UL18_HCMVA
ID UL18_HCMVA Reviewed; 368 AA.
AC P08560; Q7M6R5;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 02-JUN-2021, entry version 118.
DE RecName: Full=Glycoprotein UL18;
DE Flags: Precursor;
GN Name=H301; Synonyms=UL18;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2827039; DOI=10.1038/331269a0;
RA Beck S., Barrell B.G.;
RT "Human cytomegalovirus encodes a glycoprotein homologous to MHC class-I
RT antigens.";
RL Nature 331:269-272(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [3]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [4]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [5]
RP INTERACTION WITH HOST LILRB1.
RX PubMed=10591185; DOI=10.1016/s1074-7613(00)80135-1;
RA Chapman T.L., Heikeman A.P., Bjorkman P.J.;
RT "The inhibitory receptor LIR-1 uses a common binding interaction to
RT recognize class I MHC molecules and the viral homolog UL18.";
RL Immunity 11:603-613(1999).
RN [6]
RP FUNCTION.
RX PubMed=18688275; DOI=10.1371/journal.ppat.1000123;
RA Kim Y., Park B., Cho S., Shin J., Cho K., Jun Y., Ahn K.;
RT "Human cytomegalovirus UL18 utilizes US6 for evading the NK and T-cell
RT responses.";
RL PLoS Pathog. 4:E1000123-E1000123(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 21-301.
RX PubMed=18632577; DOI=10.1073/pnas.0804551105;
RA Yang Z., Bjorkman P.J.;
RT "Structure of UL18, a peptide-binding viral MHC mimic, bound to a host
RT inhibitory receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10095-10100(2008).
CC -!- FUNCTION: Plays a role in the protection against host NK cell
CC cytotoxicity by interacting with and modulating the activity of the
CC host inhibitory leukocyte Ig-like receptor 1/LILRB1, which is expressed
CC on monocytes, dendritic cells, as well as subsets of T and NK cells.
CC UL18 exerts an inhibitory effect on LIR-1+ NK cells, while it
CC stimulates LIR-1- NK cell. These modulations prevent lysis of the
CC infected cells by NK cells. {ECO:0000269|PubMed:18688275}.
CC -!- SUBUNIT: Interacts with host LILRB1. {ECO:0000269|PubMed:10591185}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; Y00293; CAA68399.1; -; Genomic_DNA.
DR EMBL; X17403; CAA35417.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00121.1; -; Genomic_DNA.
DR PIR; S09781; HLBECM.
DR PDB; 3D2U; X-ray; 2.21 A; A/E=21-301.
DR PDBsum; 3D2U; -.
DR SMR; P08560; -.
DR DIP; DIP-46164N; -.
DR EvolutionaryTrace; P08560; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0033644; C:host cell membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0042612; C:MHC class I protein complex; IEA:UniProtKB-KW.
DR GO; GO:0002474; P:antigen processing and presentation of peptide antigen via MHC class I; IEA:UniProtKB-KW.
DR GO; GO:0039671; P:evasion by virus of host natural killer cell activity; IEA:UniProtKB-KW.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
DR GO; GO:0031623; P:receptor internalization; TAS:UniProtKB.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.500.10; -; 1.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003597; Ig_C1-set.
DR InterPro; IPR011161; MHC_I-like_Ag-recog.
DR InterPro; IPR037055; MHC_I-like_Ag-recog_sf.
DR InterPro; IPR011162; MHC_I/II-like_Ag-recog.
DR Pfam; PF07654; C1-set; 1.
DR Pfam; PF00129; MHC_I; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF54452; SSF54452; 1.
DR PROSITE; PS00290; IG_MHC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Host membrane; Host-virus interaction;
KW Immunity; Membrane; MHC I; Modulation of host NK-cell activity by virus;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix;
KW Viral immunoevasion.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..368
FT /note="Glycoprotein UL18"
FT /id="PRO_0000037452"
FT TRANSMEM 321..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 19..114
FT /note="Alpha-1-like"
FT REGION 115..208
FT /note="Alpha-2-like"
FT REGION 209..303
FT /note="Alpha-3-like"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 66
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 74
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 95
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 127
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 150
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 167
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 177
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 240
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 282
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 291
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT STRAND 22..35
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 48..58
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 71..78
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 82..108
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 130..139
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:3D2U"
FT TURN 159..161
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 163..167
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 168..176
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 181..191
FT /evidence="ECO:0007829|PDB:3D2U"
FT HELIX 193..204
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 212..221
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 224..237
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 240..248
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 269..278
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 281..288
FT /evidence="ECO:0007829|PDB:3D2U"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:3D2U"
SQ SEQUENCE 368 AA; 41735 MW; 48AE7EFB4DDCCB4E CRC64;
MMTMWCLTLF VLWMLRVVGM HVLRYGYTGI FDDTSHMTLT VVGIFDGQHF FTYHVNSSDK
ASSRANGTIS WMANVSAAYP TYLDGERAKG DLIFNQTEQN LLELEIALGY RSQSVLTWTH
ECNTTENGSF VAGYEGFGWD GETLMELKDN LTLWTGPNYE ISWLKQNKTY IDGKIKNISE
GDTTIQRNYL KGNCTQWSVI YSGFQPPVTH PVVKGGVRNQ NDNRAEAFCT SYGFFPGEIN
ITFIHYGDKV PEDSEPQCNP LLPTLDGTFH QGCYVAIFCN QNYTCRVTHG NWTVEIPISV
TSPDDSSSGE VPDHPTANKR YNTMTISSVL LALLLCALLF AFLHYFTTLK QYLRNLAFAW
RYRKVRSS
