ID US27_HCMVA Reviewed; 362 AA. AC P09703; Q7M6H4; DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1989, sequence version 1. DT 22-FEB-2023, entry version 114. DE RecName: Full=G-protein coupled receptor homolog US27; DE AltName: Full=HHRF2; GN Name=US27; 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=3031311; DOI=10.1016/0022-2836(86)90359-1; RA Weston K.M., Barrell B.G.; RT "Sequence of the short unique region, short repeats, and part of the long RT repeats of human cytomegalovirus."; RL J. Mol. Biol. 192:177-208(1986). 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 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 [4] 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 [5] 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 [6] 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 [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 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). RN [10] RP STRUCTURE BY ELECTRON MICROSCOPY (3.10 ANGSTROMS) IN COMPLEX WITH HOST RP GNAI1; GNB1 AND GNG2, FUNCTION, AND INTERACTION WITH HOST GNAI1. RX PubMed=35061538; DOI=10.1126/sciadv.abl5442; RA Tsutsumi N., Maeda S., Qu Q., Voegele M., Jude K.M., Suomivuori C.M., RA Panova O., Waghray D., Kato H.E., Velasco A., Dror R.O., Skiniotis G., RA Kobilka B.K., Garcia K.C.; RT "Atypical structural snapshots of human cytomegalovirus GPCR interactions RT with host G proteins."; RL Sci. Adv. 8:eabl5442-eabl5442(2022). CC -!- FUNCTION: Interacts with the host Gi complex without activating it, CC thereby probably interfering with the chemokine-Gi signaling CC (PubMed:35061538). May also function as a G protein sink to sequester G CC protein from the cell surface via internalization (PubMed:35061538). CC Plays an important role in spread of HCMV via the extracellular route. CC {ECO:0000269|PubMed:35061538}. CC -!- SUBUNIT: Heterodimer with US28 (PubMed:21684267). Interacts with host CC Gi alpha-1 subunit GNAI1; this interaction does not lead to the CC catalytic activation of Gi complex (PubMed:35061538). CC {ECO:0000269|PubMed:21684267, ECO:0000269|PubMed:35061538}. 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}. CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; CAA35259.1; -; Genomic_DNA. DR EMBL; X04650; CAA28337.1; -; Genomic_DNA. DR EMBL; BK000394; DAA00214.1; -; Genomic_DNA. DR PIR; B27216; QQBED2. DR PDB; 7RKX; EM; 3.10 A; R=1-362. DR PDB; 7RKY; EM; 3.80 A; R=1-362. DR PDBsum; 7RKX; -. DR PDBsum; 7RKY; -. DR SMR; P09703; -. DR GlyCosmos; P09703; 4 sites, No reported glycans. DR Proteomes; UP000008991; Genome. DR Proteomes; UP000008992; Genome. DR GO; GO:0020002; C:host cell plasma 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:0004930; F:G protein-coupled receptor activity; IEA:UniProtKB-KW. DR GO; GO:0042785; P:evasion of host immune response via modulation of host cytokine network; IEA:UniProtKB-KW. DR GO; GO:0019049; P:mitigation of host antiviral defense response; IEA:UniProtKB-KW. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR PANTHER; PTHR10489:SF932; G_PROTEIN_RECEP_F1_2 DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. 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 3D-structure; G-protein coupled receptor; Glycoprotein; Host cell membrane; KW 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..362 FT /note="G-protein coupled receptor homolog US27" FT /id="PRO_0000070245" FT TOPO_DOM 1..34 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 35..58 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 59..67 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 68..90 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 91..104 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 105..126 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 127..148 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 149..167 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 168..193 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 194..213 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 214..233 FT /note="Intravirion" FT /evidence="ECO:0000255" FT TRANSMEM 234..257 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 258..274 FT /note="Virion surface" FT /evidence="ECO:0000255" FT TRANSMEM 275..298 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 299..362 FT /note="Intravirion" FT /evidence="ECO:0000255" FT REGION 341..362 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 15 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 TURN 22..24 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 28..32 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 37..56 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 59..63 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 65..93 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 99..132 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 149..161 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:7RKX" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:7RKX" FT TURN 170..173 FT /evidence="ECO:0007829|PDB:7RKX" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 187..199 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 202..222 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 229..244 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 246..260 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 267..289 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 292..297 FT /evidence="ECO:0007829|PDB:7RKX" FT HELIX 299..308 FT /evidence="ECO:0007829|PDB:7RKX" SQ SEQUENCE 362 AA; 41994 MW; D4C22064001EFECA CRC64; MTTSTNNQTL TQVSNMTNHT LNSTEIYQLF EYTRLGVWLM CIVGTFLNVL VITTILYYRR KKKSPSDTYI CNLAVADLLI VVGLPFFLEY AKHHPKLSRE VVCSGLNACF YICLFAGVCF LINLSMDRYC VIVWGVELNR VRNNKRATCW VVIFWILAVL MGMPHYLMYS HTNNECVGEF ANETSGWFPV FLNTKVNICG YLAPIALMAY TYNRMVRFII NYVGKWHMQT LHVLLVVVVS FASFWFPFNL ALFLESIRLL AGVYNDTLQN VIIFCLYVGQ FLAYVRACLN PGIYILVGTQ MRKDMWTTLR VFACCCVKQE IPYQDIDIEL QKDIQRRAKH TKRTHYDRKN APMESGEEEF LL //