ID   UL20_HHV11              Reviewed;         222 AA.
AC   P10204;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   24-JAN-2024, entry version 84.
DE   RecName: Full=Protein UL20;
GN   Name=UL20;
OS   Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC   Herpesvirales; Orthoherpesviridae; Alphaherpesvirinae; Simplexvirus;
OC   Simplexvirus humanalpha1; Human herpesvirus 1.
OX   NCBI_TaxID=10299;
OH   NCBI_TaxID=9606; Homo sapiens (Human).
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2839594; DOI=10.1099/0022-1317-69-7-1531;
RA   McGeoch D.J., Dalrymple M.A., Davison A.J., Dolan A., Frame M.C., McNab D.,
RA   Perry L.J., Scott J.E., Taylor P.;
RT   "The complete DNA sequence of the long unique region in the genome of
RT   herpes simplex virus type 1.";
RL   J. Gen. Virol. 69:1531-1574(1988).
RN   [2]
RP   FUNCTION.
RC   STRAIN=F;
RX   PubMed=1719228; DOI=10.1128/jvi.65.12.6414-6424.1991;
RA   Baines J.D., Ward P.L., Campadelli-Fiume G., Roizman B.;
RT   "The UL20 gene of herpes simplex virus 1 encodes a function necessary for
RT   viral egress.";
RL   J. Virol. 65:6414-6424(1991).
RN   [3]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=F;
RX   PubMed=7933124; DOI=10.1128/jvi.68.11.7406-7417.1994;
RA   Ward P.L., Campadelli-Fiume G., Avitabile E., Roizman B.;
RT   "Localization and putative function of the UL20 membrane protein in cells
RT   infected with herpes simplex virus 1.";
RL   J. Virol. 68:7406-7417(1994).
RN   [4]
RP   SUBCELLULAR LOCATION.
RC   STRAIN=F;
RX   PubMed=15254173; DOI=10.1128/jvi.78.15.8015-8025.2004;
RA   Avitabile E., Lombardi G., Gianni T., Capri M., Campadelli-Fiume G.;
RT   "Coexpression of UL20p and gK inhibits cell-cell fusion mediated by herpes
RT   simplex virus glycoproteins gD, gH-gL, and wild-type gB or an endocytosis-
RT   defective gB mutant and downmodulates their cell surface expression.";
RL   J. Virol. 78:8015-8025(2004).
RN   [5]
RP   FUNCTION.
RC   STRAIN=KOS;
RX   PubMed=17996071; DOI=10.1186/1743-422x-4-120;
RA   Melancon J.M., Fulmer P.A., Kousoulas K.G.;
RT   "The herpes simplex virus UL20 protein functions in glycoprotein K (gK)
RT   intracellular transport and virus-induced cell fusion are independent of
RT   UL20 functions in cytoplasmic virion envelopment.";
RL   Virol. J. 4:120-120(2007).
RN   [6]
RP   INTERACTION WITH GK.
RC   STRAIN=KOS;
RX   PubMed=18434401; DOI=10.1128/jvi.00147-08;
RA   Foster T.P., Chouljenko V.N., Kousoulas K.G.;
RT   "Functional and physical interactions of the herpes simplex virus type 1
RT   UL20 membrane protein with glycoprotein K.";
RL   J. Virol. 82:6310-6323(2008).
RN   [7]
RP   VIRION.
RC   STRAIN=F;
RX   PubMed=18596102; DOI=10.1128/jvi.00904-08;
RA   Loret S., Guay G., Lippe R.;
RT   "Comprehensive characterization of extracellular herpes simplex virus type
RT   1 virions.";
RL   J. Virol. 82:8605-8618(2008).
RN   [8]
RP   INTERACTION WITH GB.
RX   PubMed=20573833; DOI=10.1128/jvi.00298-10;
RA   Chouljenko V.N., Iyer A.V., Chowdhury S., Kim J., Kousoulas K.G.;
RT   "The herpes simplex virus type 1 UL20 protein and the amino terminus of
RT   glycoprotein K (gK) physically interact with gB.";
RL   J. Virol. 84:8596-8606(2010).
CC   -!- FUNCTION: Plays an essential role in egress of virus particles from the
CC       nucleus, cytoplasmic envelopment and virus-induced cell fusion. Forms a
CC       functional protein complex with gK and this interaction is absolutely
CC       essential for their coordinate intracellular transport, gK
CC       glycosylation, expression on host cell surface, and function. Together,
CC       they modulate gB-mediated virus-induced cell fusion and virion egress
CC       and therefore actively participate in these processes.
CC       {ECO:0000269|PubMed:1719228, ECO:0000269|PubMed:17996071}.
CC   -!- SUBUNIT: Interacts with gK (via N-terminus); this interaction plays a
CC       role in the coordinate transport of UL20 and gK to the trans-Golgi
CC       network (TGN), and is required for their cell surface expression.
CC       Interacts with gB. {ECO:0000269|PubMed:18434401,
CC       ECO:0000269|PubMed:20573833}.
CC   -!- INTERACTION:
CC       P10204; P68331: gK; NbExp=5; IntAct=EBI-7906325, EBI-7906305;
CC   -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:18596102,
CC       ECO:0000269|PubMed:7933124}. Host Golgi apparatus membrane
CC       {ECO:0000269|PubMed:15254173}; Multi-pass membrane protein
CC       {ECO:0000255}. Host nucleus membrane {ECO:0000269|PubMed:15254173};
CC       Multi-pass membrane protein {ECO:0000255}. Note=During virion
CC       morphogenesis, this protein probably accumulates in the trans-Golgi
CC       where secondary envelopment occurs. It is probably transported with gK
CC       to the cell surface from where it is endocytosed and directed to the
CC       trans-Golgi network (TGN). {ECO:0000269|PubMed:15254173}.
CC   -!- SIMILARITY: Belongs to the alphaherpesvirinae UL20 family.
CC       {ECO:0000305}.
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DR   EMBL; X14112; CAA32333.1; -; Genomic_DNA.
DR   PIR; B30084; WMBEWN.
DR   RefSeq; YP_009137094.1; NC_001806.2.
DR   IntAct; P10204; 2.
DR   MINT; P10204; -.
DR   DNASU; 2703371; -.
DR   GeneID; 2703371; -.
DR   KEGG; vg:2703371; -.
DR   Proteomes; UP000009294; Genome.
DR   GO; GO:0044178; C:host cell Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0044200; C:host cell nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0044423; C:virion component; IEA:UniProtKB-KW.
DR   GO; GO:0019058; P:viral life cycle; IEA:InterPro.
DR   InterPro; IPR007629; Herpes_UL20.
DR   Pfam; PF04544; Herpes_UL20; 1.
PE   1: Evidence at protein level;
KW   Host Golgi apparatus; Host membrane; Host nucleus; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Virion.
FT   CHAIN           1..222
FT                   /note="Protein UL20"
FT                   /id="PRO_0000115966"
FT   TRANSMEM        64..84
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        98..118
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        180..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   222 AA;  24231 MW;  D10C373183E96218 CRC64;
     MTMRDDLPLV DRDLVDEAAF GGEEGELPLE EQFSLSSYGT SDFFVSSAYS RLPPHTQPVF
     SKRVILFLWS FLVLKPLEMV AAGMYYGLTG RVVAPACILA AIVGYYVTWA VRALLLYVNI
     KRDRLPLSAP VFWGMSVFLG GTALCALFAA AHETFSPDGL FHFIATNQML PPTDPLRTRA
     LGIACAAGAS MWVAAADSFA ASANFFLARF WTRAILNAPV AF
//