ID   GD_EHV1A                Reviewed;         402 AA.
AC   P24872;
DT   01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   02-JUN-2021, entry version 90.
DE   RecName: Full=Envelope glycoprotein D;
DE            Short=gD;
DE   AltName: Full=Glycoprotein 17/18;
DE   Flags: Precursor;
GN   Name=gD; Synonyms=GP17/18;
OS   Equine herpesvirus 1 (strain AB1) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10328;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1316942; DOI=10.1099/0022-1317-73-5-1227;
RA   Elton D.M., Halliburton I.W., Killington R.A., Meredith D.M., Bonass W.A.;
RT   "Identification of the equine herpesvirus type 1 glycoprotein 17/18 as a
RT   homologue of herpes simplex virus glycoprotein D.";
RL   J. Gen. Virol. 73:1227-1233(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 242-402.
RX   PubMed=1647359; DOI=10.1016/0378-1119(91)90412-5;
RA   Elton D.M., Halliburton I.W., Killington R.A., Meredith D.M., Bonass W.A.;
RT   "Sequence analysis of the 4.7-kb BamHI-EcoRI fragment of the equine
RT   herpesvirus type-1 short unique region.";
RL   Gene 101:203-208(1991).
CC   -!- FUNCTION: Envelope glycoprotein that binds to host cell entry
CC       receptors. May trigger fusion with host membrane, by recruiting the
CC       fusion machinery composed of gB and gH/gL (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I
CC       membrane protein {ECO:0000250}. 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; M60946; AAA46087.1; -; Genomic_DNA.
DR   EMBL; M36299; AAA66546.1; -; Genomic_DNA.
DR   SMR; P24872; -.
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: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-virus interaction; Membrane; Signal;
KW   Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW   Viral attachment to host entry receptor; Viral envelope protein; Virion;
KW   Virus entry into host cell.
FT   SIGNAL          1..30
FT                   /evidence="ECO:0000255"
FT   CHAIN           31..402
FT                   /note="Envelope glycoprotein D"
FT                   /id="PRO_0000038221"
FT   TOPO_DOM        31..355
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        356..372
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        373..402
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          281..315
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        53
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        297
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        88..209
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        126..223
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        138..147
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
SQ   SEQUENCE   402 AA;  45211 MW;  78A0593232D0238C CRC64;
     MSTFKLMMDG RLVFAMAIAI LSVVLSCGTC EKAKRAVRGR QDRPKEFPPP RYNYTILTRY
     NATALASPFI NDQVKNVDLR IVTATRPCEM IALIAKTNID SILKELAAAQ KTYSARLTWF
     KIMPTCATPI HDVSYMKCNP KLSFAMCDER SDILWQASLI TMAAETDDEL GLVLAAPAHS
     ASGLYRRVIE IDGRQIYTDF SVTIPSERCP IAFEQNFGNP DRCKTPEQYS RGEVFTRRFL
     GEFNFPQGEH MTWLKFWFVY DGGNLPVQFY EAQAFARPVP PDNHPGFDSV ESEITQNKTD
     PKPGQADPKP NQPFKWPSIK HLAPRLDEVD EVIEPVTKPP KTSKSNSTFV GISVGLGIAG
     LVLVGVILYV CLRRKKELKK SAQNGLTRLR STFKDVKYTQ LP