=10.1128/jvi.77.12.6731-6742.2003;
RA Cairns T.M., Milne R.S., Ponce-de-Leon M., Tobin D.K., Cohen G.H.,
RA Eisenberg R.J.;
RT "Structure-function analysis of herpes simplex virus type 1 gD and gH-gL:
RT clues from gDgH chimeras.";
RL J. Virol. 77:6731-6742(2003).
RN [7]
RP INTERACTION WITH VP16.
RC STRAIN=SC16;
RX PubMed=14675620; DOI=10.1016/j.virol.2003.08.023;
RA Gross S.T., Harley C.A., Wilson D.W.;
RT "The cytoplasmic tail of Herpes simplex virus glycoprotein H binds to the
RT tegument protein VP16 in vitro and in vivo.";
RL Virology 317:1-12(2003).
RN [8]
RP FUNCTION.
RX PubMed=17548810; DOI=10.1073/pnas.0703790104;
RA Farnsworth A., Wisner T.W., Webb M., Roller R.J., Cohen G.H.,
RA Eisenberg R.J., Johnson D.C.;
RT "Herpes simplex virus glycoproteins gB and gH function in fusion between
RT the virion envelope and the outer nuclear membrane.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:10187-10192(2007).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH GB AND GD.
RX PubMed=17670828; DOI=10.1128/jvi.01343-07;
RA Avitabile E., Forghieri C., Campadelli-Fiume G.;
RT "Complexes between herpes simplex virus glycoproteins gD, gB, and gH
RT detected in cells by complementation of split enhanced green fluorescent
RT protein.";
RL J. Virol. 81:11532-11537(2007).
RN [10]
RP INTERACTION OF GH/GL HETERODIMER WITH GB.
RC STRAIN=KOS;
RX PubMed=18003913; DOI=10.1073/pnas.0707452104;
RA Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H.,
RA Eisenberg R.J.;
RT "Bimolecular complementation reveals that glycoproteins gB and gH/gL of
RT herpes simplex virus interact with each other during cell fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007).
CC -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for
CC the fusion of viral and plasma membranes leading to virus entry into
CC the host cell. Following initial binding to host receptor, membrane
CC fusion is mediated by the fusion machinery composed of gB and the
CC heterodimer gH/gL. May also be involved in the fusion between the
CC virion envelope and the outer nuclear membrane during virion
CC morphogenesis. {ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:17548810}.
CC -!- SUBUNIT: Interacts with glycoprotein L (gL); this interaction is
CC necessary for the correct processing and cell surface expression of gH.
CC The heterodimer gH/gL seems to interact with gB trimers during fusion
CC (By similarity). Associates with the gB-gH/gL-gD complex (Probable).
CC Interacts with VP16. {ECO:0000255|HAMAP-Rule:MF_04033,
CC ECO:0000269|PubMed:12767993, ECO:0000269|PubMed:14675620,
CC ECO:0000269|PubMed:17670828, ECO:0000269|PubMed:18003913,
CC ECO:0000269|PubMed:9621073, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04033}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04033}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04033};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04033}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04033}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04033}.
CC -!- PTM: N-glycosylated, O-glycosylated, and sialylated.
CC {ECO:0000255|HAMAP-Rule:MF_04033, ECO:0000305|PubMed:9621073}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein H family.
CC {ECO:0000255|HAMAP-Rule:MF_04033}.
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DR EMBL; X03896; CAA27534.1; -; Genomic_DNA.
DR EMBL; X14112; CAA32335.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63484.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62244.1; -; Genomic_DNA.
DR PIR; A24018; VGBEG1.
DR RefSeq; YP_009137096.1; NC_001806.2.
DR PDB; 2LQY; NMR; -; A=625-644.
DR PDBsum; 2LQY; -.
DR BMRB; P06477; -.
DR SMR; P06477; -.
DR BioGRID; 971414; 1.
DR ChEMBL; CHEMBL2364696; -.
DR DrugCentral; P06477; -.
DR TCDB; 1.G.10.1.1; the herpes simplex virus membrane fusion complex (hsv-mfc) family.
DR PRIDE; P06477; -.
DR GeneID; 24271466; -.
DR KEGG; vg:24271466; -.
DR PRO; PR:P06477; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.3190; -; 1.
DR HAMAP; MF_04033; HSV_GH; 1.
DR InterPro; IPR003493; Herpes_gH.
DR InterPro; IPR035305; Herpes_glycoH_C.
DR InterPro; IPR038172; Herpes_glycoH_C_sf.
DR Pfam; PF17488; Herpes_glycoH_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host endosome; Host membrane; Membrane;
KW Reference proteome; Sialic acid; Signal; Transmembrane;
KW Transmembrane helix; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CHAIN 19..838
FT /note="Envelope glycoprotein H"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT /id="PRO_0000436656"
FT TOPO_DOM 19..803
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT TOPO_DOM 825..838
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT REGION 174..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 259..323
FT /note="Interaction with gL"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 332
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 437
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 670
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT CARBOHYD 784
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04033"
FT VARIANT 15
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 138
FT /note="S -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 150
FT /note="A -> T (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 284
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT HELIX 627..633
FT /evidence="ECO:0007829|PDB:2LQY"
FT HELIX 634..636
FT /evidence="ECO:0007829|PDB:2LQY"
FT HELIX 638..641
FT /evidence="ECO:0007829|PDB:2LQY"
SQ SEQUENCE 838 AA; 90366 MW; 9AFDE1E690BD498F CRC64;
MGNGLWFVGV IILGVAWGQV HDWTEQTDPW FLDGLGMDRM YWRDTNTGRL WLPNTPDPQK
PPRGFLAPPD ELNLTTASLP LLRWYEERFC FVLVTTAEFP RDPGQLLYIP KTYLLGRPPN
ASLPAPTTVE PTAQPPPSVA PLKGLLHNPA ASVLLRSRAW VTFSAVPDPE ALTFPRGDNV
ATASHPSGPR DTPPPRPPVG ARRHPTTELD ITHLHNASTT WLATRGLLRS PGRYVYFSPS
ASTWPVGIWT TGELVLGCDA ALVRARYGRE FMGLVISMHD SPPVEVMVVP AGQTLDRVGD
PADENPPGAL PGPPGGPRYR VFVLGSLTRA DNGSALDALR RVGGYPEEGT NYAQFLSRAY
AEFFSGDAGA EQGPRPPLFW RLTGLLATSG FAFVNAAHAN GAVCLSDLLG FLAHSRALAG
LAARGAAGCA ADSVFFNVSV LDPTARLQLE ARLQHLVAEI LEREQSLALH ALGYQLAFVL
DSPSAYDAVA PSAAHLIDAL YAEFLGGRVL TTPVVHRALF YASAVLRQPF LAGVPSAVQR
ERARRSLLIA SALCTSDVAA ATNADLRTAL ARADHQKTLF WLPDHFSPCA ASLRFDLDES
VFILDALAQA TRSETPVEVL AQQTHGLAST LTRWAHYNAL IRAFVPEASH RCGGQSANVE
PRILVPITHN ASYVVTHSPL PRGIGYKLTG VDVRRPLFLT YLTATCEGST RDIESKRLVR
TQNQRDLGLV GAVFMRYTPA GEVMSVLLVD TDNTQQQIAA GPTEGAPSVF SSDVPSTALL
LFPNGTVIHL LAFDTQPVAA IAPGFLAASA LGVVMITAAL AGILKVLRTS VPFFWRRE
