GB_BHV2B
ID GB_BHV2B Reviewed; 917 AA.
AC P12641;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 2.
DT 02-JUN-2021, entry version 88.
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};
OS Bovine herpesvirus 2 (strain BMV) (BoHV-2) (Bovine mammillitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10296;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2841793; DOI=10.1016/0042-6822(88)90583-1;
RA Hammerschmidt W., Conraths F., Mankertz J., Pauli G., Ludwig H.,
RA Buhk H.-J.;
RT "Conservation of a gene cluster including glycoprotein B in bovine
RT herpesvirus type 2 (BHV-2) and herpes simplex virus type 1 (HSV-1).";
RL Virology 165:388-405(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-200.
RX PubMed=2457278; DOI=10.1016/0042-6822(88)90584-3;
RA Hammerschmidt W., Conraths F., Mankertz J., Buhk H.-J., Pauli G.,
RA Ludwig H.;
RT "Common epitopes of glycoprotein B map within the major DNA-binding
RT proteins of bovine herpesvirus type 2 (BHV-2) and herpes simplex virus type
RT 1 (HSV-1).";
RL Virology 165:406-418(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; M21628; AAA46053.1; -; Genomic_DNA.
DR EMBL; M21632; AAA46052.1; -; Genomic_DNA.
DR PIR; C29242; VGBEBH.
DR SMR; P12641; -.
DR PRIDE; P12641; -.
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: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..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 23..917
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038169"
FT TOPO_DOM 23..792
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 814..917
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 21..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 196..202
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 281..288
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 737..790
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 865..868
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 907..910
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 31..45
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 110
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 164
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 421
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 453
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 505
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 692
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 139..591
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 156..547
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 230..294
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 387..435
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 614..651
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 917 AA; 101883 MW; 1B96CBF50DB4D3F3 CRC64;
MAISRRSLHA IILTVLLLAA TAAPSQSGSR SRSRRKSERQ STNRGRDNNS IRGGVAQTPE
SSPLPALDLT PQPPMEKEEP DTLAPRASRD APGTPKVPAM PGVTPEPSGN ASEPADPAEL
RADLRGLKGS SDDPNFYVCP PPTGATVVRL EEPRPCPELP KGLNFTEGIA VTFKENLAPY
KFKATMYYKA VTVASVWSGY SYNQFMNIFE DRAPIPFEEI VDRIHGRGMC LSTAKYVRNN
LETTAFHNDA DEHEMKLVPA ESAPGLHRGW HTTRLKNNPT GSAWIHRHGT TVDCIVDEVE
AKSSYPYNEF VLATGDFVYA SPFFGYRDGS HSEHNAYAAD RFKQVDGFFP RDFGTGRRHG
SPVTYNLLTT PMFTVGWNWA PKRPSVCTMT KWREVPEMLR AEYGSSFRFT SNALSATFTT
NLTQYSLSRV DLGDCVGKEA REAIDRIYLE KYNNTHLRVG SVQYYLATGG FLIAYQPLLS
NNLADLYVKE LMREQALKPE ERKLNATTDG KVITTTSSVE FARLQFTYNH IQKHVNEMFG
RMAVSWCELQ NQELTLWNEA KKINPSAIAS VTLHRRVSAC MLGDVLAIST CVAVPAENVI
MQNSMRIPSK PGTCYSRPLL SFKHVDGEEL MEGQLGENNE IRLDRDAVEP CSVGHKRYFL
FGAGYVYFEE YTYSHQLSRS DITAVSTFID LNITMLEDHE FVPLEVYTRQ EIKDSGLLDY
AEVQRRNQLH ALRFADIDTV IKADPNAAIF AGLHGFFEGL GDVGRAVGRV VLGVVGGVVA
TVSGVSSFLS NPFGALAIGL LVLGGLVAAF FAFRYVMRLQ RNPMKALYPL TTKDLKHPSE
GGGGEEAMED FDEQKLDEAR SMIKYMALVS AMERTKHKAG RRGGTSAILN ARLTDMVMRK
RGAKPKYEAL PETDEDI
