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 13-NOV-2019, entry version 90. 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; Herpesvirales; Herpesviridae; Alphaherpesvirinae; OC Varicellovirus. OX NCBI_TaxID=10323; OH NCBI_TaxID=9913; Bos taurus (Bovine). RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2841484; 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 CC of virion envelope. Essential for the initial attachment to CC heparan sulfate moieties of the host cell surface proteoglycans. CC Involved in fusion of viral and cellular membranes leading to CC virus entry into the host cell. Following initial binding to its CC host receptors, membrane fusion is mediated by the fusion CC machinery composed at least of gB and the heterodimer gH/gL. May CC be involved in the fusion between the virion envelope and the CC outer nuclear membrane during virion egress. {ECO:0000255|HAMAP- CC Rule:MF_04032}. CC -!- SUBUNIT: Homotrimer; disulfide-linked. Binds to heparan sulfate CC proteoglycans. Interacts with gH/gL heterodimer. CC {ECO:0000255|HAMAP-Rule:MF_04032}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP- CC Rule:MF_04032}; Single-pass type I membrane protein CC {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane CC {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane CC protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane CC {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane CC protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host Golgi apparatus CC membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I CC 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 CC is probably transported to the cell surface from where it is CC endocytosed and directed to the trans-Golgi network (TGN). CC {ECO:0000255|HAMAP-Rule:MF_04032}. CC -!- PTM: A proteolytic cleavage by host furin generates two subunits CC that 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 KO; K19255; -. 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; KW Viral attachment to host cell; Viral envelope protein; Virion; KW Virus entry into host cell. FT SIGNAL 1 62 {ECO:0000255}. FT CHAIN 63 932 Envelope glycoprotein B. FT /FTId=PRO_0000038168. FT TOPO_DOM 63 806 Virion surface. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT TRANSMEM 807 827 Helical. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT TOPO_DOM 828 932 Intravirion. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT REGION 184 190 Involved in fusion and/or binding to host FT membrane. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT REGION 269 276 Involved in fusion and/or binding to host FT membrane. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT REGION 751 804 Hydrophobic membrane proximal region. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT REGION 784 804 Hydrophobic membrane proximal region. FT MOTIF 880 883 Golgi targeting. {ECO:0000255|HAMAP- FT Rule:MF_04032}. FT MOTIF 921 924 Internalization motif. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT COMPBIAS 64 95 Pro-rich. FT COMPBIAS 491 494 Poly-Ala. FT COMPBIAS 861 865 Poly-Glu. FT CARBOHYD 105 105 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT CARBOHYD 153 153 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT CARBOHYD 441 441 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT CARBOHYD 483 483 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT CARBOHYD 640 640 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT CARBOHYD 706 706 N-linked (GlcNAc...) asparagine; by host. FT {ECO:0000255|HAMAP-Rule:MF_04032}. FT DISULFID 128 607 {ECO:0000255|HAMAP-Rule:MF_04032}. FT DISULFID 145 563 {ECO:0000255|HAMAP-Rule:MF_04032}. FT DISULFID 218 282 {ECO:0000255|HAMAP-Rule:MF_04032}. FT DISULFID 375 423 {ECO:0000255|HAMAP-Rule:MF_04032}. FT DISULFID 628 665 {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 //