GD_HHV1F
ID GD_HHV1F Reviewed; 394 AA.
AC Q05059;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; ORFNames=US6;
OS Human herpesvirus 1 (strain F) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10304;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6289440; DOI=10.1126/science.6289440;
RA Watson R.J., Weis J.H., Salstrom J.S., Enquist L.W.;
RT "Herpes simplex virus type-1 glycoprotein D gene: nucleotide sequence and
RT expression in Escherichia coli.";
RL Science 218:381-384(1982).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dean H.J., Terhune S.S., Johnson R.M., Spear P.G.;
RT "Variability among strains of herpes simplex virus in sensitivity to gD-
RT mediated interference.";
RL Submitted (FEB-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION.
RX PubMed=15123804; DOI=10.1073/pnas.0401883101;
RA Cocchi F., Fusco D., Menotti L., Gianni T., Eisenberg R.J., Cohen G.H.,
RA Campadelli-Fiume G.;
RT "The soluble ectodomain of herpes simplex virus gD contains a membrane-
RT proximal pro-fusion domain and suffices to mediate virus entry.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7445-7450(2004).
RN [4]
RP INTERACTION WITH VP22 AND UL11 TEGUMENT PROTEINS.
RX PubMed=17035313; DOI=10.1128/jvi.01842-06;
RA Farnsworth A., Wisner T.W., Johnson D.C.;
RT "Cytoplasmic residues of herpes simplex virus glycoprotein gE required for
RT secondary envelopment and binding of tegument proteins VP22 and UL11 to gE
RT and gD.";
RL J. Virol. 81:319-331(2007).
RN [5]
RP INTERACTION WITH GB AND GH/GL.
RX PubMed=19386594; DOI=10.1074/jbc.m109.005728;
RA Gianni T., Amasio M., Campadelli-Fiume G.;
RT "Herpes simplex virus gD forms distinct complexes with fusion executors gB
RT and gH/gL in part through the C-terminal profusion domain.";
RL J. Biol. Chem. 284:17370-17382(2009).
RN [6]
RP SUBCELLULAR LOCATION.
RX PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA Loret S., Guay G., Lippe R.;
RT "Comprehensive characterization of extracellular herpes simplex virus type
RT 1 virions.";
RL J. Virol. 82:8605-8618(2008).
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, ECO:0000269|PubMed:15123804}.
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 (via C-terminus) with VP22 tegument protein;
CC this interaction might be very weak. Interacts with host RSAD2 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:17035313,
CC ECO:0000269|PubMed:19386594}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000269|PubMed:18596102};
CC Single-pass type I membrane protein {ECO:0000269|PubMed:18596102}. Host
CC Golgi apparatus {ECO:0000250|UniProtKB:Q69091}. Note=During virion
CC morphogenesis, this protein probably accumulates in the endosomes and
CC trans-Golgi where final envelopment occurs. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein D family.
CC {ECO:0000305}.
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DR EMBL; L09242; AAB59754.1; -; Genomic_DNA.
DR BMRB; Q05059; -.
DR SMR; Q05059; -.
DR ABCD; Q05059; 2 sequenced antibodies.
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 1: Evidence at protein level;
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..394
FT /note="Envelope glycoprotein D"
FT /id="PRO_5000142083"
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 /evidence="ECO:0000250"
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:0000250|UniProtKB:P57083"
FT DISULFID 131..227
FT /evidence="ECO:0000250|UniProtKB:P57083"
FT DISULFID 143..152
FT /evidence="ECO:0000250|UniProtKB:P57083"
SQ SEQUENCE 394 AA; 43308 MW; 90593F3C19486AC5 CRC64;
MGGAAARLGA VILFVVIVGL HGVRGKYALA 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
VYWMRRRTQK APKRIRLPHI REDDQPSSHQ PLFY
