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-DEC-2020, entry version 93. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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 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 64..95 FT /note="Pro-rich" FT COMPBIAS 491..494 FT /note="Poly-Ala" FT COMPBIAS 861..865 FT /note="Poly-Glu" 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 //