GD_HHV23
ID GD_HHV23 Reviewed; 393 AA.
AC P03172; A7U8A6;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; Synonyms=US6;
OS Human herpesvirus 2 (strain 333) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10313;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate Lasky;
RX PubMed=6321120; DOI=10.1089/dna.1.1984.3.23;
RA Lasky L.A., Dowbenko D.J.;
RT "DNA sequence analysis of the type-common glycoprotein-D genes of herpes
RT simplex virus types 1 and 2.";
RL DNA 3:23-29(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6323270; DOI=10.1016/0378-1119(83)90203-2;
RA Watson R.J.;
RT "DNA sequence of the Herpes simplex virus type 2 glycoprotein D gene.";
RL Gene 26:307-312(1983).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate BBKC, Isolate CAMB4, Isolate MMA, and Isolate WTW1A;
RX PubMed=9652417; DOI=10.1086/515590;
RA Terhune S.S., Coleman K.T., Sekulovich R., Burke R.L., Spear P.G.;
RT "Limited variability of glycoprotein gene sequences and neutralizing
RT targets in herpes simplex virus type 2 isolates and stability on passage in
RT cell culture.";
RL J. Infect. Dis. 178:8-15(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17928351; DOI=10.1128/jvi.01528-07;
RA Adamiak B., Ekblad M., Bergstrom T., Ferro V., Trybala E.;
RT "Herpes simplex virus type 2 glycoprotein G is targeted by the sulfated
RT oligo- and polysaccharide inhibitors of virus attachment to cells.";
RL J. Virol. 81:13424-13434(2007).
RN [5]
RP PROTEIN SEQUENCE OF 139-152 AND 245-259, AND 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 INTERACTION WITH HUMAN RECEPTORS TNFRSF14 AND NECTIN1.
RX PubMed=9696799; DOI=10.1128/jvi.72.9.7064-7074.1998;
RA Krummenacher C., Nicola A.V., Whitbeck J.C., Lou H., Hou W., Lambris J.D.,
RA Geraghty R.J., Spear P.G., Cohen G.H., Eisenberg R.J.;
RT "Herpes simplex virus glycoprotein D can bind to poliovirus receptor-
RT related protein 1 or herpesvirus entry mediator, two structurally unrelated
RT mediators of virus entry.";
RL J. Virol. 72:7064-7074(1998).
RN [7]
RP INTERACTION WITH HUMAN RECEPTOR NECTIN2.
RX PubMed=11602758; DOI=10.1128/jvi.75.22.11185-11195.2001;
RA Martinez W.M., Spear P.G.;
RT "Structural features of nectin-2 (HveB) required for herpes simplex virus
RT entry.";
RL J. Virol. 75:11185-11195(2001).
CC -!- FUNCTION: Envelope glycoprotein that binds to the potential host cell
CC entry receptors TNFRSF14/HVEM and NECTIN1. May trigger fusion with host
CC membrane, by recruiting the fusion machinery composed of gB and gH/gL
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with host receptor
CC TNFRSF14. Interacts with host receptor NECTIN1. Interacts with host
CC receptor NECTIN2. Interacts (via profusion domain) with gB; this
CC interaction occurs in the absence of gH/gL. Interacts (via profusion
CC domain) with gH/gL heterodimer; this interaction occurs in the absence
CC of gB. Associates with the gB-gH/gL-gD complex. Interacts (via C-
CC terminus) with UL11 tegument protein (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. 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; K02373; AAA45842.1; -; Genomic_DNA.
DR EMBL; K01408; AAA45841.1; -; Genomic_DNA.
DR EMBL; U12180; AAB60552.1; -; Genomic_DNA.
DR EMBL; U12182; AAB60554.1; -; Genomic_DNA.
DR EMBL; U12183; AAB60555.1; -; Genomic_DNA.
DR EMBL; AF021342; AAB72102.1; -; Genomic_DNA.
DR EMBL; EU018124; ABU45461.1; -; Genomic_DNA.
DR EMBL; EU018125; ABU45462.1; -; Genomic_DNA.
DR PIR; A03731; VGBED2.
DR PIR; A03732; VGBE33.
DR PDB; 4MYV; X-ray; 1.80 A; A/B=26-310.
DR PDB; 4MYW; X-ray; 3.19 A; A/C=26-310.
DR PDBsum; 4MYV; -.
DR PDBsum; 4MYW; -.
DR SMR; P03172; -.
DR PRIDE; P03172; -.
DR ABCD; P03172; 1 sequenced antibody.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046814; P:coreceptor-mediated virion attachment to host cell; IMP:BHF-UCL.
DR GO; GO:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IDA:BHF-UCL.
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; Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Metal-binding; Signal; Transmembrane;
KW 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..393
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000038217"
FT TOPO_DOM 26..339
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 364..393
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 25..57
FT /note="Interaction with TNFRSF14"
FT REGION 261..305
FT /note="Profusion"
FT /evidence="ECO:0000250"
FT REGION 274..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..292
FT /note="Polar residues"
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 52
FT /note="R -> Q (in strain: Isolate Lasky, Isolate BBKC,
FT Isolate CAM4B, Isolate WTW1A and Isolate MMA)"
FT VARIANT 249
FT /note="I -> T (in strain: Isolate Lasky)"
FT VARIANT 337
FT /note="S -> A (in strain: Isolate Lasky)"
FT VARIANT 353
FT /note="V -> A (in strain: Isolate Lasky, Isolate BBKC,
FT Isolate CAM4B, Isolate WTW1A and Isolate MMA)"
FT VARIANT 367..369
FT /note="AQM -> RSV (in strain: Isolate Lasky)"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:4MYW"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:4MYV"
FT HELIX 102..105
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 110..127
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 132..147
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:4MYV"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:4MYW"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:4MYW"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:4MYV"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:4MYV"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:4MYV"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:4MYV"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:4MYV"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:4MYV"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:4MYW"
FT TURN 263..265
FT /evidence="ECO:0007829|PDB:4MYW"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:4MYW"
SQ SEQUENCE 393 AA; 43220 MW; 6BA446D37666B9CB CRC64;
MGRLTSGVGT AALLVVAVGL RVVCAKYALA DPSLKMADPN RFRGKNLPVL DRLTDPPGVK
RVYHIQPSLE DPFQPPSIPI TVYYAVLERA CRSVLLHAPS EAPQIVRGAS DEARKHTYNL
TIAWYRMGDN CAIPITVMEY TECPYNKSLG VCPIRTQPRW SYYDSFSAVS EDNLGFLMHA
PAFETAGTYL RLVKINDWTE ITQFILEHRA RASCKYALPL RIPPAACLTS KAYQQGVTVD
SIGMLPRFIP ENQRTVALYS LKIAGWHGPK PPYTSTLLPP ELSDTTNATQ PELVPEDPED
SALLEDPAGT VSSQIPPNWH IPSIQDVAPH HAPAAPSNPG LIIGALAGST LAVLVIGGIA
FWVRRRAQMA PKRLRLPHIR DDDAPPSHQP LFY
