ID   GL_HHV7J                Reviewed;         246 AA.
AC   P52509;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 76.
DE   RecName: Full=Envelope glycoprotein L {ECO:0000255|HAMAP-Rule:MF_04036};
DE            Short=gL {ECO:0000255|HAMAP-Rule:MF_04036};
DE   Flags: Precursor;
GN   Name=gL {ECO:0000255|HAMAP-Rule:MF_04036}; Synonyms=U82;
OS   Human herpesvirus 7 (strain JI) (HHV-7) (Human T lymphotropic virus).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX   NCBI_TaxID=57278;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=8709220; DOI=10.1128/jvi.70.9.5975-5989.1996;
RA   Nicholas J.;
RT   "Determination and analysis of the complete nucleotide sequence of human
RT   herpesvirus.";
RL   J. Virol. 70:5975-5989(1996).
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_04036}.
CC   -!- SUBUNIT: Interacts with glycoprotein H (gH); this interaction is
CC       necessary for the correct processing and cell surface expression of gH.
CC       {ECO:0000255|HAMAP-Rule:MF_04036}.
CC   -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04036}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04036}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04036}.
CC       Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04036}; Peripheral
CC       membrane protein {ECO:0000255|HAMAP-Rule:MF_04036}; Extracellular side
CC       {ECO:0000255|HAMAP-Rule:MF_04036}. Host Golgi apparatus, host trans-
CC       Golgi network {ECO:0000255|HAMAP-Rule:MF_04036}. 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_04036}.
CC   -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L family.
CC       {ECO:0000255|HAMAP-Rule:MF_04036}.
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DR   EMBL; U43400; AAC54744.1; -; Genomic_DNA.
DR   PIR; T41984; T41984.
DR   SMR; P52509; -.
DR   Proteomes; UP000009246; 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   HAMAP; MF_04036; HSV_GL_betahv; 1.
DR   InterPro; IPR002689; Cytomegalo_gL.
DR   Pfam; PF01801; Cytomega_gL; 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..19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT   CHAIN           20..246
FT                   /note="Envelope glycoprotein L"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT                   /id="PRO_0000038270"
SQ   SEQUENCE   246 AA;  29259 MW;  82358B538CC33E12 CRC64;
     MKTNIFFIFL ISILNQIYAL FNNSYYSNLE QECIKNILNC TQSKTLSLLE PIDQAPIPKS
     DIISRLLYHT PYISRRDQVL IDEDFLETFY LLYNNPNQLH TLLSLIKDSE SGHNWLGFLN
     NFERCLSDNT LLTCRDNVCK SYSYEKLKFT GNIFVENIIG FEFNIPSNMI NFNMSILIYL
     ENEETRTQRI VRIDHHGINV FDALLNCLRY FSRYYNFSFP LIQEMEKYNE VLPFRSEFSN
     LLIRTY