ID   GL_HCMV1                Reviewed;         278 AA.
AC   Q68667;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 62.
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=UL115;
OS   Human cytomegalovirus (strain 119) (HHV-5) (Human herpesvirus 5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX   NCBI_TaxID=73483;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Milne R.S.B., Mathers K.E., Booth J.C.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
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       (By similarity). In human cytomegalovirus, forms two distincts
CC       complexes to mediate viral entry, a trimer and a pentamer at the
CC       surface of the virion envelope. The gH-gL-gO trimer is required for
CC       infection in fibroblasts by interacting with host PDGFRA. The gH-gL-
CC       UL128-UL130-UL131A pentamer is essential for viral entry in epithelial,
CC       endothelial and myeloid cells via interaction with host NRP2 (By
CC       similarity). {ECO:0000250|UniProtKB:F5HCH8, ECO:0000255|HAMAP-
CC       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       (By similarity). Forms the envelope pentamer complex (PC) composed of
CC       gH, gL, UL128, UL130, and UL131A. The pentamer interacts with host
CC       NRP2. Forms the envelope trimer complex composed of gH, gL, and gO. The
CC       trimer interacts with host PDGFRA (By similarity).
CC       {ECO:0000250|UniProtKB:F5HCH8, 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U56912; AAA99164.1; -; Genomic_DNA.
DR   SMR; Q68667; -.
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:0098670; P:entry receptor-mediated virion attachment to host cell; IEA:UniProtKB-KW.
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;
KW   Host-virus interaction; Membrane; Signal; Viral attachment to host cell;
KW   Viral attachment to host entry receptor; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT   SIGNAL          1..32
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT   CHAIN           33..278
FT                   /note="Envelope glycoprotein L"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT                   /id="PRO_0000038280"
SQ   SEQUENCE   278 AA;  30831 MW;  946D1E7E78AE1279 CRC64;
     MCRRPDCGFS FSPGPVILLW CCLLLSIVSS AAVNVAPTAA EKVPAECPEL TRRCLLGEVF
     QGDEYESWLR PLVNVTGRDG PLSQLIRYRP VTPEAANSVL LDEAFLDTLA LLYNNPDQLR
     ALLTLLSSDT APRWMTVMRG YSECGDGSPA VYTCVDDLCR GYDLTRLSYG RSIFTEHVLG
     FELVPPSLFN VVVAIRNEAT RTNRAVRLPV STAAAPEGIT LFYGLYNAVK EFCLRHQLDP
     PLLRHLDKYY AGLPPELKQT RVNLPAHSRY GPQAVDAR