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}; 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; 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 //