GL_HHV8P
ID GL_HHV8P Reviewed; 167 AA.
AC F5HDB7;
DT 16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 35.
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=47;
OS Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's
OS sarcoma-associated herpesvirus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Gammaherpesvirinae; Rhadinovirus.
OX NCBI_TaxID=868565;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10400794; DOI=10.1128/jvi.73.8.6953-6963.1999;
RA Glenn M., Rainbow L., Aurade F., Davison A., Schulz T.F.;
RT "Identification of a spliced gene from Kaposi's sarcoma-associated
RT herpesvirus encoding a protein with similarities to latent membrane
RT proteins 1 and 2A of Epstein-Barr virus.";
RL J. Virol. 73:6953-6963(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16760382; DOI=10.1099/vir.0.81919-0;
RA Rezaee S.A.R., Cunningham C., Davison A.J., Blackbourn D.J.;
RT "Kaposi's sarcoma-associated herpesvirus immune modulation: an overview.";
RL J. Gen. Virol. 87:1781-1804(2006).
RN [3]
RP FUNCTION.
RX PubMed=11932406; DOI=10.1128/jvi.76.9.4390-4400.2002;
RA Pertel P.E.;
RT "Human herpesvirus 8 glycoprotein B (gB), gH, and gL can mediate cell
RT fusion.";
RL J. Virol. 76:4390-4400(2002).
RN [4]
RP FUNCTION, AND INTERACTION WITH GLYCOPROTEIN H.
RX PubMed=18945775; DOI=10.1128/jvi.01170-08;
RA Hahn A., Birkmann A., Wies E., Dorer D., Mahr K., Sturzl M., Titgemeyer F.,
RA Neipel F.;
RT "Kaposi's sarcoma-associated herpesvirus gH/gL: glycoprotein export and
RT interaction with cellular receptors.";
RL J. Virol. 83:396-407(2009).
RN [5]
RP FUNCTION, AND INTERACTION WITH HOST EPHA2.
RX PubMed=22635007; DOI=10.1038/nm.2805;
RA Hahn A.S., Kaufmann J.K., Wies E., Naschberger E., Panteleev-Ivlev J.,
RA Schmidt K., Holzer A., Schmidt M., Chen J., Konig S., Ensser A., Myoung J.,
RA Brockmeyer N.H., Sturzl M., Fleckenstein B., Neipel F.;
RT "The ephrin receptor tyrosine kinase A2 is a cellular receptor for Kaposi's
RT sarcoma-associated herpesvirus.";
RL Nat. Med. 18:961-966(2012).
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 Targets heparan sulfate proteoglycans of the syndecan family as well as
CC host EPHA2 to promote viral entry. {ECO:0000255|HAMAP-Rule:MF_04034,
CC ECO:0000269|PubMed:11932406, ECO:0000269|PubMed:18945775,
CC ECO:0000269|PubMed:22635007}.
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 When in complex with gH, interacts with host EPHA2; this interaction
CC triggers EPHA2 phosphorylation and endocytosis, allowing virus entry.
CC {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:18945775,
CC ECO:0000269|PubMed:22635007}.
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; AF148805; ABD28897.1; -; Genomic_DNA.
DR RefSeq; YP_001129399.1; NC_009333.1.
DR PDB; 7B7N; X-ray; 2.69 A; L=21-167.
DR PDBsum; 7B7N; -.
DR SMR; F5HDB7; -.
DR BioGRID; 1776978; 18.
DR PRIDE; F5HDB7; -.
DR DNASU; 4961475; -.
DR GeneID; 4961475; -.
DR KEGG; vg:4961475; -.
DR Proteomes; UP000000942; 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; 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..20
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT CHAIN 21..167
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000423758"
FT REGION 18..131
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT REGION 142..167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT TURN 31..35
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:7B7N"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 54..56
FT /evidence="ECO:0007829|PDB:7B7N"
FT STRAND 59..66
FT /evidence="ECO:0007829|PDB:7B7N"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 77..89
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 92..94
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 97..115
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 119..122
FT /evidence="ECO:0007829|PDB:7B7N"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7B7N"
SQ SEQUENCE 167 AA; 17999 MW; F711D54C707A8106 CRC64;
MGIFALFAVL WTTLLVTSHA YVALPCCAIQ ASAASTLPLF FAVHSIHFAD PNHCNGVCIA
KLRSKTGDIT VETCVNGFNL RSFLVAVVRR LGSWASQENL RLLWYLQRSL TAYTVGFNAT
TADSSIHNVN IIIISVGKAM NRTGSVSGSQ TRAKSSSRRA HAGQKGK
