ID   GL_HHV11                Reviewed;         224 AA.
AC   P10185; Q09ID2; Q76WT7;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 102.
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 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2846760; DOI=10.1099/0022-1317-69-11-2831;
RA   Perry L.J., McGeoch D.J.;
RT   "The DNA sequences of the long repeat region and adjoining parts of the
RT   long unique region in the genome of herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:2831-2846(1988).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nonneuroinvasive mutant HF10;
RX   PubMed=17218138; DOI=10.1016/j.micinf.2006.10.019;
RA   Ushijima Y., Luo C., Goshima F., Yamauchi Y., Kimura H., Nishiyama Y.;
RT   "Determination and analysis of the DNA sequence of highly attenuated herpes
RT   simplex virus type 1 mutant HF10, a potential oncolytic virus.";
RL   Microbes Infect. 9:142-149(2007).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17 syn+;
RA   Cunningham C., Davison A.J.;
RT   "Herpes simplex virus type 1 bacterial artificial chromosome.";
RL   Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   INTERACTION WITH GH.
RX   PubMed=12767993; DOI=10.1128/jvi.77.12.6731-6742.2003;
RA   Cairns T.M., Milne R.S., Ponce-de-Leon M., Tobin D.K., Cohen G.H.,
RA   Eisenberg R.J.;
RT   "Structure-function analysis of herpes simplex virus type 1 gD and gH-gL:
RT   clues from gDgH chimeras.";
RL   J. Virol. 77:6731-6742(2003).
RN   [6]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=F;
RX   PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA   Loret S., Guay G., Lippe R.;
RT   "Comprehensive characterization of extracellular herpes simplex virus type
RT   1 virions.";
RL   J. Virol. 82:8605-8618(2008).
RN   [7]
RP   FUNCTION.
RC   STRAIN=F;
RX   PubMed=19386594; DOI=10.1074/jbc.m109.005728;
RA   Gianni T., Amasio M., Campadelli-Fiume G.;
RT   "Herpes simplex virus gD forms distinct complexes with fusion executors gB
RT   and gH/gL in part through the C-terminal profusion domain.";
RL   J. Biol. Chem. 284:17370-17382(2009).
RN   [8]
RP   INTERACTION WITH GH, AND SUBCELLULAR LOCATION.
RX   PubMed=19726507; DOI=10.1128/jvi.01369-09;
RA   Fan Q., Lin E., Spear P.G.;
RT   "Insertional mutations in herpes simplex virus 1 gL identify functional
RT   domains for association with gH and for membrane fusion.";
RL   J. Virol. 83:11607-11615(2009).
RN   [9]
RP   SUBCELLULAR LOCATION.
RX   PubMed=25746217; DOI=10.3390/v7030915;
RA   Lau S.Y., Crump C.M.;
RT   "HSV-1 gM and the gK/pUL20 complex are important for the localization of gD
RT   and gH/L to viral assembly sites.";
RL   Viruses 7:915-938(2015).
RN   [10]
RP   FUNCTION.
RX   PubMed=26157134; DOI=10.1073/pnas.1506846112;
RA   Gianni T., Massaro R., Campadelli-Fiume G.;
RT   "Dissociation of HSV gL from gH by alphavbeta6- or alphavbeta8-integrin
RT   promotes gH activation and virus entry.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:E3901-3910(2015).
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, ECO:0000269|PubMed:19386594,
CC       ECO:0000269|PubMed:26157134}.
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:12767993}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04034,
CC       ECO:0000269|PubMed:18596102}; Peripheral membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_04034}; Extracellular side
CC       {ECO:0000255|HAMAP-Rule:MF_04034}. Host cell membrane
CC       {ECO:0000255|HAMAP-Rule:MF_04034, ECO:0000269|PubMed:25746217};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04034};
CC       Extracellular side {ECO:0000255|HAMAP-Rule:MF_04034}. Host Golgi
CC       apparatus, host trans-Golgi network {ECO:0000255|HAMAP-Rule:MF_04034}.
CC       Note=gL associates with the extravirion surface through its binding to
CC       gH. During virion morphogenesis, this protein probably accumulates in
CC       the host trans-Golgi where secondary envelopment occurs.
CC       {ECO:0000255|HAMAP-Rule:MF_04034}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L (gL) family.
CC       Alphaherpesvirinae gL subfamily. {ECO:0000255|PROSITE-
CC       ProRule:PRU01368}.
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DR   EMBL; X14112; CAA32337.1; -; Genomic_DNA.
DR   EMBL; D00373; BAA00272.1; -; Genomic_DNA.
DR   EMBL; DQ889502; ABI63463.1; -; Genomic_DNA.
DR   EMBL; FJ593289; ACM62223.1; -; Genomic_DNA.
DR   PIR; A28133; WMBEX1.
DR   RefSeq; YP_009137075.1; NC_001806.2.
DR   SMR; P10185; -.
DR   BioGRID; 971430; 1.
DR   ChEMBL; CHEMBL2364696; -.
DR   DrugCentral; P10185; -.
DR   TCDB; 1.G.10.1.1; the herpes simplex virus membrane fusion complex (hsv-mfc) family.
DR   DNASU; 2703393; -.
DR   GeneID; 2703393; -.
DR   KEGG; vg:2703393; -.
DR   PRO; PR:P10185; -.
DR   Proteomes; UP000009294; Genome.
DR   Proteomes; UP000180652; 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; 3.30.390.170; -; 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.
DR   PROSITE; PS52024; GL_AHV; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT   CHAIN           20..224
FT                   /note="Envelope glycoprotein L"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT                   /id="PRO_0000038264"
FT   DOMAIN          23..201
FT                   /note="gL alphaherpesvirus-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01368"
FT   REGION          20..161
FT                   /note="Interaction with gH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT   REGION          161..224
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        44..76
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01368"
FT   DISULFID        149..160
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01368"
FT   VARIANT         90
FT                   /note="K -> R (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         100
FT                   /note="V -> G (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         109
FT                   /note="Y -> H (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         115
FT                   /note="N -> D (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         168
FT                   /note="P -> L (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         171
FT                   /note="G -> R (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         181
FT                   /note="P -> S (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         196
FT                   /note="P -> S (in strain: Nonneuroinvasive mutant HF10)"
FT   VARIANT         224
FT                   /note="L -> I (in strain: Nonneuroinvasive mutant HF10)"
SQ   SEQUENCE   224 AA;  24934 MW;  CED51D2FC1D7777F CRC64;
     MGILGWVGLI AVGVLCVRGG LPSTEYVIRS RVAREVGDIL KVPCVPLPSD DLDWRYETPS
     AINYALIDGI FLRYHCPGLD TVLWDRHAQK AYWVNPFLFV AGFLEDLSYP AFPANTQETE
     TRLALYKEIR QALDSRKQAA SHTPVKAGCV NFDYSRTRRC VGRQDLGPTN GTSGRTPVLP
     PDDEAGLQPK PLTTPPPIIA TSDPTPRRDA ATKSRRRRPH SRRL
//