GB_EHV4
ID GB_EHV4 Reviewed; 919 AA.
AC P17472;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 84.
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 Equine herpesvirus 4 (strain 1942) (EHV-4) (Equine rhinopneumonitis virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10333;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2915378; DOI=10.1128/jvi.63.3.1123-1133.1989;
RA Riggio M.P., Cullinane A.A., Onions D.E.;
RT "Identification and nucleotide sequence of the glycoprotein gB gene of
RT equine herpesvirus 4.";
RL J. Virol. 63:1123-1133(1989).
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=AAA46106.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M26171; AAA46106.1; ALT_INIT; Genomic_DNA.
DR PIR; A31880; VGBEQH.
DR SMR; P17472; -.
DR PRIDE; P17472; -.
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..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 29..919
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038175"
FT TOPO_DOM 29..788
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 810..919
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 138..144
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 223..231
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 733..786
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 765..785
FT /note="Hydrophobic membrane proximal region"
FT REGION 900..919
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 864..867
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 904..907
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 902..919
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 460..461
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 106
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 216
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 364
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 438
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 456
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 493
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 496
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 499
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 666
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 688
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 81..586
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 98..542
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 172..237
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 330..378
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 607..647
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 919 AA; 103711 MW; C77E48F26C37BC7B CRC64;
MSKDSTSLGV RTIVIACLVL LGCCIVEAVP TTPSSQPSTP ASTQSAKTVD QTLLPTETPD
PLRLAVRESG ILAEDGDFYT CPPPTGSTVV RIEPPRSCPK FDLGRNFTEG IAVIFKENIA
PYKFRANVYY KDIVVTKVWK GYSHTSLSDR YNDRVPVSVE EIFTLIDSKG KCSSKAEYLR
DNIMHHAYHD DEDEVELDLV PSKFATPGAR AWQTTNDTTS YVGWMPWRHY TSTSVNCIVE
EVEARSVYPY DSFALSTGDI VYTSPFYGLR SAAQLEHNSY AQERFRQVEG YQPRDLDSKL
QAGEPVTKNF ITTPHVTVSW NWTEKKIEAC TLTKWKEVDE LVRDEFRGSY RFTIRSISST
FISNTTQFKL EDAPLTDCVS KEAKDAIDSI YRKQYESTHV FSGDVEFYLA RGGFLIAFRP
MISNELARLY LNELVRSNRT YDLKNLLNPN ANHNTNRTRR SLLSIPEPTP TQESLHREQI
LHRLHKRAVE AANSTNSSNV TAKQLELIKT TSSIEFAMLQ FAYDHIQSHV NEMLSRIATA
WCTLQNKERT LWNEMVKVNP SAIVSATLDE RVAARVLGDV IAITHCVKIE GNVYLQNSMR
SSDSNTCYSR PPVTFTITKN ANSRGTIEGQ LGEENEVYTE RKLIEPCAIN QKRYFKFGKE
YVYYENYTYV RKVPPTEIEV ISTYVELNLT LLEDREFLPL EVYTRAELED TGLLDYSEIQ
RRNQLHALRF YDIDSVVNVD NTAVIMQGIA TFFKGLGKVG EAVGTLVLGA AGAVVSTVSG
IASFINNPFG GLAIGLLVIA GLVAAFFAYR YVMQLRSNPM KALYPITTRS LKNKAKASYG
QNDDDDTSDF DEAKLEEARE MIKYMSMVSA LEKQEKKAMK KNKGVGLIAS NVSKLALRRR
GPKYTRLRED DPMESEKMV
