GL_HHV1K
ID GL_HHV1K Reviewed; 224 AA.
AC Q96912;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, 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=UL1;
OS Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10306;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=KOS, and mutant 804;
RX PubMed=8661409; DOI=10.1006/viro.1996.0347;
RA Novotny M.J., Parish M.L., Spear P.G.;
RT "Variability of herpes simplex virus 1 gL and anti-gL antibodies that
RT inhibit cell fusion but not viral infectivity.";
RL Virology 221:1-13(1996).
RN [2]
RP INTERACTION WITH GH, AND GLYCOSYLATION.
RC STRAIN=KOS;
RX PubMed=9621073; DOI=10.1128/jvi.72.7.6092-6103.1998;
RA Peng T., Ponce de Leon M., Novotny M.J., Jiang H., Lambris J.D., Dubin G.,
RA Spear P.G., Cohen G.H., Eisenberg R.J.;
RT "Structural and antigenic analysis of a truncated form of the herpes
RT simplex virus glycoprotein gH-gL complex.";
RL J. Virol. 72:6092-6103(1998).
RN [3]
RP INTERACTION OF GH/GL HETERODIMER WITH GB.
RX PubMed=18003913; DOI=10.1073/pnas.0707452104;
RA Atanasiu D., Whitbeck J.C., Cairns T.M., Reilly B., Cohen G.H.,
RA Eisenberg R.J.;
RT "Bimolecular complementation reveals that glycoproteins gB and gH/gL of
RT herpes simplex virus interact with each other during cell fusion.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:18718-18723(2007).
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 {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 {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:18003913,
CC ECO:0000269|PubMed:9621073}.
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 -!- PTM: N-glycosylated, O-glycosylated, and sialylated.
CC {ECO:0000305|PubMed:9621073}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L family.
CC {ECO:0000255|HAMAP-Rule:MF_04034}.
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DR EMBL; U53683; AAA99790.1; -; Genomic_DNA.
DR SMR; Q96912; -.
DR iPTMnet; Q96912; -.
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; 3.30.390.170; -; 1.
DR HAMAP; MF_04034; HSV_GL_alphagamma; 1.
DR InterPro; IPR022200; Herpes_gL_C.
DR InterPro; IPR007923; Herpes_gL_N.
DR InterPro; IPR038311; Herpes_gL_N_sf.
DR InterPro; IPR034708; HSV_GL_alphagamma.
DR Pfam; PF12524; GlyL_C; 1.
DR Pfam; PF05259; Herpes_UL1; 1.
PE 1: Evidence at protein level;
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; Signal;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW Virus entry into host cell.
FT SIGNAL 1..22
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT CHAIN 23..224
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000385474"
FT REGION 20..161
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT REGION 20..161
FT /note="Interaction with gL"
FT REGION 161..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 170
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000269|PubMed:9621073"
SQ SEQUENCE 224 AA; 24897 MW; 4056711229B15023 CRC64;
MGILGWVGLI AVGVLCVRGG LSSTEYVIRS RVAREVGDIL KVPCVPLPSD DLDWRYETPS
AINYALIDGI FLRYHCPGLD TVLWDRHAQK AYWVNPFLFV AGFLEDLSHP AFPANTQETE
TRLALYKEIR QALDSRKQAA SHTPVKAGCV NFDYSRTRRC VGRQDLGPTN GTSGRTPVLP
PDDEAGLQPK PLTTPPPIIA TSDPTPRRDA ATKSRRRRPH SRRL
