GB_EBVB9
ID GB_EBVB9 Reviewed; 857 AA.
AC P03188; Q777B0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 23-FEB-2022, entry version 116.
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}; ORFNames=BALF4;
OS Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=10377;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6092825;
RA Bankier A.T., Deininger P.L., Farrell P.J., Barrell B.G.;
RT "Sequence analysis of the 17,166 base-pair EcoRI fragment C of B95-8
RT Epstein-Barr virus.";
RL Mol. Biol. Med. 1:21-45(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6087149; DOI=10.1038/310207a0;
RA Baer R., Bankier A.T., Biggin M.D., Deininger P.L., Farrell P.J.,
RA Gibson T.J., Hatfull G., Hudson G.S., Satchwell S.C., Seguin C.,
RA Tuffnell P.S., Barrell B.G.;
RT "DNA sequence and expression of the B95-8 Epstein-Barr virus genome.";
RL Nature 310:207-211(1984).
RN [3]
RP IDENTIFICATION OF PROTEIN.
RX PubMed=3027378; DOI=10.1128/jvi.61.2.499-508.1987;
RA Gong M., Ooka T., Matsuo T., Kieff E.;
RT "Epstein-Barr virus glycoprotein homologous to herpes simplex virus gB.";
RL J. Virol. 61:499-508(1987).
RN [4]
RP SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
RX PubMed=15534216; DOI=10.1073/pnas.0407320101;
RA Johannsen E., Luftig M., Chase M.R., Weicksel S., Cahir-McFarland E.,
RA Illanes D., Sarracino D., Kieff E.;
RT "Proteins of purified Epstein-Barr virus.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:16286-16291(2004).
RN [5]
RP MUTAGENESIS OF 112-TRP-TYR-113; 193-TRP--TRP-196 AND 428-ARG--ARG-432, AND
RP PROTEOLYTIC CLEAVAGE.
RX PubMed=17655906; DOI=10.1016/j.virol.2007.06.031;
RA Backovic M., Leser G.P., Lamb R.A., Longnecker R., Jardetzky T.S.;
RT "Characterization of EBV gB indicates properties of both class I and class
RT II viral fusion proteins.";
RL Virology 368:102-113(2007).
RN [6]
RP OLIGOMERIZATION REGION.
RX PubMed=18987135; DOI=10.1128/jvi.01817-08;
RA Reimer J.J., Backovic M., Deshpande C.G., Jardetzky T., Longnecker R.;
RT "Analysis of Epstein-Barr virus glycoprotein B functional domains via
RT linker insertion mutagenesis.";
RL J. Virol. 83:734-747(2009).
RN [7]
RP PROTEOLYTIC CLEAVAGE BY HOST FURIN.
RX PubMed=19218203; DOI=10.1099/vir.0.007237-0;
RA Sorem J., Longnecker R.;
RT "Cleavage of Epstein-Barr virus glycoprotein B is required for full
RT function in cell-cell fusion with both epithelial and B cells.";
RL J. Gen. Virol. 90:591-595(2009).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.20 ANGSTROMS) OF 23-685, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-163; ASN-290 AND ASN-629.
RX PubMed=19196955; DOI=10.1073/pnas.0810530106;
RA Backovic M., Longnecker R., Jardetzky T.S.;
RT "Structure of a trimeric variant of the Epstein-Barr virus glycoprotein
RT B.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:2880-2885(2009).
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|PubMed:15534216,
CC ECO:0000305|PubMed:17655906, ECO:0000305|PubMed:19218203}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein B family.
CC {ECO:0000255|HAMAP-Rule:MF_04032}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; V01555; CAA24806.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53463.1; -; Genomic_DNA.
DR PIR; A03749; QQBE1L.
DR RefSeq; YP_401713.1; NC_007605.1.
DR PDB; 3FVC; X-ray; 3.20 A; A=23-685.
DR PDBsum; 3FVC; -.
DR SMR; P03188; -.
DR DIP; DIP-47669N; -.
DR IntAct; P03188; 10.
DR MINT; P03188; -.
DR iPTMnet; P03188; -.
DR PRIDE; P03188; -.
DR DNASU; 3783680; -.
DR GeneID; 3783680; -.
DR KEGG; vg:3783680; -.
DR EvolutionaryTrace; P03188; -.
DR Proteomes; UP000153037; Genome.
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; -; 2.
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 1: Evidence at protein level;
KW 3D-structure; Disulfide bond; Glycoprotein; Host cell membrane;
KW Host endosome; Host Golgi apparatus; Host membrane; Host-virus interaction;
KW Membrane; Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral attachment to host cell; Viral envelope protein; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..21
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CHAIN 22..857
FT /note="Envelope glycoprotein B"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT /id="PRO_0000038190"
FT TOPO_DOM 22..732
FT /note="Virion surface"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TRANSMEM 733..753
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT TOPO_DOM 754..857
FT /note="Intravirion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 108..114
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 192..200
FT /note="Involved in fusion and/or binding to host membrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 398..453
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..620
FT /note="Oligomerization"
FT REGION 678..730
FT /note="Hydrophobic membrane proximal region"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT REGION 709..729
FT /note="Hydrophobic membrane proximal region"
FT REGION 832..857
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 432..433
FT /note="Cleavage; by host furin"
FT /evidence="ECO:0000255"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 163
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 348
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 395
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 436
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 563
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT CARBOHYD 629
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955"
FT DISULFID 51..528
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955, ECO:0007744|PDB:3FVC"
FT DISULFID 68..484
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955, ECO:0007744|PDB:3FVC"
FT DISULFID 141..206
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955, ECO:0007744|PDB:3FVC"
FT DISULFID 295..342
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032,
FT ECO:0000269|PubMed:19196955, ECO:0007744|PDB:3FVC"
FT DISULFID 551..588
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04032"
FT MUTAGEN 112..113
FT /note="WY->HR: Loss of fusion with epithelial cells."
FT /evidence="ECO:0000269|PubMed:17655906"
FT MUTAGEN 193..196
FT /note="WLIW->RVEA: Loss of fusion with epithelial cells."
FT /evidence="ECO:0000269|PubMed:17655906"
FT MUTAGEN 428..432
FT /note="RRRRR->DDDDK: Complete loss of proteolytic
FT cleavage."
FT /evidence="ECO:0000269|PubMed:17655906"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 77..87
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 92..110
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 115..125
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 129..135
FT /evidence="ECO:0007829|PDB:3FVC"
FT TURN 136..138
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 140..149
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 179..183
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 197..215
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 222..224
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 229..232
FT /evidence="ECO:0007829|PDB:3FVC"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 251..257
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 272..278
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 283..287
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 291..293
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 296..310
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:3FVC"
FT TURN 320..323
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 324..329
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 344..356
FT /evidence="ECO:0007829|PDB:3FVC"
FT TURN 357..361
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 362..368
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 379..387
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 458..498
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 502..510
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 516..519
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 522..525
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 556..560
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 567..572
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 576..579
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 593..598
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 601..606
FT /evidence="ECO:0007829|PDB:3FVC"
FT STRAND 609..615
FT /evidence="ECO:0007829|PDB:3FVC"
FT TURN 616..618
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 646..650
FT /evidence="ECO:0007829|PDB:3FVC"
FT HELIX 657..673
FT /evidence="ECO:0007829|PDB:3FVC"
SQ SEQUENCE 857 AA; 95639 MW; D9BCE9487D8A1411 CRC64;
MTRRRVLSVV VLLAALACRL GAQTPEQPAP PATTVQPTAT RQQTSFPFRV CELSSHGDLF
RFSSDIQCPS FGTRENHTEG LLMVFKDNII PYSFKVRSYT KIVTNILIYN GWYADSVTNR
HEEKFSVDSY ETDQMDTIYQ CYNAVKMTKD GLTRVYVDRD GVNITVNLKP TGGLANGVRR
YASQTELYDA PGWLIWTYRT RTTVNCLITD MMAKSNSPFD FFVTTTGQTV EMSPFYDGKN
KETFHERADS FHVRTNYKIV DYDNRGTNPQ GERRAFLDKG TYTLSWKLEN RTAYCPLQHW
QTFDSTIATE TGKSIHFVTD EGTSSFVTNT TVGIELPDAF KCIEEQVNKT MHEKYEAVQD
RYTKGQEAIT YFITSGGLLL AWLPLTPRSL ATVKNLTELT TPTSSPPSSP SPPAPSAARG
STPAAVLRRR RRDAGNATTP VPPTAPGKSL GTLNNPATVQ IQFAYDSLRR QINRMLGDLA
RAWCLEQKRQ NMVLRELTKI NPTTVMSSIY GKAVAAKRLG DVISVSQCVP VNQATVTLRK
SMRVPGSETM CYSRPLVSFS FINDTKTYEG QLGTDNEIFL TKKMTEVCQA TSQYYFQSGN
EIHVYNDYHH FKTIELDGIA TLQTFISLNT SLIENIDFAS LELYSRDEQR ASNVFDLEGI
FREYNFQAQN IAGLRKDLDN AVSNGRNQFV DGLGELMDSL GSVGQSITNL VSTVGGLFSS
LVSGFISFFK NPFGGMLILV LVAGVVILVI SLTRRTRQMS QQPVQMLYPG IDELAQQHAS
GEGPGINPIS KTELQAIMLA LHEQNQEQKR AAQRAAGPSV ASRALQAARD RFPGLRRRRY
HDPETAAALL GEAETEF
