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 11-MAY-2016, entry version 80. DE RecName: Full=Envelope glycoprotein B; DE Short=gB; DE AltName: Full=Glycoprotein 11A; DE AltName: Full=Glycoprotein 16; DE AltName: Full=Glycoprotein B; DE AltName: Full=Glycoprotein G130; DE AltName: Full=Glycoprotein GVP-6; DE AltName: Full=Glycoprotein I; DE Flags: Precursor; GN Name=gB; Synonyms=GI; ORFNames=UL27; OS Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine OS rhinotracheitis virus). OC Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC Alphaherpesvirinae; 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 the virion envelope. Essential for the fusion of viral and CC cellular membranes leading to virus entry into the host cell. CC Membrane fusion is mediated by the fusion machinery composed at CC least of gB and the heterodimer gH/gL (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homotrimer; disulfide-linked. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass CC type I membrane protein {ECO:0000250}. Host cell membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC Host endosome membrane {ECO:0000250}; Single-pass type I membrane CC protein {ECO:0000250}. Host Golgi apparatus membrane CC {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. CC Note=During virion morphogenesis, this protein probably CC accumulates in the endosomes and trans-Golgi where secondary CC envelopment occurs. It is probably transported to the cell surface CC from where it is endocytosed and directed to the trans-Golgi CC network (TGN) (By similarity). {ECO:0000250}. 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:0000305}. 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 ProteinModelPortal; 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-KW. DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-KW. DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR GO; GO:0019062; P:virion attachment to host cell; IEA:UniProtKB-KW. DR InterPro; IPR000234; Herpes_Glycoprot_B. DR Pfam; PF00606; Glycoprotein_B; 1. PE 3: Inferred from homology; KW Cleavage on pair of basic residues; Disulfide bond; Glycoprotein; KW Host cell membrane; Host endosome; Host Golgi apparatus; KW Host membrane; Host-virus interaction; Membrane; Signal; KW Transmembrane; Transmembrane helix; Viral attachment to host cell; KW Viral envelope protein; Virion; 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}. FT TRANSMEM 807 827 Helical. {ECO:0000255}. FT TOPO_DOM 828 932 Intravirion. {ECO:0000255}. FT REGION 784 804 Hydrophobic membrane proximal region. FT MOTIF 880 883 Golgi targeting. {ECO:0000255}. FT MOTIF 921 924 Internalization motif. {ECO:0000255}. FT COMPBIAS 64 95 Pro-rich. FT COMPBIAS 491 494 Poly-Ala. FT COMPBIAS 861 865 Poly-Glu. FT SITE 504 505 Cleavage; by host furin. {ECO:0000255}. FT CARBOHYD 105 105 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 153 153 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 441 441 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 483 483 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 640 640 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT CARBOHYD 706 706 N-linked (GlcNAc...); by host. FT {ECO:0000255}. FT DISULFID 128 607 {ECO:0000250|UniProtKB:P06437}. FT DISULFID 145 563 {ECO:0000250|UniProtKB:P06437}. FT DISULFID 218 282 {ECO:0000250|UniProtKB:P06437}. FT DISULFID 375 423 {ECO:0000250|UniProtKB:P06437}. FT DISULFID 628 665 {ECO:0000250|UniProtKB:P06437}. 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 //