ID   GD_CHV1                 Reviewed;         395 AA.
AC   P36342;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Envelope glycoprotein D;
DE            Short=gD;
DE   Flags: Precursor;
GN   Name=gD;
OS   Cercopithecine herpesvirus 1 (CeHV-1) (Simian herpes B virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX   NCBI_TaxID=10325;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
OH   NCBI_TaxID=9541; Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OH   NCBI_TaxID=90387; Macaca leonina (Northern pig-tailed macaque) (Macaca nemestrina leonina).
OH   NCBI_TaxID=9544; Macaca mulatta (Rhesus macaque).
OH   NCBI_TaxID=9545; Macaca nemestrina (Pig-tailed macaque).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1331298; DOI=10.1099/0022-1317-73-11-2963;
RA   Bennett A.M., Harrington L., Kelly D.C.;
RT   "Nucleotide sequence analysis of genes encoding glycoproteins D and J in
RT   simian herpes B virus.";
RL   J. Gen. Virol. 73:2963-2967(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}.
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DR   EMBL; S48101; AAB24129.1; -; Genomic_DNA.
DR   PIR; JQ1746; JQ1746.
DR   SMR; P36342; -.
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-virus interaction; Membrane;
KW   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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..395
FT                   /note="Envelope glycoprotein D"
FT                   /id="PRO_0000038218"
FT   TOPO_DOM        18..342
FT                   /note="Virion surface"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..362
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        363..395
FT                   /note="Intravirion"
FT                   /evidence="ECO:0000255"
FT   REGION          289..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         63
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        287
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   DISULFID        90..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   395 AA;  42643 MW;  9500E5F3EB20812F CRC64;
     MGSGIAAVLL SLAVALARVP AGEGEYVPVE RSLTRVNPGR FRGAHLPPLE QKTDPPDVRR
     VYHVQPFVEN PFQTPSVPVA VYYAVLERAC RSVLLWAPTE AVQVVRGAPE ATRSDARYNL
     TVAWYRTSDD CAIPILVMEY AECQYDKPLG ACPVRNLPRW SFYDSFSATG DDDLGLLMHA
     PAFETAGTYV RLVKVNGWVE VTQFIFEHRG KGPCRYTLPL RILPAACLRA PVFEQGVTVD
     AIGMLPRFIP ENQRIVAVYS LQAAGWHGPK APFTSTLLPP EVVETANVTR PELAPEERGT
     SRTPGDEPAP AVAAQLPPNW HVPEASDVTI QGPAPAPSGH TGAVVGALAG AGLAAGVVVL
     AVYLVRRRGR AAGKHVRLPE LLEEAHGPAR RGAPY