ID   GD_EHV1B                Reviewed;         452 AA.
AC   Q6DLD9; P24379;
DT   09-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   02-JUN-2021, entry version 83.
DE   RecName: Full=Envelope glycoprotein D;
DE            Short=gD;
DE   AltName: Full=Glycoprotein 17/18;
DE   Flags: Precursor;
GN   Name=gD; Synonyms=GP17/18; OrderedLocusNames=72;
OS   Equine herpesvirus 1 (strain Ab4p) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=31520;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=1318606; DOI=10.1016/0042-6822(92)90706-u;
RA   Telford E.A.R., Watson M.S., McBride K., Davison A.J.;
RT   "The DNA sequence of equine herpesvirus-1.";
RL   Virology 189:304-316(1992).
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}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-51 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AY665713; AAT67329.1; -; Genomic_DNA.
DR   PIR; I36802; VGBEG3.
DR   SMR; Q6DLD9; -.
DR   Proteomes; UP000001189; Genome.
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;
KW   Reference proteome; 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.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..452
FT                   /note="Envelope glycoprotein D"
FT                   /id="PRO_0000038222"
FT   TOPO_DOM        20..405
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        406..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        423..452
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          331..365
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        111
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        347
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        396
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        138..259
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        176..273
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        188..197
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
SQ   SEQUENCE   452 AA;  51099 MW;  CF51E914F7F2E9DC CRC64;
     MPAVLLVLYV NPPPSVCILT QKLSLGLYNQ WWRVCRSVPP PWYVFFNKRS MSTFKLMMDG
     RLVFAMAIAI LSVVLSCGTC EKAKRAVRGR QDRPKEFPPP RYNYTILTRY NATALASPFI
     NDQVKNVDLR IVTATRPCEM IALIAKTNID SILKELAAAQ KTYSARLTWF KIMPTCATPI
     HDVSYMKCNP KLSFAMCDER SDILWQASLI TMAAETDDEL GLVLAAPAHS ASGLYRRVIE
     IDGRRIYTDF SVTIPSERCP IAFEQNFGNP DRCKTPEQYS RGEVFTRRFL GEFNFPQGEH
     MTWLKFWFVY DGGNLPVQFY EAQAFARPVP PDNHPGFDSV ESEITQNKTD PKPGQADPKP
     NQPFKWPSIK HLAPRLDEVD EVIEPVTKPP KTSKSNSTFV GISVGLGIAG LVLVGVILYV
     CLRRKKELKK SAQNGLTRLR STFKDVKYTQ LP