GD_HHV1H
ID GD_HHV1H Reviewed; 393 AA.
AC P06476;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; Synonyms=US6;
OS Human herpesvirus 1 (strain HZT) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10305;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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).
CC -!- FUNCTION: Envelope glycoprotein that binds to the potential host cell
CC entry receptors TNFRSF14/HVEM, NECTIN1 and 3-O-sulfated heparan
CC sulfate. May trigger fusion with host membrane, by recruiting the
CC fusion machinery composed of gB and gH/gL (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer (By similarity). Interacts with host receptor
CC TNFRSF14. Interacts with host receptor NECTIN1. 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. Interacts (via C-terminus) with UL11 tegument protein (By
CC similarity). Interacts with host RSAD2 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC membrane protein {ECO:0000250}. Host Golgi apparatus
CC {ECO:0000250|UniProtKB:Q69091}. 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; K02372; AAA45786.1; -; Genomic_DNA.
DR BMRB; P06476; -.
DR SMR; P06476; -.
DR PRIDE; P06476; -.
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; 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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host Golgi apparatus; Host-virus interaction;
KW Membrane; Metal-binding; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral envelope protein; Virion; 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_0000038216"
FT TOPO_DOM 26..338
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..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 260..304
FT /note="Profusion"
FT /evidence="ECO:0000250"
FT REGION 273..300
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 239
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 118
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 286
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 90..213
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 130..226
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 142..151
FT /evidence="ECO:0000250|UniProtKB:P57083"
SQ SEQUENCE 393 AA; 43368 MW; 348E8D35BA4B6FE9 CRC64;
MGGAAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVL DQLTDPPGVR
RVYHIQAGLP NPFQPPSLPI TVYRRVERAC RSVLLNAPSE APQIVRGASE DVRKQPYNLT
IAWFRMGGNC AIPITVMEYT ECSYNKSLGA CPIRTQPRWN YYDSFSAVSE DNLGFLMHAP
AFETAGTYLR LVKINDWTEI TQFILEHRAK GSCKYTLPLR IPPSACLSPQ AYQQGVTVDS
IGMLPRFIPE NQRTVAVYSL KIAGWHGPRA PYTSTLLPPE LPETPNATQP ELAPEDPEDS
ALLEDPVGTV APQIPPNWHI PSIQDAATPY HPPATPNNMG LIAGAVGGSL LAALVICGIV
YWMRRRTRKA PKRIRLPHIR EDDQPSSHQP LFY
