UL33_HCMVA
ID UL33_HCMVA Reviewed; 412 AA.
AC P16849; Q7M6Q0;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=G-protein coupled receptor homolog UL33;
DE Short=vGPCR UL33;
GN Name=UL33;
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=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 SIMILARITY TO G-PROTEIN COUPLED RECEPTORS.
RX PubMed=2158627; DOI=10.1038/344774a0;
RA Chee M.S., Satchwell S.C., Preddie E., Weston K.M., Barrell B.G.;
RT "Human cytomegalovirus encodes three G protein-coupled receptor
RT homologues.";
RL Nature 344:774-777(1990).
RN [3]
RP GENOME REANNOTATION, AND SEQUENCE REVISION.
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 SUBCELLULAR LOCATION.
RX PubMed=11886592; DOI=10.1034/j.1600-0854.2002.030307.x;
RA Fraile-Ramos A., Pelchen-Matthews A., Kledal T.N., Browne H.,
RA Schwartz T.W., Marsh M.;
RT "Localization of HCMV UL33 and US27 in endocytic compartments and viral
RT membranes.";
RL Traffic 3:218-232(2002).
RN [6]
RP FUNCTION.
RX PubMed=14522997; DOI=10.1074/jbc.m306530200;
RA Casarosa P., Gruijthuijsen Y.K., Michel D., Beisser P.S., Holl J.,
RA Fitzsimons C.P., Verzijl D., Bruggeman C.A., Mertens T., Leurs R., Vink C.,
RA Smit M.J.;
RT "Constitutive signaling of the human cytomegalovirus-encoded receptor UL33
RT differs from that of its rat cytomegalovirus homolog R33 by promiscuous
RT activation of G proteins of the Gq, Gi, and Gs classes.";
RL J. Biol. Chem. 278:50010-50023(2003).
RN [7]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [8]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [9]
RP REVIEW.
RX PubMed=15172446; DOI=10.1016/j.humimm.2004.02.002;
RA Michelson S.;
RT "Consequences of human cytomegalovirus mimicry.";
RL Hum. Immunol. 65:465-475(2004).
RN [10]
RP INTERACTION WITH US28.
RX PubMed=21684267; DOI=10.1016/j.bcp.2011.06.009;
RA Tschische P., Tadagaki K., Kamal M., Jockers R., Waldhoer M.;
RT "Heteromerization of human cytomegalovirus encoded chemokine receptors.";
RL Biochem. Pharmacol. 82:610-619(2011).
CC -!- FUNCTION: G-protein-coupled receptor (vGPCR) that constitutively
CC activates multiple oncogenic signaling pathways including STAT3, AP-1,
CC phospholipase C, NF-kappa-B or cAMP-responsive element (CRE) pathways
CC (PubMed:14522997). Plays an important role in viral reactivation from
CC latency through activation of host CREB1, facilitating its recruitment
CC to the viral major immediate early (MIE) genes. In turn, expression of
CC the MIE-driven genes such as UL123 are de-repressed. Facilitates also
CC virus dissemination via the extracellular and cell-to-cell route (By
CC similarity). {ECO:0000250|UniProtKB:Q6SW98,
CC ECO:0000269|PubMed:14522997}.
CC -!- SUBUNIT: Heterodimerizes with US28. {ECO:0000269|PubMed:21684267}.
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:11886592}. Host cell
CC membrane {ECO:0000269|PubMed:11886592}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:11886592}. Host cytoplasm
CC {ECO:0000250|UniProtKB:Q6SW98}. Note=Present in the virion assembly
CC compartment (VAC) of HCMV-infected cells.
CC {ECO:0000250|UniProtKB:Q6SW98}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA35432.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA37385.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; X17403; CAA35432.1; ALT_FRAME; Genomic_DNA.
DR EMBL; X53293; CAA37385.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BK000394; DAA00138.1; -; Genomic_DNA.
DR PIR; S09796; QQBET9.
DR SMR; P16849; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW.
DR GO; GO:0039553; P:suppression by virus of host chemokine activity; IEA:UniProtKB-KW.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 1: Evidence at protein level;
KW Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Host cell membrane; Host cytoplasm; Host membrane; Host-virus interaction;
KW Inhibition of host chemokines by virus; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix;
KW Viral immunoevasion; Virion.
FT CHAIN 1..412
FT /note="G-protein coupled receptor homolog UL33"
FT /id="PRO_0000070240"
FT TOPO_DOM 1..29
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..54
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 55..70
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..102
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 103..129
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 130..138
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..160
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..203
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 225..240
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT TRANSMEM 241..267
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..281
FT /note="Virion surface"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..305
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..412
FT /note="Intravirion"
FT /evidence="ECO:0000255"
FT REGION 377..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 7
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 18
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT CARBOHYD 22
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 180
FT /note="N-linked (GlcNAc...) asparagine; by host"
FT /evidence="ECO:0000255"
FT DISULFID 104..188
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 412 AA; 46295 MW; 19C1B2344717DECD CRC64;
MDTIIHNSTR NNTPPHINDT CNMTGPLFAI RTTEAVLNTF IIFVGGPLNA IVLITQLLTN
RVLGYSTPTI YMTNLYSTNF LTLTVLPFIV LSNQWLLPAG VASCKFLSVI YYSSCTVGFA
TVALIAADRY RVLHKRTYAR QSYRSTYMIL LLTWLAGLIF SVPAAVYTTV VMHHDANDTN
NTNGHATCVL YFVAEEVHTV LLSWKVLLTM VWGAAPVIMM TWFYAFFYST VQRTSQKQRS
RTLTFVSVLL ISFVALQTPY VSLMIFNSYA TTAWPMQCEH LTLRRTIGTL ARVVPHLHCL
INPILYALLG HDFLQRMRQC FRGQLLDRRA FLRSQQNQRA TAETNLAAGN NSQSVATSLD
TNSKNYNQHA KRSVSFNFPS GTWKGGQKTA SNDTSTKIPH RLSQSHHNLS GV
