GD_HHV2H
ID GD_HHV2H Reviewed; 393 AA.
AC Q69467; O12514;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; ORFNames=US6;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3027242; DOI=10.1099/0022-1317-68-1-19;
RA McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT "DNA sequence and genetic content of the HindIII l region in the short
RT unique component of the herpes simplex virus type 2 genome: identification
RT of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL J. Gen. Virol. 68:19-38(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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; Z86099; CAB06713.1; -; Genomic_DNA.
DR PIR; E43674; E43674.
DR RefSeq; YP_009137218.1; NC_001798.2.
DR PDB; 3W9E; X-ray; 2.30 A; C=1-300.
DR PDBsum; 3W9E; -.
DR SMR; Q69467; -.
DR PRIDE; Q69467; -.
DR DNASU; 1487358; -.
DR GeneID; 1487358; -.
DR KEGG; vg:1487358; -.
DR Proteomes; UP000001874; Genome.
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: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-virus interaction;
KW Membrane; Metal-binding; Reference proteome; 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_0000385470"
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..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:0000250|UniProtKB:P57083"
FT DISULFID 131..227
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 143..152
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 81..87
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 132..143
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:3W9E"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:3W9E"
FT STRAND 198..212
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 230..236
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 239..242
FT /evidence="ECO:0007829|PDB:3W9E"
FT HELIX 250..263
FT /evidence="ECO:0007829|PDB:3W9E"
SQ SEQUENCE 393 AA; 43192 MW; 9759B5C1847AF828 CRC64;
MGRLTSGVGT AALLVVAVGL RVVCAKYALA DPSLKMADPN RFRGKNLPVL DQLTDPPGVK
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
