GB_BHV1P
ID GB_BHV1P Reviewed; 928 AA.
AC P17471;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 2.
DT 02-JUN-2021, entry version 83.
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;
OS Bovine herpesvirus 1.1 (strain P8-2) (BoHV-1) (Infectious bovine
OS rhinotracheitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10324;
OH NCBI_TaxID=9913; Bos taurus (Bovine).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2845660; DOI=10.1016/0042-6822(88)90525-9;
RA Misra V., Nelson R., Smith M.;
RT "Sequence of a bovine herpesvirus type-1 glycoprotein gene that is
RT homologous to the herpes simplex gene for the glycoprotein gB.";
RL Virology 166:542-549(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 -!- SEQUENCE CAUTION:
CC Sequence=AAA46013.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; M23257; AAA46013.1; ALT_FRAME; Genomic_DNA.
DR PIR; A31166; VGBEBG.
DR SMR; P17471; -.
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..62
FT /evidence="ECO:0000255"
FT CHAIN 63..928
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038167"
FT TOPO_DOM 63..803
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 804..824
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 825..928
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 185..191
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 270..277
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 495..525
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..801
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 781..801
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 876..879
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 917..920
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 COMPBIAS 500..525
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 505..506
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
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 442
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 484
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 637
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 703
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 128..606
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 145..562
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 219..283
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 376..424
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 627..662
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CONFLICT 409
FT /note="S -> T (in Ref. 1; AAA46013)"
FT /evidence="ECO:0000305"
FT CONFLICT 673
FT /note="G -> P (in Ref. 1; AAA46013)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 928 AA; 101950 MW; 49E176253F03114E CRC64;
MAARGGAERA AGAGDGRRGQ RRHLRPGRVL AALRGPAAPG AGGARAALAA ALLWATWALL
LAAPAAGRPA TTPPAPPPEE AASPAPPASP SPPGPDGDDA ASPDNSTDVR AALRLAQAAG
ENSRFFVCPP PSGATVVRLA PARPCPEYGL GRNYTEGIGV IYKENIAPYT FKAIIYYKNV
IVTTTWAGST YAAITNQYTD RVPVGMGEIT DLVDKKWRCL SKAEYLRSGR KVVAFDRDDD
PWEAPLKPAR LSAPGVRGWH TTDDVYTALG SAGLYRTGTS VNCIVEEVEA RSVYPYDSFA
LSTGDIIYMS PFYGLREGAH REHTSYSPER FQQIEGYYKR DMATGRRLKE PVSRNFLRTQ
HVTVAWDWVP KRKNVCSLAK WREADEMLRD ESRGNFRFTA RSLSATFVSD SHTFALQNVP
LSDCVIEEAE AAVERVYRER YNGTHVLSGS LETYLARGGF VVAFRPMLSN ELAKLYLQEL
ARSNGTLEGL FAAAAPKPGP RRARRPRRLR PAPGRGQRAR RRRHAGGRVT TVSLAEFAAL
QFTHDHTRTS EHHVHRLASP WCLLQNKERA LWAEAAKLNP SAAASAALDR RAAARMLGDA
MAVTYCHELG EGRCSSRTRM RAPGGVCYSR RGSFFGNESE PVEGQLGEDN ELLPGRELVE
PCTANHKRYF RFGADYVYYE NYAYVRRVPL AELEVISTFV DLNLTVLEDR EFLPLEVYTR
AELADTGLLD YSEIQRRNQL HELRFYDIDR VVKTDGNMAI MRGLANFFQG LGAVGQAVGT
VVLGAAGAAL STVSGIASFI ANPFGALATG LLVLAGLVAA FLAYRYISRL RSNPMKALYP
ITTRALKDDP GRNRPGEEEE EFDAAKLEQA REMIKYMSLV SAVERQEHKA KKSNKAARLL
ATRLTQLALR RRAPPEYQQL PMADVGGA
