GL_HCMVM
ID GL_HCMVM Reviewed; 278 AA.
AC F5HCH8;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 35.
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}; ORFNames=UL115;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
RN [2]
RP INTERACTION WITH UL128; UL130; UL131 AND GH.
RC STRAIN=TR;
RX PubMed=17942555; DOI=10.1128/jvi.01910-07;
RA Ryckman B.J., Rainish B.L., Chase M.C., Borton J.A., Nelson J.A.,
RA Jarvis M.A., Johnson D.C.;
RT "Characterization of the human cytomegalovirus gH/gL/UL128-131 complex that
RT mediates entry into epithelial and endothelial cells.";
RL J. Virol. 82:60-70(2008).
RN [3]
RP FUNCTION, AND INTERACTION WITH GH AND PDGFRA.
RX PubMed=28403202; DOI=10.1371/journal.ppat.1006281;
RA Wu Y., Prager A., Boos S., Resch M., Brizic I., Mach M., Wildner S.,
RA Scrivano L., Adler B.;
RT "Human cytomegalovirus glycoprotein complex gH/gL/gO uses PDGFR-alpha as a
RT key for entry.";
RL PLoS Pathog. 13:E1006281-E1006281(2017).
RN [4]
RP FUNCTION, AND INTERACTION WITH HOST NRP2.
RX PubMed=30057110; DOI=10.1016/j.cell.2018.06.028;
RA Martinez-Martin N., Marcandalli J., Huang C.S., Arthur C.P., Perotti M.,
RA Foglierini M., Ho H., Dosey A.M., Shriver S., Payandeh J., Leitner A.,
RA Lanzavecchia A., Perez L., Ciferri C.;
RT "An Unbiased Screen for Human Cytomegalovirus Identifies Neuropilin-2 as a
RT Central Viral Receptor.";
RL Cell 0:0-0(2018).
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
CC (PubMed:28403202). The gH-gL-UL128-UL130-UL131A pentamer is essential
CC for viral entry in epithelial, endothelial and myeloid cells via
CC interaction with host NRP2 (PubMed:30057110). {ECO:0000255|HAMAP-
CC Rule:MF_04036, ECO:0000269|PubMed:28403202,
CC ECO:0000269|PubMed:30057110}.
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 (PubMed:17942555). The pentamer
CC interacts with host NRP2 (PubMed:30057110). Forms the envelope trimer
CC complex composed of gH, gL, and gO. The trimer interacts with host
CC PDGFRA (PubMed:28403202). {ECO:0000255|HAMAP-Rule:MF_04036,
CC ECO:0000269|PubMed:17942555, ECO:0000269|PubMed:28403202,
CC ECO:0000269|PubMed:30057110}.
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; AY446894; AAR31659.1; -; Genomic_DNA.
DR RefSeq; YP_081555.1; NC_006273.2.
DR PDB; 7LBE; EM; 2.90 A; B=1-278.
DR PDB; 7LBF; EM; 2.80 A; B=1-278.
DR PDB; 7LBG; EM; 2.60 A; B=1-278.
DR PDBsum; 7LBE; -.
DR PDBsum; 7LBF; -.
DR PDBsum; 7LBG; -.
DR SMR; F5HCH8; -.
DR TCDB; 1.G.22.1.1; the cytomegalovirus (human herpesvirus 5) glycoprotein go (go) family.
DR PRIDE; F5HCH8; -.
DR DNASU; 3077416; -.
DR GeneID; 3077416; -.
DR KEGG; vg:3077416; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR Proteomes; UP000000938; 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:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0019031; C:viral envelope; TAS:Reactome.
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; Reference proteome; Signal;
KW Viral attachment to host cell; Viral attachment to host entry receptor;
KW Viral envelope protein; Viral penetration into host cytoplasm; Virion;
KW 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_0000416445"
FT HELIX 47..55
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 77..79
FT /evidence="ECO:0007829|PDB:7LBF"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:7LBE"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 103..112
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 118..127
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 169..171
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:7LBF"
FT STRAND 176..184
FT /evidence="ECO:0007829|PDB:7LBG"
FT TURN 185..187
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 188..197
FT /evidence="ECO:0007829|PDB:7LBG"
FT TURN 198..201
FT /evidence="ECO:0007829|PDB:7LBG"
FT STRAND 202..211
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 216..218
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 219..235
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 241..251
FT /evidence="ECO:0007829|PDB:7LBG"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:7LBG"
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
