ID   GD_EHV1K                Reviewed;         442 AA.
AC   P22484;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
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 Kentucky A) (EHV-1) (Equine abortion virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10329;
OH   NCBI_TaxID=9796; Equus caballus (Horse).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1845821; DOI=10.1016/0042-6822(91)90021-3;
RA   Flowers C.C., Eastman E.M., O'Callaghan D.J.;
RT   "Sequence analysis of a glycoprotein D gene homolog within the unique short
RT   segment of the EHV-1 genome.";
RL   Virology 180:175-184(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1316673; DOI=10.1016/0042-6822(92)90509-n;
RA   Colle C.F. III, Flowers C.C., O'Callaghan D.J.;
RT   "Open reading frames encoding a protein kinase, homolog of glycoprotein gX
RT   of pseudorabies virus, and a novel glycoprotein map within the unique short
RT   segment of equine herpesvirus type 1.";
RL   Virology 188:545-557(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   -!- SEQUENCE CAUTION:
CC       Sequence=AAA46073.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M62923; AAA46081.1; -; Genomic_DNA.
DR   EMBL; M86931; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; M87497; AAA46073.1; ALT_INIT; Genomic_DNA.
DR   PIR; A38518; VGBEEA.
DR   SMR; P22484; -.
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..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..442
FT                   /note="Envelope glycoprotein D"
FT                   /id="PRO_0000038224"
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..442
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          331..364
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   442 AA;  49908 MW;  323CDCA9C9762F05 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 IAFELNFGNP DRCKTPEQYS RGEVFTRRFL GEFNFPQGEH
     MTWVKFWFVY DGGNLPVQFY EAQAFARPVP PDNHPGFDSV ESEITQNKTD PKPGQADPKP
     NQPFKWPSIK HLVPRLDEVD EVIEPVTKPP KTSKSNSTFV GISVGLGIAG LVLVGVILYV
     CLRRKKELKV CTERLDSPTL DL