GL_HHV2H
ID GL_HHV2H Reviewed; 224 AA.
AC P28278;
DT 01-DEC-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-1992, sequence version 1.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=Envelope glycoprotein L {ECO:0000255|HAMAP-Rule:MF_04034};
DE Short=gL {ECO:0000255|HAMAP-Rule:MF_04034};
DE Flags: Precursor;
GN Name=gL {ECO:0000255|HAMAP-Rule:MF_04034}; ORFNames=UL1;
OS Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Alphaherpesvirinae; Simplexvirus.
OX NCBI_TaxID=10315;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1662697; DOI=10.1099/0022-1317-72-12-3057;
RA McGeoch D.J., Cunningham C., McIntyre G., Dolan A.;
RT "Comparative sequence analysis of the long repeat regions and adjoining
RT parts of the long unique regions in the genomes of herpes simplex viruses
RT types 1 and 2.";
RL J. Gen. Virol. 72:3057-3075(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=9499055; DOI=10.1128/jvi.72.3.2010-2021.1998;
RA Dolan A., Jamieson F.E., Cunningham C., Barnett B.C., McGeoch D.J.;
RT "The genome sequence of herpes simplex virus type 2.";
RL J. Virol. 72:2010-2021(1998).
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_04034}.
CC -!- SUBUNIT: Interacts with glycoprotein H (gH); this interaction is
CC necessary for the correct processing and cell surface expression of gH.
CC The heterodimer gH/gL seems to interact with gB trimers during fusion.
CC {ECO:0000255|HAMAP-Rule:MF_04034}.
CC -!- SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-
CC Rule:MF_04034}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_04034}; Extracellular side {ECO:0000255|HAMAP-Rule:MF_04034}.
CC Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04034}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_04034}; Extracellular side
CC {ECO:0000255|HAMAP-Rule:MF_04034}. Host Golgi apparatus, host trans-
CC Golgi network {ECO:0000255|HAMAP-Rule:MF_04034}. 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_04034}.
CC -!- SIMILARITY: Belongs to the herpesviridae glycoprotein L family.
CC {ECO:0000255|HAMAP-Rule:MF_04034}.
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DR EMBL; D10470; BAA01264.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06761.1; -; Genomic_DNA.
DR PIR; JQ1494; WMBEHG.
DR RefSeq; YP_009137152.1; NC_001798.2.
DR PDB; 3M1C; X-ray; 3.00 A; B=21-224.
DR PDBsum; 3M1C; -.
DR SMR; P28278; -.
DR PRIDE; P28278; -.
DR DNASU; 1487292; -.
DR GeneID; 1487292; -.
DR KEGG; vg:1487292; -.
DR EvolutionaryTrace; P28278; -.
DR Proteomes; UP000001874; 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 Gene3D; 3.30.390.170; -; 1.
DR HAMAP; MF_04034; HSV_GL_alphagamma; 1.
DR InterPro; IPR022200; Herpes_gL_C.
DR InterPro; IPR007923; Herpes_gL_N.
DR InterPro; IPR038311; Herpes_gL_N_sf.
DR InterPro; IPR034708; HSV_GL_alphagamma.
DR Pfam; PF12524; GlyL_C; 1.
DR Pfam; PF05259; Herpes_UL1; 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; Membrane;
KW Reference proteome; Signal; Viral envelope protein;
KW Viral penetration into host cytoplasm; Virion; Virus entry into host cell.
FT SIGNAL 1..16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT CHAIN 17..224
FT /note="Envelope glycoprotein L"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT /id="PRO_0000038265"
FT REGION 20..161
FT /note="Interaction with gH"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04034"
FT REGION 168..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..196
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 36..40
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 69..73
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 81..85
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 86..89
FT /evidence="ECO:0007829|PDB:3M1C"
FT STRAND 90..94
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 96..108
FT /evidence="ECO:0007829|PDB:3M1C"
FT HELIX 117..134
FT /evidence="ECO:0007829|PDB:3M1C"
FT TURN 135..138
FT /evidence="ECO:0007829|PDB:3M1C"
SQ SEQUENCE 224 AA; 25193 MW; CD585849250D7C1F CRC64;
MGFVCLFGLV VMGAWGAWGG SQATEYVLRS VIAKEVGDIL RVPCMRTPAD DVSWRYEAPS
VIDYARIDGI FLRYHCPGLD TFLWDRHAQR AYLVNPFLFA AGFLEDLSHS VFPADTQETT
TRRALYKEIR DALGSRKQAV SHAPVRAGCV NFDYSRTRRC VGRRDLRPAN TTSTWEPPVS
SDDEASSQSK PLATQPPVLA LSNAPPRRVS PTRGRRRHTR LRRN
