GD_HHV1P
ID GD_HHV1P Reviewed; 394 AA.
AC P57083; P03171;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE Flags: Precursor;
GN Name=gD; Synonyms=US6;
OS Human herpesvirus 1 (strain Patton) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10308;
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 X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 26-310 IN COMPLEX WITH TNFRSF14,
RP DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-119.
RX PubMed=11511370; DOI=10.1016/s1097-2765(01)00298-2;
RA Carfi A., Willis S.H., Whitbeck J.C., Krummenacher C., Cohen G.H.,
RA Eisenberg R.J., Wiley D.C.;
RT "Herpes simplex virus glycoprotein D bound to the human receptor HveA.";
RL Mol. Cell 8:169-179(2001).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) OF 48-331 IN COMPLEX WITH ZINC IONS,
RP DISULFIDE BONDS, ZINC-BINDING, GLYCOSYLATION AT ASN-119, AND MUTAGENESIS OF
RP VAL-62; TRP-319 AND ALA-327.
RX PubMed=16292345; DOI=10.1038/sj.emboj.7600875;
RA Krummenacher C., Supekar V.M., Whitbeck J.C., Lazear E., Connolly S.A.,
RA Eisenberg R.J., Cohen G.H., Wiley D.C., Carfi A.;
RT "Structure of unliganded HSV gD reveals a mechanism for receptor-mediated
RT activation of virus entry.";
RL EMBO J. 24:4144-4153(2005).
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.
CC 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; X02138; CAA26060.1; -; Genomic_DNA.
DR EMBL; J02217; AAA45785.1; -; Genomic_DNA.
DR PIR; A94268; VGBED1.
DR PDB; 1JMA; X-ray; 2.65 A; A=26-310.
DR PDB; 1L2G; X-ray; 2.85 A; A/B/C/D=26-310.
DR PDB; 2C36; X-ray; 2.11 A; A/B=48-332.
DR PDB; 2C3A; X-ray; 2.50 A; A/B=47-332.
DR PDBsum; 1JMA; -.
DR PDBsum; 1L2G; -.
DR PDBsum; 2C36; -.
DR PDBsum; 2C3A; -.
DR BMRB; P57083; -.
DR SMR; P57083; -.
DR IntAct; P57083; 1.
DR MINT; P57083; -.
DR iPTMnet; P57083; -.
DR PRIDE; P57083; -.
DR EvolutionaryTrace; P57083; -.
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 3D-structure; Disulfide bond; Glycoprotein; Host Golgi apparatus;
KW Host-virus interaction; Membrane; Metal-binding; 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..394
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000038214"
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 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:0000269|PubMed:16292345,
FT ECO:0007744|PDB:2C36"
FT BINDING 240
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:16292345,
FT ECO:0007744|PDB:2C36"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:11511370,
FT ECO:0000269|PubMed:16292345, ECO:0007744|PDB:1JMA,
FT ECO:0007744|PDB:1L2G, ECO:0007744|PDB:2C36,
FT ECO:0007744|PDB:2C3A"
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:0000269|PubMed:11511370,
FT ECO:0000269|PubMed:16292345, ECO:0007744|PDB:1JMA,
FT ECO:0007744|PDB:1L2G, ECO:0007744|PDB:2C36,
FT ECO:0007744|PDB:2C3A"
FT DISULFID 131..227
FT /evidence="ECO:0000269|PubMed:11511370,
FT ECO:0000269|PubMed:16292345, ECO:0007744|PDB:1JMA,
FT ECO:0007744|PDB:1L2G, ECO:0007744|PDB:2C36,
FT ECO:0007744|PDB:2C3A"
FT DISULFID 143..152
FT /evidence="ECO:0000269|PubMed:11511370,
FT ECO:0000269|PubMed:16292345, ECO:0007744|PDB:1JMA,
FT ECO:0007744|PDB:1L2G, ECO:0007744|PDB:2C36,
FT ECO:0007744|PDB:2C3A"
FT MUTAGEN 62
FT /note="V->C: Impaired virus entry into host cell; when
FT associated with C-327. Inability of the corresponding
FT soluble gD to bind TNFRSF14 and NECTIN1."
FT /evidence="ECO:0000269|PubMed:16292345"
FT MUTAGEN 319
FT /note="W->A: Impaired virus entry into host cell."
FT /evidence="ECO:0000269|PubMed:16292345"
FT MUTAGEN 327
FT /note="A->C: Impaired virus entry into host cell; when
FT associated with C-62. Inability of the corresponding
FT soluble gD to bind TNFRSF14 and NECTIN1."
FT /evidence="ECO:0000269|PubMed:16292345"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:1JMA"
FT TURN 39..41
FT /evidence="ECO:0007829|PDB:1JMA"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1JMA"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 111..114
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 118..128
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 131..143
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 153..156
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 159..162
FT /evidence="ECO:0007829|PDB:2C36"
FT TURN 164..166
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 187..195
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 198..212
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:2C36"
FT TURN 239..243
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 250..264
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2C36"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:1JMA"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2C36"
FT STRAND 326..330
FT /evidence="ECO:0007829|PDB:2C36"
SQ SEQUENCE 394 AA; 43347 MW; 052ABB5F53033D5E CRC64;
MGGTAARLGA 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
