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G-protein coupled receptor homolog US28 (HHRF3)

 US28_HCMVA              Reviewed;         354 AA.
P69332; P09704; P32952; Q7M6H3;
15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
15-FEB-2005, sequence version 1.
25-APR-2018, entry version 75.
RecName: Full=G-protein coupled receptor homolog US28;
AltName: Full=HHRF3;
Name=US28;
Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
Viruses; dsDNA viruses, no RNA stage; Herpesvirales; Herpesviridae;
Betaherpesvirinae; Cytomegalovirus.
NCBI_TaxID=10360;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3031311; DOI=10.1016/0022-2836(86)90359-1;
Weston K.M., Barrell B.G.;
"Sequence of the short unique region, short repeats, and part of the
long repeats of human cytomegalovirus.";
J. Mol. Biol. 192:177-208(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=2161319;
Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
"Analysis of the protein-coding content of the sequence of human
cytomegalovirus strain AD169.";
Curr. Top. Microbiol. Immunol. 154:125-169(1990).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND LIGAND-BINDING.
STRAIN=Isolate clinical VHL/E;
PubMed=7540006; DOI=10.1006/bbrc.1995.1814;
Kuhn D.E., Beall C.J., Kolattukudy P.E.;
"The cytomegalovirus US28 protein binds multiple CC chemokines with
high affinity.";
Biochem. Biophys. Res. Commun. 211:325-330(1995).
[4]
SIMILARITY TO G-PROTEIN COUPLED RECEPTORS.
PubMed=2158627; DOI=10.1038/344774a0;
Chee M.S., Satchwell S.C., Preddie E., Weston K.M., Barrell B.G.;
"Human cytomegalovirus encodes three G protein-coupled receptor
homologues.";
Nature 344:774-777(1990).
[5]
IDENTIFICATION OF C-TERMINAL FRAMESHIFT, AND FUNCTION.
PubMed=7961796;
Gao J.-L., Murphy P.M.;
"Human cytomegalovirus open reading frame US28 encodes a functional
beta chemokine receptor.";
J. Biol. Chem. 269:28539-28542(1994).
[6]
GENOME REANNOTATION.
PubMed=12533697; DOI=10.1099/vir.0.18606-0;
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
"The human cytomegalovirus genome revisited: comparison with the
chimpanzee cytomegalovirus genome.";
J. Gen. Virol. 84:17-28(2003).
[7]
ERRATUM.
Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J.,
Alcendor D.J., McGeoch D.J., Hayward G.S.;
J. Gen. Virol. 84:1053-1053(2003).
[8]
FUNCTION.
PubMed=11050102; DOI=10.1074/jbc.M008965200;
Casarosa P., Bakker R.A., Verzijl D., Navis M., Timmerman H.,
Leurs R., Smit M.J.;
"Constitutive signaling of the human cytomegalovirus-encoded chemokine
receptor US28.";
J. Biol. Chem. 276:1133-1137(2001).
[9]
PHOSPHORYLATION.
PubMed=12244063; DOI=10.1074/jbc.M208214200;
Mokros T., Rehm A., Droese J., Oppermann M., Lipp M., Hopken U.E.;
"Surface expression and endocytosis of the human cytomegalovirus-
encoded chemokine receptor US28 is regulated by agonist-independent
phosphorylation.";
J. Biol. Chem. 277:45122-45128(2002).
[10]
INTERACTION WITH HOST GPRASP1.
PubMed=20102549; DOI=10.1111/j.1600-0854.2010.1045.x;
Tschische P., Moser E., Thompson D., Vischer H.F., Parzmair G.P.,
Pommer V., Platzer W., Schwarzbraun T., Schaider H., Smit M.J.,
Martini L., Whistler J.L., Waldhoer M.;
"The G-protein coupled receptor associated sorting protein GASP-1
regulates the signalling and trafficking of the viral chemokine
receptor US28.";
Traffic 11:660-674(2010).
-!- FUNCTION: Receptor for a C-C type chemokine. Binds to a number of
different CC-chemokines including CCL5/RANTES, CCL2/MCP-1,
CCL3/MIP-1-alpha as well as CX3CL1/Fractalkine. Transduces signals
resulting in the activation of MAP kinase signaling pathways and
augmentation of intracellular calcium ion levels, leading to
alterations in chemotactic behavior of vascular smooth muscle
cells and macrophages. The US28 receptor also exhibits high levels
of agonist-independent signaling activity and agonist-independent
endocytosis. Interacts with endogenous Gaq/11 subunits and thereby
constitutively activates phospholipase C.
{ECO:0000269|PubMed:11050102, ECO:0000269|PubMed:7961796}.
-!- SUBUNIT: Interacts with host GPRASP1; this interaction targets
US28 to lysosomes for degradation. {ECO:0000269|PubMed:20102549}.
-!- INTERACTION:
P78423:CX3CL1 (xeno); NbExp=4; IntAct=EBI-16147206, EBI-15188013;
-!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane
protein.
-!- PTM: Phosphorylated. High phosphorylation occurs concomitantly
with receptor endocytosis and correlate with low receptor presence
at the plasma membrane. {ECO:0000269|PubMed:12244063}.
-!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
{ECO:0000255|PROSITE-ProRule:PRU00521}.
-!- SEQUENCE CAUTION:
Sequence=CAA28338.1; Type=Frameshift; Positions=299; Evidence={ECO:0000305};
Sequence=CAA35260.1; Type=Frameshift; Positions=299; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; X04650; CAA28338.1; ALT_FRAME; Genomic_DNA.
EMBL; X17403; CAA35260.1; ALT_FRAME; Genomic_DNA.
EMBL; L20501; AAA98741.1; -; Genomic_DNA.
PIR; C27216; QQBED3.
PDB; 4XT1; X-ray; 2.89 A; A=1-354.
PDB; 4XT3; X-ray; 3.80 A; A=1-354.
PDBsum; 4XT1; -.
PDBsum; 4XT3; -.
ProteinModelPortal; P69332; -.
SMR; P69332; -.
DIP; DIP-61489N; -.
IntAct; P69332; 1.
BindingDB; P69332; -.
ChEMBL; CHEMBL4259; -.
iPTMnet; P69332; -.
PRIDE; P69332; -.
OrthoDB; VOG090000NY; -.
Proteomes; UP000008991; Genome.
GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0004950; F:chemokine receptor activity; IEA:InterPro.
GO; GO:0006935; P:chemotaxis; IEA:InterPro.
GO; GO:0030683; P:evasion or tolerance by virus of host immune response; IEA:UniProtKB-KW.
GO; GO:0044864; P:positive regulation by virus of host cell division; IDA:CACAO.
GO; GO:0039553; P:suppression by virus of host chemokine activity; IEA:UniProtKB-KW.
InterPro; IPR000355; Chemokine_rcpt.
InterPro; IPR000276; GPCR_Rhodpsn.
InterPro; IPR017452; GPCR_Rhodpsn_7TM.
Pfam; PF00001; 7tm_1; 1.
PRINTS; PR00657; CCCHEMOKINER.
PRINTS; PR00237; GPCRRHODOPSN.
PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; G-protein coupled receptor;
Glycoprotein; Host cell membrane; Host membrane;
Host-virus interaction; Inhibition of host chemokines by virus;
Membrane; Receptor; Reference proteome; Transducer; Transmembrane;
Transmembrane helix; Viral immunoevasion.
CHAIN 1 354 G-protein coupled receptor homolog US28.
/FTId=PRO_0000070246.
TOPO_DOM 1 37 Extracellular. {ECO:0000255}.
TRANSMEM 38 58 Helical; Name=1. {ECO:0000255}.
TOPO_DOM 59 69 Cytoplasmic. {ECO:0000255}.
TRANSMEM 70 90 Helical; Name=2. {ECO:0000255}.
TOPO_DOM 91 101 Extracellular. {ECO:0000255}.
TRANSMEM 102 122 Helical; Name=3. {ECO:0000255}.
TOPO_DOM 123 145 Cytoplasmic. {ECO:0000255}.
TRANSMEM 146 166 Helical; Name=4. {ECO:0000255}.
TOPO_DOM 167 183 Extracellular. {ECO:0000255}.
TRANSMEM 184 204 Helical; Name=5. {ECO:0000255}.
TOPO_DOM 205 228 Cytoplasmic. {ECO:0000255}.
TRANSMEM 229 249 Helical; Name=6. {ECO:0000255}.
TOPO_DOM 250 273 Extracellular. {ECO:0000255}.
TRANSMEM 274 294 Helical; Name=7. {ECO:0000255}.
TOPO_DOM 295 354 Cytoplasmic. {ECO:0000255}.
COMPBIAS 2 7 Poly-Thr.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine; by host.
{ECO:0000255}.
VARIANT 18 19 ED -> DE (in strain: Isolate clinical
VHL/E).
VARIANT 25 25 F -> L (in strain: Isolate clinical VHL/
E).
VARIANT 267 267 R -> K (in strain: Isolate clinical VHL/
E).
VARIANT 346 346 V -> A (in strain: Isolate clinical VHL/
E).
HELIX 26 59 {ECO:0000244|PDB:4XT1}.
HELIX 67 83 {ECO:0000244|PDB:4XT1}.
HELIX 86 94 {ECO:0000244|PDB:4XT1}.
HELIX 104 133 {ECO:0000244|PDB:4XT1}.
HELIX 141 157 {ECO:0000244|PDB:4XT1}.
HELIX 160 163 {ECO:0000244|PDB:4XT1}.
STRAND 166 169 {ECO:0000244|PDB:4XT1}.
STRAND 172 175 {ECO:0000244|PDB:4XT1}.
STRAND 177 180 {ECO:0000244|PDB:4XT1}.
HELIX 184 196 {ECO:0000244|PDB:4XT1}.
HELIX 198 215 {ECO:0000244|PDB:4XT1}.
HELIX 223 255 {ECO:0000244|PDB:4XT1}.
HELIX 263 280 {ECO:0000244|PDB:4XT1}.
HELIX 283 290 {ECO:0000244|PDB:4XT1}.
TURN 291 294 {ECO:0000244|PDB:4XT1}.
HELIX 296 308 {ECO:0000244|PDB:4XT1}.
SEQUENCE 354 AA; 41064 MW; 295A2F7C54DF7AAD CRC64;
MTPTTTTAEL TTEFDYDEDA TPCVFTDVLN QSKPVTLFLY GVVFLFGSIG NFLVIFTITW
RRRIQCSGDV YFINLAAADL LFVCTLPLWM QYLLDHNSLA SVPCTLLTAC FYVAMFASLC
FITEIALDRY YAIVYMRYRP VKQACLFSIF WWIFAVIIAI PHFMVVTKKD NQCMTDYDYL
EVSYPIILNV ELMLGAFVIP LSVISYCYYR ISRIVAVSQS RHKGRIVRVL IAVVLVFIIF
WLPYHLTLFV DTLKLLKWIS SSCEFERSLK RALILTESLA FCHCCLNPLL YVFVGTKFRQ
ELHCLLAEFR QRLFSRDVSW YHSMSFSRRS SPSRRETSSD TLSDEVCRVS QIIP


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