GL_VZVO
ID GL_VZVO Reviewed; 160 AA.
AC Q9J3N1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 64.
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 Oka vaccine) (HHV-3) (Human herpesvirus 3).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Varicellovirus.
OX NCBI_TaxID=341980;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=10720545; DOI=10.1086/315335;
RA Argaw T., Cohen J.I., Klutch M., Lekstrom K., Yoshikawa T., Asano Y.,
RA Krause P.R.;
RT "Nucleotide sequences that distinguish Oka vaccine from parental Oka and
RT other varicella-zoster virus isolates.";
RL J. Infect. Dis. 181:1153-1157(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=11162813; DOI=10.1006/viro.2000.0775;
RA Faga B., Maury W., Bruckner D.A., Grose C.;
RT "Identification and mapping of single nucleotide polymorphisms in the
RT varicella-zoster virus genome.";
RL Virology 280:1-6(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate Human/Japan/P-Oka/1970, and
RC Oka varicella vaccine Biken (V-Oka-Biken);
RX PubMed=12388706; DOI=10.1128/jvi.76.22.11447-11459.2002;
RA Gomi Y., Sunamachi H., Mori Y., Nagaike K., Takahashi M., Yamanishi K.;
RT "Comparison of the complete DNA sequences of the Oka varicella vaccine and
RT its parental virus.";
RL J. Virol. 76:11447-11459(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oka varicella vaccine VarilRix (V-Oka-GSK), and
RC Oka varicella vaccine Varivax (V-Oka-Merk);
RX PubMed=18787000; DOI=10.1128/jvi.00777-08;
RA Tillieux S.L., Halsey W.S., Thomas E.S., Voycik J.J., Sathe G.M.,
RA Vassilev V.;
RT "Complete DNA sequences of two oka strain varicella-zoster virus genomes.";
RL J. Virol. 82:11023-11044(2008).
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; AF206304; AAF61661.1; -; Genomic_DNA.
DR EMBL; AY016448; AAK19941.1; -; Genomic_DNA.
DR EMBL; AB097932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB097933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; DQ008354; AAY57669.1; -; Genomic_DNA.
DR EMBL; DQ008355; AAY57740.1; -; Genomic_DNA.
DR PDB; 4XHJ; X-ray; 3.16 A; B/F=23-160.
DR PDB; 4XI5; X-ray; 3.90 A; B=23-160.
DR PDBsum; 4XHJ; -.
DR PDBsum; 4XI5; -.
DR SMR; Q9J3N1; -.
DR IntAct; Q9J3N1; 28.
DR ABCD; Q9J3N1; 2 sequenced antibodies.
DR Proteomes; UP000002603; Genome.
DR Proteomes; UP000008504; Genome.
DR Proteomes; UP000008505; Genome.
DR Proteomes; UP000008506; 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 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; 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..160
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000385475"
FT REGION 24..149
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 50..53
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 68..70
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 79..82
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 94..98
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 100..110
FT /evidence="ECO:0007829|PDB:4XHJ"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:4XHJ"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 131..133
FT /evidence="ECO:0007829|PDB:4XHJ"
FT TURN 151..155
FT /evidence="ECO:0007829|PDB:4XHJ"
SQ SEQUENCE 160 AA; 17779 MW; 145DEEB8714565F6 CRC64;
MASHKWLLQM IVFLKTITIA YCLHLQDDTP LFFGAKPLSD VSLIITEPCV SSVYEAWDYA
APPVSNLSEA LSGIVVKTKC PVPEVILWFK DKQMAYWTNP YVTLKGLTQS VGEEHKSGDI
RDALLDALSG VWVDSTPSST NIPENGCVWG ADRLFQRVCQ
