GL_HHV6Z
ID GL_HHV6Z Reviewed; 250 AA.
AC P52526;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=CB10L, U82;
OS Human herpesvirus 6B (strain Z29) (HHV-6 variant B) (Human B lymphotropic
OS virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=36351;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8634027; DOI=10.1007/bf01718406;
RA Lindquester G.J., Inoue N., Allen R.D., Castelli J.W., Stamey F.R.,
RA Dambaugh T.R., O'Brian J.J., Danovich R.M., Frenkel N., Pellett P.E.;
RT "Restriction endonuclease mapping and molecular cloning of the human
RT herpesvirus 6 variant B strain Z29 genome.";
RL Arch. Virol. 141:367-379(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10482553; DOI=10.1128/jvi.73.10.8040-8052.1999;
RA Dominguez G., Dambaugh T.R., Stamey F.R., Dewhurst S., Inoue N.,
RA Pellett P.E.;
RT "Human herpesvirus 6B genome sequence: coding content and comparison with
RT human herpesvirus 6A.";
RL J. Virol. 73:8040-8052(1999).
RN [3]
RP IDENTIFICATION IN COMPLEX WITH GLYCOPROTEIN O AND GLYCOPROTEIN H.
RC STRAIN=HST;
RX PubMed=15078943; DOI=10.1128/jvi.78.9.4609-4616.2004;
RA Mori Y., Akkapaiboon P., Yonemoto S., Koike M., Takemoto M., Sadaoka T.,
RA Sasamoto Y., Konishi S., Uchiyama Y., Yamanishi K.;
RT "Discovery of a second form of tripartite complex containing gH-gL of human
RT herpesvirus 6 and observations on CD46.";
RL J. Virol. 78:4609-4616(2004).
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 {ECO:0000255|HAMAP-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). Part of a gH-gL-gO complex (PubMed:15078943).
CC {ECO:0000255|HAMAP-Rule:MF_04036, ECO:0000269|PubMed:15078943}.
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}.
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; AF157706; AAB06366.1; -; Genomic_DNA.
DR PIR; T44227; T44227.
DR RefSeq; NP_050261.1; NC_000898.1.
DR SMR; P52526; -.
DR PRIDE; P52526; -.
DR DNASU; 1497082; -.
DR GeneID; 1497082; -.
DR KEGG; vg:1497082; -.
DR Proteomes; UP000006930; 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: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 3: Inferred from homology;
KW 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; Membrane;
KW Reference proteome; Signal; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT CHAIN 19..250
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04036"
FT /id="PRO_0000038269"
SQ SEQUENCE 250 AA; 28904 MW; 0DE7723F50194104 CRC64;
MELLLFVMSL ILLTFSKAMP LFDHNSFYFE KLDDCIAAVI NCTRSEVPLL LEPIYQPPVY
NEDVMSILLK PPTKKKPFSR IMVTNEFLSD FLLLQDNPEQ LRTLFALIGD PESRDNWLNF
FNGFQTCSPS VGITTCISDN CRKYLPERIT YVNNFFVDNI AGLEFNISEN TDSFYSNIGF
LLYLENPATG ITKIIRFPFN SLTLFDTILN CLKYFHLKTG VEFDLLKQME AYNSKLPFRS
SRPTILIRNT