UL16P_HCMVA
ID UL16P_HCMVA Reviewed; 230 AA.
AC P16757; Q7M6R7;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 02-JUN-2021, entry version 68.
DE RecName: Full=Protein UL16;
DE Flags: Precursor;
GN Name=UL16;
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 [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 [2]
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 [3]
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 [4]
RP INTERACTION WITH HOST ULBP1; ULBP2 AND MICB.
RX PubMed=11239445; DOI=10.1016/s1074-7613(01)00095-4;
RA Cosman D., Mullberg J., Sutherland C.L., Chin W., Armitage R., Fanslow W.,
RA Kubin M., Chalupny N.J.;
RT "ULBPs, novel MHC class I-related molecules, bind to CMV glycoprotein UL16
RT and stimulate NK cytotoxicity through the NKG2D receptor.";
RL Immunity 14:123-133(2001).
RN [5]
RP FUNCTION.
RX PubMed=12847260; DOI=10.4049/jimmunol.171.2.902;
RA Rolle A., Mousavi-Jazi M., Eriksson M., Odeberg J., Soderberg-Naucler C.,
RA Cosman D., Karre K., Cerboni C.;
RT "Effects of human cytomegalovirus infection on ligands for the activating
RT NKG2D receptor of NK cells: up-regulation of UL16-binding protein (ULBP)1
RT and ULBP2 is counteracted by the viral UL16 protein.";
RL J. Immunol. 171:902-908(2003).
RN [6]
RP FUNCTION.
RX PubMed=12782710; DOI=10.1084/jem.20022059;
RA Dunn C., Chalupny N.J., Sutherland C.L., Dosch S., Sivakumar P.V.,
RA Johnson D.C., Cosman D.;
RT "Human cytomegalovirus glycoprotein UL16 causes intracellular sequestration
RT of NKG2D ligands, protecting against natural killer cell cytotoxicity.";
RL J. Exp. Med. 197:1427-1439(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 27-184.
RX PubMed=20090832; DOI=10.1371/journal.ppat.1000723;
RA Muller S., Zocher G., Steinle A., Stehle T.;
RT "Structure of the HCMV UL16-MICB complex elucidates select binding of a
RT viral immunoevasin to diverse NKG2D ligands.";
RL PLoS Pathog. 6:E1000723-E1000723(2010).
CC -!- FUNCTION: Plays a role in escape from host immune response. Blocks the
CC interaction between the host KLRK1 receptor with the ligands ULBP1 and
CC ULBP2. ULBPs activate multiple signaling pathways in primary NK cells,
CC resulting in the production of cytokines and chemokines. The
CC sequestration of diverse KLRK1 ligands in the endoplasmic reticulum and
CC cis-Golgi apparatus of cells by UL16 inhibits the activation of NK
CC cells. {ECO:0000269|PubMed:12782710, ECO:0000269|PubMed:12847260}.
CC -!- SUBUNIT: Interacts with host ULBP1, ULBP2 and MICB.
CC {ECO:0000269|PubMed:11239445}.
CC -!- SUBCELLULAR LOCATION: Host membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the HHV-5 UL16 protein family. {ECO:0000305}.
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; X17403; CAA35448.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00119.1; -; Genomic_DNA.
DR PIR; S09778; S09778.
DR PDB; 2WY3; X-ray; 1.80 A; B/D=27-184.
DR PDBsum; 2WY3; -.
DR SMR; P16757; -.
DR IntAct; P16757; 3.
DR EvolutionaryTrace; P16757; -.
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:0039671; P:evasion by virus of host natural killer cell activity; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1990; -; 1.
DR InterPro; IPR038671; HCMV_UL16_sf.
DR InterPro; IPR035123; UL16.
DR Pfam; PF17622; UL16; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Glycoprotein; Host membrane; Host-virus interaction;
KW Membrane; Modulation of host NK-cell activity by virus; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix; Viral immunoevasion.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..230
FT /note="Protein UL16"
FT /id="PRO_0000037451"
FT TOPO_DOM 27..184
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 185..205
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 206..230
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 35
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 41
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 84
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 101
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2WY3"
FT TURN 32..35
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:2WY3"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 60..68
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 88..94
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 108..115
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 117..128
FT /evidence="ECO:0007829|PDB:2WY3"
FT TURN 132..134
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 136..144
FT /evidence="ECO:0007829|PDB:2WY3"
FT STRAND 147..157
FT /evidence="ECO:0007829|PDB:2WY3"
SQ SEQUENCE 230 AA; 26147 MW; B72F2C241C569967 CRC64;
MERRRGTVPL GWVFFVLCLS ASSSCAVDLG SKSSNSTCRL NVTELASIHP GETWTLHGMC
ISICYYENVT EDEIIGVAFT WQHNESVVDL WLYQNDTVIR NFSDITTNIL QDGLKMRTVP
VTKLYTSRMV TNLTVGRYDC LRCENGTTKI IERLYVRLGS LYPRPPGSGL AKHPSVSADE
ELSATLARDI VLVSAITLFF FLLALRIPQR LCQRLRIRLP HRYQRLRTED
