GL_EBVB9
ID GL_EBVB9 Reviewed; 137 AA.
AC P03212; Q777E0;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=Envelope glycoprotein L {ECO:0000255|HAMAP-Rule:MF_04034};
DE Short=gL {ECO:0000255|HAMAP-Rule:MF_04034};
DE Flags: Precursor;
GN Name=gL {ECO:0000255|HAMAP-Rule:MF_04034}; ORFNames=BKRF2;
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 [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 [2]
RP SUBCELLULAR LOCATION.
RX PubMed=7539502; DOI=10.1128/jvi.69.7.3987-3994.1995;
RA Li Q., Turk S.M., Hutt-Fletcher L.M.;
RT "The Epstein-Barr virus (EBV) BZLF2 gene product associates with the gH and
RT gL homologs of EBV and carries an epitope critical to infection of B cells
RT but not of epithelial cells.";
RL J. Virol. 69:3987-3994(1995).
RN [3]
RP INTERACTION WITH GH AND GP42.
RX PubMed=9621012; DOI=10.1128/jvi.72.7.5552-5558.1998;
RA Wang X., Kenyon W.J., Li Q., Mullberg J., Hutt-Fletcher L.M.;
RT "Epstein-Barr virus uses different complexes of glycoproteins gH and gL to
RT infect B lymphocytes and epithelial cells.";
RL J. Virol. 72:5552-5558(1998).
RN [4]
RP FUNCTION.
RX PubMed=11562531; DOI=10.1099/0022-1317-82-10-2373;
RA Maruo S., Yang L., Takada K.;
RT "Roles of Epstein-Barr virus glycoproteins gp350 and gp25 in the infection
RT of human epithelial cells.";
RL J. Gen. Virol. 82:2373-2383(2001).
RN [5]
RP SUBCELLULAR LOCATION.
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 [6]
RP FUNCTION, AND INTERACTION WITH HOST EPHA2.
RX PubMed=29292383; DOI=10.1038/s41564-017-0080-8;
RA Zhang H., Li Y., Wang H.B., Zhang A., Chen M.L., Fang Z.X., Dong X.D.,
RA Li S.B., Du Y., Xiong D., He J.Y., Li M.Z., Liu Y.M., Zhou A.J., Zhong Q.,
RA Zeng Y.X., Kieff E., Zhang Z., Gewurz B.E., Zhao B., Zeng M.S.;
RT "Ephrin receptor A2 is an epithelial cell receptor for Epstein-Barr virus
RT entry.";
RL Nat. Microbiol. 3:1-8(2018).
RN [7]
RP FUNCTION, AND INTERACTION WITH HOST EPHA2.
RX PubMed=29292384; DOI=10.1038/s41564-017-0081-7;
RA Chen J., Sathiyamoorthy K., Zhang X., Schaller S., Perez White B.E.,
RA Jardetzky T.S., Longnecker R.;
RT "Ephrin receptor A2 is a functional entry receptor for Epstein-Barr
RT virus.";
RL Nat. Microbiol. 3:172-180(2018).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (3.58 ANGSTROMS) OF 24-131, AND DISULFIDE BOND.
RX PubMed=21149717; DOI=10.1073/pnas.1011806108;
RA Matsuura H., Kirschner A.N., Longnecker R., Jardetzky T.S.;
RT "Crystal structure of the Epstein-Barr virus (EBV) glycoprotein
RT H/glycoprotein L (gH/gL) complex.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:22641-22646(2010).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 24-135.
RX PubMed=27929061; DOI=10.1038/ncomms13557;
RA Sathiyamoorthy K., Hu Y.X., Moehl B.S., Chen J., Longnecker R.,
RA Jardetzky T.S.;
RT "Structural basis for Epstein-Barr virus host cell tropism mediated by gp42
RT and gHgL entry glycoproteins.";
RL Nat. Commun. 7:13557-13557(2016).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 24-137.
RX PubMed=28939750; DOI=10.1073/pnas.1704661114;
RA Sathiyamoorthy K., Jiang J., Moehl B.S., Chen J., Zhou Z.H., Longnecker R.,
RA Jardetzky T.S.;
RT "Inhibition of EBV-mediated membrane fusion by anti-gHgL antibodies.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:703-710(2017).
CC -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is required for
CC the fusion of viral and plasma membranes leading to virus entry into
CC the host cell. Acts as a functional inhibitor of gH and maintains gH in
CC an inhibited form. Upon binding to host integrins, gL dissociates from
CC gH leading to activation of the viral fusion glycoproteins gB and gH.
CC Fusion of EBV with B-lymphocytes requires the additional receptor-
CC binding protein gp42, which forms a complex with gH/gL. The heterodimer
CC gH/gL targets also host EPHA2 to promote viral entry.
CC {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:11562531,
CC ECO:0000269|PubMed:29292383, ECO:0000269|PubMed:29292384}.
CC -!- SUBUNIT: Interacts with glycoprotein H (gH); this interaction is
CC necessary for the correct processing and cell surface expression of gH.
CC The heterodimer gH/gL seems to interact with gB trimers during fusion.
CC The heterodimer gH/gL interacts with host EPHA2 to facilitate virus
CC internalization and fusion. {ECO:0000255|HAMAP-Rule:MF_04034,
CC ECO:0000269|PubMed:29292383, ECO:0000269|PubMed:29292384,
CC ECO:0000269|PubMed:9621012}.
CC -!- INTERACTION:
CC P03212; P03231: gH; NbExp=3; IntAct=EBI-15897767, EBI-15815779;
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04034}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04034}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04034}.
CC Host cell membrane {ECO:0000250, ECO:0000255|HAMAP-Rule:MF_04034,
CC ECO:0000269|PubMed:15534216, ECO:0000269|PubMed:7539502}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04034}; Extracellular side
CC {ECO:0000255|HAMAP-Rule:MF_04034}. Host Golgi apparatus, host trans-
CC Golgi network {ECO:0000255|HAMAP-Rule:MF_04034}. Note=gL associates
CC with the extravirion surface through its binding to gH. During virion
CC morphogenesis, this protein probably accumulates in the host trans-
CC Golgi where secondary envelopment occurs. {ECO:0000255|HAMAP-
CC Rule:MF_04034}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L family.
CC {ECO:0000255|HAMAP-Rule:MF_04034}.
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DR EMBL; V01555; CAA24817.1; -; Genomic_DNA.
DR EMBL; AJ507799; CAD53428.1; -; Genomic_DNA.
DR PIR; D43043; QQBE32.
DR RefSeq; YP_401678.1; NC_007605.1.
DR PDB; 3PHF; X-ray; 3.58 A; 2/4/6/B/D/F/H/J/L/N/P/R/T/V/X/Z=24-131.
DR PDB; 5T1D; X-ray; 3.10 A; B=24-135.
DR PDB; 5W0K; X-ray; 3.10 A; B/D=24-137.
DR PDB; 7CZE; X-ray; 3.00 A; B/D/F/H=24-132.
DR PDBsum; 3PHF; -.
DR PDBsum; 5T1D; -.
DR PDBsum; 5W0K; -.
DR PDBsum; 7CZE; -.
DR SMR; P03212; -.
DR DIP; DIP-47676N; -.
DR IntAct; P03212; 1.
DR PRIDE; P03212; -.
DR ABCD; P03212; 2 sequenced antibodies.
DR DNASU; 3783710; -.
DR GeneID; 3783710; -.
DR KEGG; vg:3783710; -.
DR SIGNOR; P03212; -.
DR EvolutionaryTrace; P03212; -.
DR Proteomes; UP000153037; Genome.
DR GO; GO:0044177; C:host cell Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0019031; C:viral envelope; IEA:UniProtKB-UniRule.
DR GO; GO:0055036; C:virion membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019064; P:fusion of virus membrane with host plasma membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR Gene3D; 3.10.390.20; -; 1.
DR HAMAP; MF_04034; HSV_GL_alphagamma; 1.
DR InterPro; IPR020175; Herpes_gL_rhadinovirus.
DR InterPro; IPR038313; Herpes_gL_rhadinovirus_sf.
DR InterPro; IPR034708; HSV_GL_alphagamma.
DR Pfam; PF11108; Phage_glycop_gL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Disulfide bond;
KW Fusion of virus membrane with host cell membrane;
KW Fusion of virus membrane with host membrane; Glycoprotein;
KW Host cell membrane; Host Golgi apparatus; Host membrane; Membrane;
KW Reference proteome; Signal; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT CHAIN 23..137
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000038273"
FT REGION 23..128
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT DISULFID 28..56
FT /evidence="ECO:0000269|PubMed:21149717"
FT DISULFID 29..79
FT /evidence="ECO:0000269|PubMed:21149717"
FT TURN 41..43
FT /evidence="ECO:0007829|PDB:7CZE"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:7CZE"
FT TURN 53..58
FT /evidence="ECO:0007829|PDB:7CZE"
FT STRAND 61..65
FT /evidence="ECO:0007829|PDB:7CZE"
FT TURN 70..73
FT /evidence="ECO:0007829|PDB:7CZE"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:7CZE"
FT HELIX 82..95
FT /evidence="ECO:0007829|PDB:7CZE"
FT TURN 96..99
FT /evidence="ECO:0007829|PDB:7CZE"
FT HELIX 102..117
FT /evidence="ECO:0007829|PDB:7CZE"
FT STRAND 120..122
FT /evidence="ECO:0007829|PDB:5T1D"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:7CZE"
FT TURN 128..131
FT /evidence="ECO:0007829|PDB:5T1D"
SQ SEQUENCE 137 AA; 15080 MW; F0C03CDACD1893A2 CRC64;
MRAVGVFLAI CLVTIFVLPT WGNWAYPCCH VTQLRAQHLL ALENISDIYL VSNQTCDGFS
LASLNSPKNG SNQLVISRCA NGLNVVSFFI SILKRSSSAL TGHLRELLTT LETLYGSFSV
EDLFGANLNR YAWHRGG
