GL_HCMVA
ID GL_HCMVA Reviewed; 278 AA.
AC P16832; Q7M6S9;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 25-MAY-2022, entry version 87.
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 AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12368327; DOI=10.1128/jvi.76.21.10841-10848.2002;
RA Rasmussen L., Geissler A., Cowan C., Chase A., Winters M.;
RT "The genes encoding the gCIII complex of human cytomegalovirus exist in
RT highly diverse combinations in clinical isolates.";
RL J. Virol. 76:10841-10848(2002).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Isolate 650, and Isolate 813;
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP IDENTIFICATION IN A COMPLEX WITH GO AND GH.
RX PubMed=9733861; DOI=10.1128/jvi.72.10.8191-8197.1998;
RA Huber M.T., Compton T.;
RT "The human cytomegalovirus UL74 gene encodes the third component of the
RT glycoprotein H-glycoprotein L-containing envelope complex.";
RL J. Virol. 72:8191-8197(1998).
RN [6]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [7]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [8]
RP INTERACTION WITH GO, AND SUBCELLULAR LOCATION.
RX PubMed=21880752; DOI=10.1128/jvi.05659-11;
RA Vanarsdall A.L., Chase M.C., Johnson D.C.;
RT "Human cytomegalovirus glycoprotein gO complexes with gH/gL, promoting
RT interference with viral entry into human fibroblasts but not entry into
RT epithelial cells.";
RL J. Virol. 85:11638-11645(2011).
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) (PubMed:9733861,
CC PubMed:21880752). {ECO:0000250|UniProtKB:F5HCH8, ECO:0000255|HAMAP-
CC Rule:MF_04036, ECO:0000269|PubMed:21880752,
CC ECO:0000269|PubMed:9733861}.
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,
CC ECO:0000269|PubMed:21880752}. Note=gL associates with the extravirion
CC surface through its binding to gH. During virion morphogenesis, this
CC protein probably accumulates in the host trans-Golgi where secondary
CC envelopment occurs. {ECO:0000255|HAMAP-Rule:MF_04036}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L family.
CC {ECO:0000255|HAMAP-Rule:MF_04036}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35317.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X17403; CAA35317.1; ALT_INIT; Genomic_DNA.
DR EMBL; AF530171; AAM96168.1; -; Genomic_DNA.
DR EMBL; AF530172; AAM96169.1; -; Genomic_DNA.
DR EMBL; AF530173; AAM96170.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00105.1; -; Genomic_DNA.
DR PIR; S09882; S09882.
DR PDB; 7M30; EM; 3.81 A; B=31-278.
DR PDBsum; 7M30; -.
DR SMR; P16832; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; 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: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_0000038278"
SQ SEQUENCE 278 AA; 30913 MW; 9DD91A50BE0C25E5 CRC64;
MCRRPDCGFS FSPGPVVLLW CCLLLPIVSS VAVSVAPTAA EKVPAECPEL TRRCLLGEVF
QGDKYESWLR PLVNVTRRDG PLSQLIRYRP VTPEAANSVL LDDAFLDTLA LLYNNPDQLR
ALLTLLSSDT APRWMTVMRG YSECGDGSPA VYTCVDDLCR GYDLTRLSYG RSIFTEHVLG
FELVPPSLFN VVVAIRNEAT RTNRAVRLPV STAAAPEGIT LFYGLYNAVK EFCLRHQLDP
PLLRHLDKYY AGLPPELKQT RVNLPAHSRY GPQAVDAR
