GB_EHV1A
ID GB_EHV1A Reviewed; 980 AA.
AC P18551;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1990, sequence version 1.
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=GP14;
OS Equine herpesvirus 1 (strain AB1) (EHV-1) (Equine abortion virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=10328;
OH NCBI_TaxID=9796; Equus caballus (Horse).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Bonass W.A., Elton D.M., Stocks J.M., Killington R.A., Meredith D.M.,
RA Halliburton I.W.;
RT "Molecular analysis of the Equine herpesvirus type-1 strain Ab1,
RT glycoprotein B gene and its expression in COS cells.";
RL Submitted (JUL-1990) to the EMBL/GenBank/DDBJ databases.
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; M36298; AAA46068.1; -; Genomic_DNA.
DR SMR; P18551; -.
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..86
FT /evidence="ECO:0000255"
FT CHAIN 87..980
FT /note="Envelope glycoprotein B"
FT /id="PRO_0000038171"
FT TOPO_DOM 87..849
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 850..870
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 871..980
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 88..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..203
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 282..290
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 505..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 794..847
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 823..843
FT /note="Hydrophobic membrane proximal region"
FT MOTIF 925..928
FT /note="Golgi targeting"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MOTIF 965..968
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 95..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 165
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 275
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 380
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 423
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 497
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 514
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 515
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 560
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 727
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 749
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 140..647
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 157..603
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 231..296
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 389..437
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 668..708
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 980 AA; 109736 MW; 264D273CED70E5A1 CRC64;
MSSGCRSVGG STWGNWRGDG GDLRQRRVLS PVCSAPAAGS WIGSQLGNVG NLLATPHPLG
KPASSRVGTI VLACLLLFGS CVVRAVPTTP SPPTSTPTSM STHSHGTVDP TLLPTETPDP
LRLAVRESGI LAEDGDFYTC PPPTGSTVVR IEPPRTCPKF DLGRNFTEGI AVIFKENIAP
YKFRANVYYK DIVVTRVWKG YSHTSLSDRY NDRVPVSVEE IFGLIDSKGK CSSKAEYLRD
NIMHHAYHDD EDEVELDLVP SKFATPGARA WQTTNDTTSY VGWMPWRHYT STSVNCIVEE
VEARSVYPYD SFALSTGDIV YASPFYGLRA AARIEHNSYA QDSFRQVEGY RPRDLDSKLQ
AEEPVTKNFI TTPHVTVSWN WTEKKVEACT LTKWKEVDEL VRDEFRGSYR FTIRSISSTF
ISNTTQFKLE SAPLTECVSK EAKEAIDSIY KKQYESTHVF SGDVEYYLAR GGFLIAFRPM
LSNELARLYL NELVRSNRTY DLKNLLNPNA NNNNNTTRRR RSLLSVPEPQ PTQDGVHREQ
ILHRLHKRAV EATAGTDSSN VTAKQLELIK TTSSIEFAML QFAYDHIQSH VNEMLSRIAT
AWCTLQNKER TLWNEMVKIN PSAIVSATLD ERVAARVLGD VIAITHCAKI EGNVYLQNSM
RSMDSNTCYS RPPVTFTITK NANNRGSIEG QLGEENEIFT ERKLIEPCAL NQKRYFKFGK
EYVYYENYTF VRKVPPTEIE VISTYVELNL TLLEDREFLP LEVYTRAELE DTGLLDYSEI
QRRNQLHALR FYDIDSVVNV DNTAVIMQGI ASFFKGLGKV GEAVGTLVLA AAGAVVSTVS
GIASFLNNPF GGLAIGLLVI AGLVAAFFAY RYVMQIRSNP MKALYPITTK ALKNKAKTSY
GQNEEDDGSD FDEAKLEEAR EMIKYMSMVS ALEKQEKKAI KKNSGVGLIA SNVSKLALRR
RGPKYTRLQQ NDTMENEKMV
