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 10-OCT-2018, entry version 75. 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; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae; OC 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; 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}; 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 SMR; P16832; -. DR OrthoDB; VOG090000M7; -. 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: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 //