GB_ILTV6
ID GB_ILTV6 Reviewed; 873 AA.
AC Q02409;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 2.
DT 02-JUN-2021, entry version 78.
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 632) (ILTV) (Gallid herpesvirus
OS 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Iltovirus.
OX NCBI_TaxID=31521;
OH NCBI_TaxID=9031; Gallus gallus (Chicken).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1665614; DOI=10.1007/bf00271532;
RA Poulsen D.J., Adams Burton C.R., O'Brian J.J., Rabin S.J., Keeler C.L. Jr.;
RT "Identification of the infectious laryngotracheitis virus glycoprotein gB
RT gene by the polymerase chain reaction.";
RL Virus Genes 5:335-347(1991).
RN [2]
RP SEQUENCE REVISION.
RA Keeler C.L. Jr.;
RL Submitted (FEB-1994) 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; X56093; CAA39573.1; -; Genomic_DNA.
DR PIR; S26690; S26690.
DR SMR; Q02409; -.
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..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 22..873
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038177"
FT TOPO_DOM 22..740
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 741..761
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 762..873
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 124..130
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 206..213
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 418..447
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..738
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 715..734
FT /note="Hydrophobic membrane proximal region"
FT REGION 781..807
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 858..861
FT /note="Internalization motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT COMPBIAS 418..432
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 92
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 201
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 252
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 350
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 569
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 625
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 67..525
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 84..481
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 157..219
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 311..359
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT DISULFID 548..598
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
SQ SEQUENCE 873 AA; 99040 MW; E73E7F6D7A0E3AAD CRC64;
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
PTIATEAIDG 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
