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   05-JUN-2019, entry version 78.
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; Herpesvirales; Herpesviridae; Betaherpesvirinae;
OC   Cytomegalovirus.
OX   NCBI_TaxID=10360;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=2161319;
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
RT   in 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.,
RA   Alcendor D.J., McGeoch D.J., Hayward G.S.;
RT   "The human cytomegalovirus genome revisited: comparison with the
RT   chimpanzee cytomegalovirus genome.";
RL   J. Gen. Virol. 84:17-28(2003).
RN   [4]
RP   ERRATUM.
RA   Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
RA   Alcendor D.J., 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;
RA   Huber M.T., Compton T.;
RT   "The human cytomegalovirus UL74 gene encodes the third component of
RT   the 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:
RT   the HCMV proteome.";
RL   J. Virol. 78:10960-10966(2004).
RN   [7]
RP   ERRATUM.
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
RT   into epithelial cells.";
RL   J. Virol. 85:11638-11645(2011).
CC   -!- FUNCTION: The heterodimer glycoprotein H-glycoprotein L is
CC       required for the fusion of viral and plasma membranes leading to
CC       virus entry into the host cell. Acts as a functional inhibitor of
CC       gH and maintains gH in an inhibited form. Upon binding to host
CC       integrins, gL dissociates from gH leading to activation of the
CC       viral fusion glycoproteins gB and gH (By similarity). In human
CC       cytomegalovirus, forms two distincts complexes to mediate viral
CC       entry, a trimer and a pentamer at the surface of the virion
CC       envelope. The gH-gL-gO trimer is required for infection in
CC       fibroblasts by interacting with host PDGFRA. The gH-gL-UL128-
CC       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
CC       of gH (By similarity). Forms the envelope pentamer complex (PC)
CC       composed of gH, gL, UL128, UL130, and UL131A. The pentamer
CC       interacts with host NRP2. Forms the envelope trimer complex
CC       composed of gH, gL, and gO. The trimer interacts with host PDGFRA
CC       (By similarity) (PubMed:9733861, PubMed:21880752).
CC       {ECO:0000250|UniProtKB:F5HCH8, ECO:0000255|HAMAP-Rule:MF_04036,
CC       ECO:0000269|PubMed:21880752, 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-
CC       Rule:MF_04036}. Host cell membrane {ECO:0000255|HAMAP-
CC       Rule:MF_04036}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_04036}; Extracellular side {ECO:0000255|HAMAP-
CC       Rule:MF_04036}. Host Golgi apparatus, host trans-Golgi network
CC       {ECO:0000255|HAMAP-Rule:MF_04036, ECO:0000269|PubMed:21880752}.
CC       Note=gL associates with the extravirion surface through its
CC       binding to gH. During virion morphogenesis, this protein probably
CC       accumulates in the host trans-Golgi where secondary envelopment
CC       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   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: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   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   Complete proteome; 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;
KW   Viral attachment to host entry receptor; Viral envelope protein;
KW   Viral penetration into host cytoplasm; Virion;
KW   Virus entry into host cell.
FT   SIGNAL        1     30       {ECO:0000255|HAMAP-Rule:MF_04036}.
FT   CHAIN        31    278       Envelope glycoprotein L.
FT                                {ECO:0000255|HAMAP-Rule:MF_04036}.
FT                                /FTId=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
//