GD_BHV1P
ID GD_BHV1P Reviewed; 417 AA.
AC P0CK29; P24906;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 02-JUN-2021, entry version 26.
DE RecName: Full=Envelope glycoprotein D;
DE Short=gD;
DE AltName: Full=Glycoprotein IV;
DE Flags: Precursor;
GN Name=gD; Synonyms=gIV, US6;
OS Bovine herpesvirus 1.1 (strain P8-2) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10324;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 19-48.
RX PubMed=2168991; DOI=10.1128/jvi.64.10.5132-5142.1990;
RA Tikoo S.K., Fitzpatrick D.R., Babiuk L.A., Zamb T.J.;
RT "Molecular cloning, sequencing, and expression of functional bovine
RT herpesvirus 1 glycoprotein gIV in transfected bovine cells.";
RL J. Virol. 64:5132-5142(1990).
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; M59846; AAA46050.1; -; Genomic_DNA.
DR PIR; A36548; VGBEIB.
DR RefSeq; NP_045370.1; NC_001847.1.
DR SMR; P0CK29; -.
DR GeneID; 1487406; -.
DR KEGG; vg:1487406; -.
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 1: Evidence at protein level;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Host-virus interaction; Membrane; Signal; Transmembrane;
KW 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..18
FT /evidence="ECO:0000269|PubMed:2168991"
FT CHAIN 19..417
FT /note="Envelope glycoprotein D"
FT /id="PRO_0000038219"
FT TOPO_DOM 19..360
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..417
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 259..356
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 75..197
FT /evidence="ECO:0000250"
FT DISULFID 114..213
FT /evidence="ECO:0000250"
FT DISULFID 126..135
FT /evidence="ECO:0000250"
SQ SEQUENCE 417 AA; 44925 MW; 4DFBE3ACF93DF545 CRC64;
MQGPTLAVLG ALLAVAVSLP TPAPRVTVYV DPPAYPMPRY NYTERWHTTG PIPSPFADGR
EQPVEVRYAT SAAACDMLAL IADPQVGRTL WEAVRRHARA YNATVIWYKI ESGCARPLYY
MEYTECEPRK HFGYCRYRTP PFWDSFLAGF AYPTDDELGL IMAAPARLVE GQYRRALYID
GTVAYTDFMV SLPAGDCWFS KLGAARGYTF GACFPARDYE QKKVLRLTYL TQYYPQEAHK
AIVDYWFMRH GGVVPPYFEE SKGYEPPPAA DGGSPAPPGD DEAREDEGET EDGAAGREGN
GGPPGPEGDG ESQTPEANGG AEGEPKPGPS PDADRPEGWP SLEAITHPPP APATPAAPDA
VPVSVGIGIA AAAIACVAAA AAGAYFVYTR RRGAGPLPRK PKKLPAFGNV NYSALPG