GB_ILTVT
ID GB_ILTVT Reviewed; 883 AA.
AC P24904;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, 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 Infectious laryngotracheitis virus (strain Thorne V882) (ILTV) (Gallid
OS herpesvirus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=10344;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1847176; DOI=10.1099/0022-1317-72-2-393;
RA Griffin A.M.;
RT "The nucleotide sequence of the glycoprotein gB gene of infectious
RT laryngotracheitis virus: analysis and evolutionary relationship to the
RT homologous gene from other herpesviruses.";
RL J. Gen. Virol. 72:393-398(1991).
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; D00818; BAA00699.1; -; Genomic_DNA.
DR PIR; A38478; VGBEIL.
DR SMR; P24904; -.
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..31
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 32..883
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038179"
FT TOPO_DOM 32..750
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 751..771
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 772..883
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 134..140
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 216..223
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 428..457
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 694..748
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 724..744
FT /note="Hydrophobic membrane proximal region"
FT REGION 791..817
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 868..871
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 428..442
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..457
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 438..439
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 121
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 211
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 262
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 579
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 635
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 649
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 77..535
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 94..491
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 167..229
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 321..369
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 558..608
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 883 AA; 100161 MW; D457DF5178840A7D CRC64;
MQSYIAVNID MASLKMLICV CVAILIPSTL SQDSHGIAGI IDPRDTASMD VGKISFSEAI
GSGAPKEPQI RNRIFACSSP TGASVARLAQ PRHCHRHADS TNMTEGIAVV FKQNIAPYVF
NVTLYYKHIT TVTTWALFSR PQITNEYVTR VPIDYHEIVR IDRSGECSSK ATYHKNFMFF
EAYDNDEAEK KLPLVPSLLR STVSKAFHTT NFTKRHQTLG YRTSTSVDCV VEYLQARSVY
PYDYFGMATG DTVEISPFYT KNTTGPRRHS VYRDYRFLEI ANYQVRDLET GQIRPPKKRN
FLTDEQFTIG WDAMEEKESV CTLSKWIEVP EAVRVSYKNS YHFSLKDMTM TFSSGKQPFN
ISRLHLAECV PTIASEAIDG IFARKYSSTH VRSGDIEYYL GSGGFLIAFQ KLMSHGLAEM
YLEEAQRQNH LPRGRERRQA AGRRTASLQS GPQGDRITTH SSATFAMLQF AYDKIQAHVN
ELIGNLLEAW CELQNRQLIV WHEMKKLNPN SLMTSLFGQP VSARLLGDIV AVSKCIEIPI
ENIRMQDSMR MPGDPTMCYT RPVLIFRYSS SPESQFSANS TENHNLDILG QLGEHNEILQ
GRNLIEPCMI NHRRYFLLGE NYLLYEDYTF VRQVNASEIE EVSIFINLNA TILEDLDFVP
VEVYTREELR DTGTLNYDDV VRYQNIYNKR FRDIDTVIRG DRGDAIFRAI ADFFGNTLGE
VGKALGTVVM TAAAAVISTV SGIASFLSNP FAALGIGIAV VVSIILGLLA FKYVMNLKSN
PVQVLFPGAV PPAGTPPRPS RRYYKDEEEV EEDSDEDDRI LATRVLKGLE LLHKDEQKAR
RQKARFSAFA KNMRNLFRRK PRTKEDDYPL LEYPSWAEES EDE
