GD_HHV1K
ID GD_HHV1K Reviewed; 394 AA.
AC A1Z0Q5; Q05060; Q69081; Q69082;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; ORFNames=US6;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Isolate KOSc, Isolate KOSc(AC3,AC6), and Isolate KOSc(AC4);
RX PubMed=17604805; DOI=10.1016/j.virol.2007.05.040;
RA Ekblad M., Adamiak B., Bergefall K., Nenonen H., Roth A., Bergstrom T.,
RA Ferro V., Trybala E.;
RT "Molecular basis for resistance of herpes simplex virus type 1 mutants to
RT the sulfated oligosaccharide inhibitor PI-88.";
RL Virology 367:244-252(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KOS, Mutant Rid1, and Mutant Rid2;
RX PubMed=8116256; DOI=10.1006/viro.1994.1098;
RA Dean H.J., Terhune S.S., Shieh M.-T., Spear P.G.;
RT "Single amino acid substitutions in glycoprotein D of herpes simplex virus
RT type 1 that confer resistance to gD-mediated interference also alter virus
RT infectivity.";
RL Virology 199:67-80(1994).
RN [3]
RP INTERACTION WITH HUMAN RECEPTORS NECTIN1 AND TNFRSF14.
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 [4]
RP BINDING TO 3-O-SULFATED HEPARAN SULFATE.
RX PubMed=10520990; DOI=10.1016/s0092-8674(00)80058-6;
RA Shukla D., Liu J., Blaiklock P., Shworak N.W., Bai X., Esko J.D.,
RA Cohen G.H., Eisenberg R.J., Rosenberg R.D., Spear P.G.;
RT "A novel role for 3-O-sulfated heparan sulfate in herpes simplex virus 1
RT entry.";
RL Cell 99:13-22(1999).
RN [5]
RP INTERACTION OF MUTANT RID1 WITH HUMAN NECTIN2.
RC STRAIN=Mutant Rid1;
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, 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. Mutant Rid1 interacts
CC with host receptor NECTIN2. Interacts (via profusion domain) with gB;
CC this interaction occurs in the absence of gH/gL. Interacts (via
CC profusion domain) with gH/gL heterodimer; this interaction occurs in
CC the absence of gB. Associates with the gB-gH/gL-gD complex. Interacts
CC (via C-terminus) with UL11 tegument protein. Interacts (via C-terminus)
CC with VP22 tegument protein; this interaction might be very weak (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; L09243; AAA19629.1; -; Unassigned_DNA.
DR EMBL; L09244; AAA19631.1; -; Unassigned_DNA.
DR EMBL; L09245; AAA19630.1; -; Unassigned_DNA.
DR EMBL; EF157319; ABM52978.1; -; Genomic_DNA.
DR EMBL; EF157320; ABM52979.1; -; Genomic_DNA.
DR EMBL; EF157321; ABM52980.1; -; Genomic_DNA.
DR BMRB; A1Z0Q5; -.
DR SMR; A1Z0Q5; -.
DR MINT; A1Z0Q5; -.
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_5000142086"
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:0000269|PubMed:9696799"
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 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 VARIANT 52
FT /note="Q -> P (in strain: Mutant rid1 and Isolate
FT KOSc(AC3,AC6); interference resistant)"
FT VARIANT 52
FT /note="Q -> R (in strain: Mutant rid2; interference
FT resistant)"
FT CONFLICT 30
FT /note="A -> V (in Ref. 1; AAA19630 and 2; ABM52980)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 43317 MW; 905A0F0F1953CB7F 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
VYWMHRRTRK APKRIRLPHI REDDQPSSHQ PLFY
