GD_HHV1A
ID GD_HHV1A Reviewed; 394 AA.
AC P36318;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; Synonyms=US6;
OS Human herpesvirus 1 (strain Angelotti) (HHV-1) (Human herpes simplex virus
OS 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10301;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2165127; DOI=10.1084/jem.172.2.487;
RA Izumi K.M., Stevens J.G.;
RT "Molecular and biological characterization of a herpes simplex virus type 1
RT (HSV-1) neuroinvasiveness gene.";
RL J. Exp. Med. 172:487-496(1990).
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; X54361; CAA38245.1; -; Genomic_DNA.
DR PIR; A47627; A47627.
DR SMR; P36318; -.
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..394
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000038215"
FT TOPO_DOM 26..339
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 340..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..394
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 25..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 374..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; 43304 MW; 47DE3BC79BB28950 CRC64;
MGGAAARLGA VILFVVIVGL HGVRGKYALA DASLKMADPN RFRGKDLPVP DRLTDPPGVR
RVYHIQAGLP DPFQPPSLPI TVYYAVLERA CRSVLLNAPS EAPQIVRGGS EDVRKQPYNL
TIAWFRMGGN CAIPITVMEY TECSYNKSLG ACPIRTQPRW NYYDSFSAVS EDNLGFLMHA
PAFETAGTYL RLVKINDWTE ITQFILEHRA KGSCKYALPL RIPPSACLSP QAYQQGVTVD
SIGMLPRFIP ENQRIVAVYS LKIAGWHGPK APYTSTLLPP ELSETPNATQ PELAPEDPED
SALLEDPVGT VAPQIPPNWH IPSIQDAATP YHPPATPNNM GLIAGAVGGS LLAALVICGI
VYWMRRRTQK GPKRIRLPHI REDDQPSSHQ PLFY
