US27_HCMVA
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 03-AUG-2022, entry version 111.
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}.
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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 PRIDE; P09703; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
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 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
