GB_BHV1C
ID GB_BHV1C Reviewed; 932 AA.
AC P12640;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 02-JUN-2021, entry version 94.
DE RecName: Full=Envelope glycoprotein B {ECO:0000255|HAMAP-Rule:MF_04032};
DE Short=gB {ECO:0000255|HAMAP-Rule:MF_04032};
DE Flags: Precursor;
GN Name=gB {ECO:0000255|HAMAP-Rule:MF_04032}; Synonyms=GI; ORFNames=UL27;
OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10323;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841484; DOI=10.1128/jvi.62.9.3319-3327.1988;
RA Whitbeck J.C., Bello L.J., Lawrence W.C.;
RT "Comparison of the bovine herpesvirus 1 gI gene and the herpes simplex
RT virus type 1 gB gene.";
RL J. Virol. 62:3319-3327(1988).
CC -!- FUNCTION: Envelope glycoprotein that forms spikes at the surface of
CC virion envelope. Essential for the initial attachment to heparan
CC sulfate moieties of the host cell surface proteoglycans. Involved in
CC fusion of viral and cellular membranes leading to virus entry into the
CC host cell. Following initial binding to its host receptors, membrane
CC fusion is mediated by the fusion machinery composed at least of gB and
CC the heterodimer gH/gL. May be involved in the fusion between the virion
CC envelope and the outer nuclear membrane during virion egress.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate
CC proteoglycans. Interacts with gH/gL heterodimer. {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032};
CC Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}.
CC Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass
CC type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi
CC apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type
CC I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Note=During
CC virion morphogenesis, this protein probably accumulates in the
CC endosomes and trans-Golgi where secondary envelopment occurs. It is
CC probably transported to the cell surface from where it is endocytosed
CC and directed to the trans-Golgi network (TGN). {ECO:0000255|HAMAP-
CC Rule:MF_04032}.
CC -!- PTM: A proteolytic cleavage by host furin generates two subunits that
CC remain linked by disulfide bonds. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
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DR EMBL; M21474; AAA46055.1; -; Genomic_DNA.
DR EMBL; Z78205; CAB01598.1; -; Genomic_DNA.
DR EMBL; AJ004801; CAA06106.1; -; Genomic_DNA.
DR PIR; A28877; VGBEBC.
DR RefSeq; NP_045331.1; NC_001847.1.
DR SMR; P12640; -.
DR GeneID; 4783419; -.
DR KEGG; vg:4783419; -.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-UniRule.
DR GO; GO:0016032; P:viral process; IMP:AgBase.
DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 2.30.29.100; -; 1.
DR HAMAP; MF_04032; HSV_GB; 1.
DR InterPro; IPR035377; Glycoprot_B_PH1.
DR InterPro; IPR035381; Glycoprot_B_PH2.
DR InterPro; IPR038631; Glycoprot_B_PH2_sf.
DR InterPro; IPR000234; Herpes_Glycoprot_B.
DR Pfam; PF17416; Glycoprot_B_PH1; 1.
DR Pfam; PF17417; Glycoprot_B_PH2; 1.
PE 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Host cell membrane; Host endosome;
KW Host Golgi apparatus; Host membrane; Host-virus interaction; Membrane;
KW Signal; Transmembrane; Transmembrane helix; Viral attachment to host cell;
KW Viral envelope protein; Virion; Virus entry into host cell.
FT SIGNAL 1..62
FT /evidence="ECO:0000255"
FT CHAIN 63..932
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038168"
FT TOPO_DOM 63..806
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 807..827
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 828..932
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 67..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..190
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 269..276
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 492..527
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 751..804
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 784..804
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 880..883
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 921..924
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 69..97
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 441
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 483
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 640
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 128..607
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 145..563
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 218..282
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 375..423
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 628..665
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 932 AA; 101196 MW; 9DCEAA85C5FC3DA3 CRC64;
MAARGGAERA AGAGDGRRGQ RRHLRPGRVL AALRGPAAPG AGGARAALAA ALLWATWALL
LAAPAAGRPA TTPPAPPPEE AASPAPPASP SPPGPDGDDA ASPDNSTDVR AALRLAQAAG
ENSRFFVCPP PSGATVVRLA PARPCPEYGL GRNYTEGIGV IYKENIAPYT FKAYIYKNVI
VTTTWAGSTY AAITNQYTDR VPVGMGEITD LVDKKWRCLS KAEYLRSGRK VVAFDRDDDP
WEAPLKPARL SAPGVRGWHT TDDVYTALGS AGLYRTGTSV NCIVEEVEAR SVYPYDSFAL
STGDIIYMSP FYGLREGAHR EHTSYSPERF QQIEGYYKRD MATGRRLKEP VSRNFLRTQH
VTVAWDWVPK RKNVCSLAKW READEMLRDE SRGNFRFTAR SLSATFVSDS HTFALQNVPL
SDCVIEEAEA AVERVYRERY NGTHVLSGSL ETYLARGGFV VAFRPMLSNE LAKLYLQELA
RSNGTLEGLF AAAAPKPGPR RARRAAPSAP GGPGAANGPA GDGDAGGRVT TVSSAEFAAL
QFTYDHIQDH VNTMFSRLAT SWCLLQNKER ALWAEAAKLN PSAAASAALD RRAAARMLGD
AMAVTYCHEL GEGRVFIENS MRAPGGVCYS RPPVSFAFGN ESEPVEGQLG EDNELLPGRE
LVEPCTANHK RYFRFGADYV YYENYAYVRR VPLAELEVIS TFVDLNLTVL EDREFLPLEV
YTRAELADTG LLDYSEIQRR NQLHELRFYD IDRVVKTDGN MAIMRGLANF FQGLGAVGQA
VGTVVLGAAG AALSTVSGIA SFIANPFGAL ATGLLVLAGL VAAFLAYRYI SRLRSNPMKA
LYPITTRALK DDARGATAPG EEEEEFDAAK LEQAREMIKY MSLVSAVERQ EHKAKKSNKG
GPLLATRLTQ LALRRRAPPE YQQLPMADVG GA
