GD_HHV11
ID GD_HHV11 Reviewed; 394 AA.
AC Q69091; B9VQK0; O12544; O12833; P03171; Q09I71;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; ORFNames=US6;
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=2984429; DOI=10.1016/0022-2836(85)90320-1;
RA McGeoch D.J., Dolan A., Donald S., Rixon F.J.;
RT "Sequence determination and genetic content of the short unique region in
RT the genome of herpes simplex virus type 1.";
RL J. Mol. Biol. 181:1-13(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2846760; DOI=10.1099/0022-1317-69-11-2831;
RA Perry L.J., McGeoch D.J.;
RT "The DNA sequences of the long repeat region and adjoining parts of the
RT long unique region in the genome of herpes simplex virus type 1.";
RL J. Gen. Virol. 69:2831-2846(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 DISULFIDE BONDS.
RX PubMed=1328685; DOI=10.1128/jvi.66.11.6668-6685.1992;
RA Long D., Wilcox W.C., Abrams W.R., Cohen G.H., Eisenberg R.J.;
RT "Disulfide bond structure of glycoprotein D of herpes simplex virus types 1
RT and 2.";
RL J. Virol. 66:6668-6685(1992).
RN [6]
RP IDENTIFICATION IN A COMPLEX WITH GB AND GH.
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 [7]
RP LACK OF INTERACTION WITH VP22.
RX PubMed=19279114; DOI=10.1128/jvi.00069-09;
RA Stylianou J., Maringer K., Cook R., Bernard E., Elliott G.;
RT "Virion incorporation of the herpes simplex virus type 1 tegument protein
RT VP22 occurs via glycoprotein E-specific recruitment to the late secretory
RT pathway.";
RL J. Virol. 83:5204-5218(2009).
RN [8]
RP INTERACTION WITH HOST RSAD2, AND SUBCELLULAR LOCATION.
RX PubMed=31921110; DOI=10.3389/fimmu.2019.02810;
RA Li M., Liao Z., Xu Z., Zou X., Wang Y., Peng H., Li Y., Ou X., Deng Y.,
RA Guo Y., Gan W., Peng T., Chen D., Cai M.;
RT "The Interaction Mechanism Between Herpes Simplex Virus 1 Glycoprotein D
RT and Host Antiviral Protein Viperin.";
RL Front. Immunol. 10:2810-2810(2019).
CC -!- FUNCTION: Envelope glycoprotein that binds to the potential host cell
CC entry receptors TNFRSF14/HVEM, NECTIN1 and 3-O-sulfated heparan sulfate
CC (By similarity). May trigger fusion with host membrane, by recruiting
CC the fusion machinery composed of gB and gH/gL. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with host receptor TNFRSF14.
CC Interacts with host receptor NECTIN1 (By similarity). Interacts (via
CC profusion domain) with gB; this interaction occurs in the absence of
CC gH/gL. Interacts (via profusion domain) with gH/gL heterodimer; this
CC interaction occurs in the absence of gB. Associates with the gB-gH/gL-
CC gD complex (Probable). Interacts (via C-terminus) with UL11 tegument
CC protein. Interacts (via C-terminus) with VP22 tegument protein (By
CC similarity); this interaction has been demonstrated in other strains,
CC but might be very weak since PubMed:19279114 has failed to see it.
CC Interacts with host RSAD2 (PubMed:31921110). {ECO:0000250,
CC ECO:0000269|PubMed:17670828, ECO:0000269|PubMed:31921110, ECO:0000305}.
CC -!- INTERACTION:
CC Q69091; Q9GL76: NECTIN1; Xeno; NbExp=4; IntAct=EBI-11691180, EBI-11691211;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host Golgi apparatus
CC {ECO:0000269|PubMed:31921110}. Note=During virion morphogenesis, this
CC protein probably accumulates in the endosomes and trans-Golgi where
CC secondary envelopment occurs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein D family.
CC {ECO:0000305}.
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DR EMBL; X14112; CAA32283.1; -; Genomic_DNA.
DR EMBL; L00036; AAA96682.1; -; Genomic_DNA.
DR EMBL; DQ889502; ABI63524.1; -; Genomic_DNA.
DR EMBL; FJ593289; ACM62295.1; -; Genomic_DNA.
DR PIR; A03730; VGBE17.
DR RefSeq; YP_009137141.1; NC_001806.2.
DR PDB; 3U82; X-ray; 3.16 A; A=26-310.
DR PDBsum; 3U82; -.
DR BMRB; Q69091; -.
DR SMR; Q69091; -.
DR IntAct; Q69091; 2.
DR ChEMBL; CHEMBL2364696; -.
DR DrugCentral; Q69091; -.
DR TCDB; 1.G.10.1.1; the herpes simplex virus membrane fusion complex (hsv-mfc) family.
DR PRIDE; Q69091; -.
DR DNASU; 2703444; -.
DR GeneID; 2703444; -.
DR KEGG; vg:2703444; -.
DR PRO; PR:Q69091; -.
DR Proteomes; UP000009294; Genome.
DR Proteomes; UP000180652; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IDA:CAFA.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR InterPro; IPR002896; Herpes_glycop_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR Pfam; PF01537; Herpes_glycop_D; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Host Golgi apparatus;
KW Host-virus interaction; Membrane; Metal-binding; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral attachment to host entry receptor; Viral envelope protein; Virion;
KW Virus entry into host cell; Zinc.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..394
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000038213"
FT TOPO_DOM 26..340
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 362..394
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 26..57
FT /note="Interaction with TNFRSF14"
FT /evidence="ECO:0000250"
FT REGION 261..305
FT /note="Profusion"
FT REGION 275..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..394
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 64
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 287
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 91..214
FT /evidence="ECO:0000269|PubMed:1328685"
FT DISULFID 131..227
FT /evidence="ECO:0000269|PubMed:1328685"
FT DISULFID 143..152
FT /evidence="ECO:0000269|PubMed:1328685"
FT VARIANT 25
FT /note="S -> G"
FT VARIANT 30
FT /note="V -> A (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 218
FT /note="L -> I (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 353
FT /note="A -> V (in strain: Nonneuroinvasive mutant HF10)"
FT VARIANT 367
FT /note="H -> R (in strain: Nonneuroinvasive mutant HF10)"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3U82"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3U82"
FT STRAND 198..212
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:3U82"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:3U82"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:3U82"
SQ SEQUENCE 394 AA; 43347 MW; 94B52171F355F6FC CRC64;
MGGAAARLGA VILFVVIVGL HGVRSKYALV DASLKMADPN RFRGKDLPVL DQLTDPPGVR
RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS EAPQIVRGAS EDVRKQPYNL
TIAWFRMGGN CAIPITVMEY TECSYNKSLG ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA
PAFETAGTYL RLVKINDWTE ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD
SIGMLPRFIP ENQRTVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED
SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS LLAALVICGI
VYWMRRHTQK APKRIRLPHI REDDQPSSHQ PLFY
