GL_EBVA8
ID GL_EBVA8 Reviewed; 137 AA.
AC Q1HVF6;
DT 26-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 1.
DT 25-MAY-2022, entry version 58.
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 AG876) (HHV-4) (Human herpesvirus 4).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Lymphocryptovirus.
OX NCBI_TaxID=82830;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16490228; DOI=10.1016/j.virol.2006.01.015;
RA Dolan A., Addison C., Gatherer D., Davison A.J., McGeoch D.J.;
RT "The genome of Epstein-Barr virus type 2 strain AG876.";
RL Virology 350:164-170(2006).
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 The heterodimer gH/gL targets also host EPHA2 to promote viral entry.
CC {ECO:0000250|UniProtKB:P03212, ECO:0000255|HAMAP-Rule:MF_04034}.
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 -!- 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:0000255|HAMAP-Rule:MF_04034}; 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; DQ279927; ABB89252.1; -; Genomic_DNA.
DR RefSeq; YP_001129472.1; NC_009334.1.
DR PDB; 6C5V; EM; 4.80 A; B=24-137.
DR PDBsum; 6C5V; -.
DR SMR; Q1HVF6; -.
DR PRIDE; Q1HVF6; -.
DR ABCD; Q1HVF6; 1 sequenced antibody.
DR GeneID; 5176156; -.
DR KEGG; vg:5176156; -.
DR Proteomes; UP000007639; 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..25
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT CHAIN 26..137
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000375947"
FT REGION 23..128
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT DISULFID 28..56
FT /evidence="ECO:0000250|UniProtKB:P03212"
FT DISULFID 29..79
FT /evidence="ECO:0000250|UniProtKB:P03212"
SQ SEQUENCE 137 AA; 15098 MW; 79D0CCDADD086FDF CRC64;
MRTVGVFLAT CLVTIFVLPT WGNWAYPCCH VTQLRAQHLL ALENISDIYL VSNQTCDGFS
LASLNSPKNG SNQLVISRCA NGLNVVSFFI SILKRSSSAL TGHLRELLTT LETLYGSFSV
EDLFGANLNR YAWHRGG
