ID   GL_VZVD                 Reviewed;         159 AA.
AC   P09308;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   25-MAY-2022, entry version 79.
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=ORF60;
OS   Varicella-zoster virus (strain Dumas) (HHV-3) (Human herpesvirus 3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX   NCBI_TaxID=10338;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=3018124; DOI=10.1099/0022-1317-67-9-1759;
RA   Davison A.J., Scott J.E.;
RT   "The complete DNA sequence of varicella-zoster virus.";
RL   J. Gen. Virol. 67:1759-1816(1986).
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}.
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; X04370; CAA27943.1; -; Genomic_DNA.
DR   PIR; H27215; WZBE60.
DR   SMR; P09308; -.
DR   PRIDE; P09308; -.
DR   Proteomes; UP000002602; 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; IPR007923; Herpes_gL_N.
DR   InterPro; IPR038311; Herpes_gL_N_sf.
DR   InterPro; IPR034708; HSV_GL_alphagamma.
DR   Pfam; PF05259; Herpes_UL1; 1.
PE   3: Inferred from homology;
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..21
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT   CHAIN           22..159
FT                   /note="Envelope glycoprotein L"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT                   /id="PRO_0000038272"
FT   REGION          23..148
FT                   /note="Interaction with gH"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
SQ   SEQUENCE   159 AA;  17617 MW;  E5C9093B1DE83ACB CRC64;
     MASHKWLLQI VFLKTITIAY CLHLQDDTPL FFGAKPLSDV SLIITEPCVS SVYEAWDYAA
     PPVSNLSEAL SGIVVKTKCP VPEVILWFKD KQMAYWTNPY VTLKGLAQSV GEEHKSGDIR
     DALLDALSGV WVDSTPSSTN IPENGCVWGA DRLFQRVCQ