GL_HCMV8
ID GL_HCMV8 Reviewed; 278 AA.
AC Q68674;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 25-MAY-2022, entry version 69.
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 5508) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=69168;
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.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.02 ANGSTROMS) OF 1-278.
RX PubMed=28783665; DOI=10.1126/sciimmunol.aan1457;
RA Chandramouli S., Malito E., Nguyen T., Luisi K., Donnarumma D., Xing Y.,
RA Norais N., Yu D., Carfi A.;
RT "Structural basis for potent antibody-mediated neutralization of human
RT cytomegalovirus.";
RL Sci. Immunol. 2:0-0(2017).
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}.
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DR EMBL; U56919; AAA99170.1; -; Genomic_DNA.
DR RefSeq; YP_081555.1; NC_006273.2.
DR PDB; 5VOB; X-ray; 3.02 A; B=1-278.
DR PDB; 5VOC; X-ray; 3.99 A; B=1-278.
DR PDB; 5VOD; X-ray; 5.90 A; B=1-278.
DR PDBsum; 5VOB; -.
DR PDBsum; 5VOC; -.
DR PDBsum; 5VOD; -.
DR SMR; Q68674; -.
DR DNASU; 3077416; -.
DR GeneID; 3077416; -.
DR KEGG; vg:3077416; -.
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 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;
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..30
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT CHAIN 31..278
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT /id="PRO_0000038287"
FT HELIX 47..56
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5VOB"
FT TURN 96..98
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 118..126
FT /evidence="ECO:0007829|PDB:5VOB"
FT TURN 129..132
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 133..142
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 145..166
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:5VOB"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:5VOB"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 220..235
FT /evidence="ECO:0007829|PDB:5VOB"
FT HELIX 241..252
FT /evidence="ECO:0007829|PDB:5VOB"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:5VOB"
FT STRAND 269..271
FT /evidence="ECO:0007829|PDB:5VOB"
SQ SEQUENCE 278 AA; 30815 MW; E2D256850D42F74D CRC64;
MCRRPDCGFS FSPGPVILLW CCLLLPIVSS AAVSVAPTAA EKVPAECPEL TRRCLLGEVF
EGDKYESWLR PLVNVTGRDG PLSQLIRYRP VTPEAANSVL LDEAFLDTLA LLYNNPDQLR
ALLTLLSSDT APRWMTVMRG YSECGDGSPA VYTCVDDLCR GYDLTRLSYG RSIFTEHVLG
FELVPPSLFN VVVAIRNEAT RTNRAVRLPV STAAAPEGIT LFYGLYNAVK EFCLRHQLDP
PLLRHLDKYY AGLPPELKQT RVNLPAHSRY GPQAVDAR
