GJ_HHV2H
ID GJ_HHV2H Reviewed; 92 AA.
AC P13293;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 1.
DT 23-FEB-2022, entry version 65.
DE RecName: Full=Envelope glycoprotein J;
DE Flags: Precursor;
GN Name=gJ; ORFNames=US5;
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=3027242; DOI=10.1099/0022-1317-68-1-19;
RA McGeoch D.J., Moss H.W.M., McNab D., Frame M.C.;
RT "DNA sequence and genetic content of the HindIII l region in the short
RT unique component of the herpes simplex virus type 2 genome: identification
RT of the gene encoding glycoprotein G, and evolutionary comparisons.";
RL J. Gen. Virol. 68:19-38(1987).
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).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30248525; DOI=10.1016/j.virol.2018.09.004;
RA Liu Y., Guan X., Li C., Ni F., Luo S., Wang J., Zhang D., Zhang M., Hu Q.;
RT "HSV-2 glycoprotein J promotes viral protein expression and virus spread.";
RL Virology 525:83-95(2018).
CC -!- FUNCTION: Functions as an activator of viral protein expression and
CC virus production. In turn, promotes cell-to-cell spread as well as
CC syncytia formation. {ECO:0000269|PubMed:30248525}.
CC -!- SUBCELLULAR LOCATION: Host Golgi apparatus membrane {ECO:0000305};
CC Single-pass type I membrane protein {ECO:0000305}. Host endoplasmic
CC reticulum membrane {ECO:0000305}; Single-pass type I membrane protein
CC {ECO:0000305}. Host endosome membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}. Note=Localizes to the endoplasmic
CC reticulum, trans-Golgi network, and early endosomes. {ECO:0000250}.
CC -!- DISRUPTION PHENOTYPE: Knockout mutant significantly impairs plaque and
CC syncytia formation and decreases virus production.
CC {ECO:0000269|PubMed:30248525}.
CC -!- SIMILARITY: Belongs to the alphaherpesvirinae glycoprotein J family.
CC {ECO:0000305}.
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DR EMBL; X04798; CAA28491.1; -; Genomic_DNA.
DR EMBL; Z86099; CAB06712.1; -; Genomic_DNA.
DR PIR; D43674; D43674.
DR RefSeq; YP_009137217.1; NC_001798.2.
DR SMR; P13293; -.
DR PRIDE; P13293; -.
DR DNASU; 1487357; -.
DR GeneID; 1487357; -.
DR KEGG; vg:1487357; -.
DR Proteomes; UP000001874; Genome.
DR GO; GO:0044167; C:host cell endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044175; C:host cell endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
PE 3: Inferred from homology;
KW Glycoprotein; Host endoplasmic reticulum; Host endosome;
KW Host Golgi apparatus; Host membrane; Membrane; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..92
FT /note="Envelope glycoprotein J"
FT /id="PRO_0000115790"
FT TOPO_DOM 23..49
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 71..92
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 33
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
SQ SEQUENCE 92 AA; 9510 MW; 3314C6D50DF0EB83 CRC64;
MDRYAVRTWG IVGILGCAAV GAAPTGPASD TTNATARLPT HPPLIRSGGF AVPLIVGGLC
LMILGMACLL EVLRRLGREL ARCCPHAGQF AP