GL_HHV6U
ID GL_HHV6U Reviewed; 250 AA.
AC P52508;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 85.
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=EDLF3, U82;
OS Human herpesvirus 6A (strain Uganda-1102) (HHV-6 variant A) (Human B
OS lymphotropic virus).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Roseolovirus.
OX NCBI_TaxID=10370;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7941342; DOI=10.1006/viro.1994.1589;
RA Nicholas J.;
RT "Nucleotide sequence analysis of a 21-kbp region of the genome of human
RT herpesvirus-6 containing homologues of human cytomegalovirus major
RT immediate-early and replication genes.";
RL Virology 204:738-750(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=7747482; DOI=10.1006/viro.1995.1228;
RA Gompels U.A., Nicholas J., Lawrence G.L., Jones M., Thomson B.J.,
RA Martin M.E.D., Efstathiou S., Craxton M.A., Macaulay H.A.;
RT "The DNA sequence of human herpesvirus-6: structure, coding content, and
RT genome evolution.";
RL Virology 209:29-51(1995).
RN [3]
RP INTERACTION WITH GLYCOPROTEIN H, AND SUBCELLULAR LOCATION.
RX PubMed=8397282; DOI=10.1099/0022-1317-74-9-1847;
RA Liu D.X., Gompels U.A., Nicholas J., Lelliott C.;
RT "Identification and expression of the human herpesvirus 6 glycoprotein H
RT and interaction with an accessory 40K glycoprotein.";
RL J. Gen. Virol. 74:1847-1857(1993).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P52526, ECO:0000255|HAMAP-Rule:MF_04036}.
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. Found in Golgi-like bodies of
CC fibroblasts. In T-lymphocytes, found in the endoplasmic reticulum.
CC {ECO:0000255|HAMAP-Rule:MF_04036, ECO:0000269|PubMed:8397282}.
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; U13194; AAA68473.1; -; Genomic_DNA.
DR EMBL; X83413; CAA58331.1; -; Genomic_DNA.
DR PIR; JQ2165; JQ2165.
DR RefSeq; NP_042975.1; NC_001664.2.
DR SMR; P52508; -.
DR PRIDE; P52508; -.
DR DNASU; 1487962; -.
DR GeneID; 1487962; -.
DR KEGG; vg:1487962; -.
DR Proteomes; UP000009295; 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 1: Evidence at protein level;
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_0000038268"
SQ SEQUENCE 250 AA; 28962 MW; 224C80F4FD8031AA CRC64;
MELLLFVMSL ILLTFSKAIP LFNHNSFYFE KLDDCIAAVI NCTKSEVPLL LEPIYQPPAY
NEDVMSILLQ PPTKKKPFSR IMVTDEFLSD FLLLQDNPEQ LRTLFALIRD PESRDNWLNF
FNGFQTCSPS VGITTCIRDN CRKYSPEKIT YVNNFFVDNI AGLEFNISEN TDSFYSNIGF
LLYLENPAKG VTKIIRFPFN SLTLFDTILN CLKYFHLKTG VELDLLKHME TYNSKLPFRS
SRPTILIRNT
