ID   GD_SUHVR                Reviewed;         402 AA.
AC   P07645;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1988, sequence version 1.
DT   02-JUN-2021, entry version 71.
DE   RecName: Full=Envelope glycoprotein D;
DE            Short=gD;
DE   AltName: Full=Protein gp50;
DE   Flags: Precursor;
OS   Suid herpesvirus 1 (strain Rice) (SuHV-1) (Pseudorabies virus (strain
OS   Rice)).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10350;
OH   NCBI_TaxID=9823; Sus scrofa (Pig).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3016293; DOI=10.1128/jvi.59.2.216-223.1986;
RA   Petrovskis E.A., Timmins J.G., Armentrout M.A., Marchioli C.C.,
RA   Yancey R.J. Jr., Post L.E.;
RT   "DNA sequence of the gene for pseudorabies virus gp50, a glycoprotein
RT   without N-linked glycosylation.";
RL   J. Virol. 59:216-223(1986).
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   -!- PTM: Not N-glycosylated.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein D family.
CC       {ECO:0000305}.
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DR   EMBL; M14001; AAC35203.1; -; Genomic_DNA.
DR   PIR; A27788; VGBE50.
DR   SMR; P07645; -.
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..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..402
FT                   /note="Envelope glycoprotein D"
FT                   /id="PRO_0000115764"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          252..350
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        280..294
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        308..342
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        66..189
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        105..205
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
FT   DISULFID        117..126
FT                   /evidence="ECO:0000250|UniProtKB:P57083"
SQ   SEQUENCE   402 AA;  44502 MW;  B8763305995871E8 CRC64;
     MLLAALLAAL VARTTLGADV DAVPAPTFPP PAYPYTESWQ LTLTTVPSPF VGPADVYHTR
     PLEDPCGVVA LISDPQVDRL LNEAVAHRRP TYRAHVAWYR IADGCAHLLY FIEYADCDPR
     QVFGRCRRRT TPMWWTPSAD YMFPTEDELG LLMVAPGRFN EGQYRRLVSV DGVNILTDFM
     VALPEGQECP FARVDQHRTY KFGACWSDDS FKRGVDVMRF LTPFYQQPPH REVVNYWYRK
     NGRTLPRAHA AATPYAIDPA RPSAGSPRPR PRPRPRPRPK PEPAPATPAP PDRLPEPATR
     DHAAGGRPTP RPPRPETPHR PFAPPAVVPS GWPQPAEPFQ PRTPAAPGVS RHRSVIVGTG
     TAMGALLVGV CVYIFFRLRG AKGYRLLGGP ADADELKAQP GP