位置:首页 > 蛋白库 > US28_HCMVA
US28_HCMVA
ID   US28_HCMVA              Reviewed;         354 AA.
AC   P69332; P09704; P32952; Q7M6H3;
DT   15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
DE   RecName: Full=G-protein coupled receptor homolog US28;
DE   AltName: Full=HHRF3;
GN   Name=US28;
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   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Isolate clinical VHL/E;
RX   PubMed=7540006; DOI=10.1006/bbrc.1995.1814;
RA   Kuhn D.E., Beall C.J., Kolattukudy P.E.;
RT   "The cytomegalovirus US28 protein binds multiple CC chemokines with high
RT   affinity.";
RL   Biochem. Biophys. Res. Commun. 211:325-330(1995).
RN   [4]
RP   CHARACTERIZATION.
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   [5]
RP   IDENTIFICATION OF C-TERMINAL FRAMESHIFT, AND FUNCTION.
RX   PubMed=7961796; DOI=10.1016/s0021-9258(19)61936-8;
RA   Gao J.-L., Murphy P.M.;
RT   "Human cytomegalovirus open reading frame US28 encodes a functional beta
RT   chemokine receptor.";
RL   J. Biol. Chem. 269:28539-28542(1994).
RN   [6]
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   [7]
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   [8]
RP   FUNCTION.
RX   PubMed=11050102; DOI=10.1074/jbc.m008965200;
RA   Casarosa P., Bakker R.A., Verzijl D., Navis M., Timmerman H., Leurs R.,
RA   Smit M.J.;
RT   "Constitutive signaling of the human cytomegalovirus-encoded chemokine
RT   receptor US28.";
RL   J. Biol. Chem. 276:1133-1137(2001).
RN   [9]
RP   PHOSPHORYLATION.
RX   PubMed=12244063; DOI=10.1074/jbc.m208214200;
RA   Mokros T., Rehm A., Droese J., Oppermann M., Lipp M., Hopken U.E.;
RT   "Surface expression and endocytosis of the human cytomegalovirus-encoded
RT   chemokine receptor US28 is regulated by agonist-independent
RT   phosphorylation.";
RL   J. Biol. Chem. 277:45122-45128(2002).
RN   [10]
RP   INTERACTION WITH HOST GPRASP1.
RX   PubMed=20102549; DOI=10.1111/j.1600-0854.2010.1045.x;
RA   Tschische P., Moser E., Thompson D., Vischer H.F., Parzmair G.P.,
RA   Pommer V., Platzer W., Schwarzbraun T., Schaider H., Smit M.J., Martini L.,
RA   Whistler J.L., Waldhoer M.;
RT   "The G-protein coupled receptor associated sorting protein GASP-1 regulates
RT   the signalling and trafficking of the viral chemokine receptor US28.";
RL   Traffic 11:660-674(2010).
RN   [11] {ECO:0007744|PDB:4XT1, ECO:0007744|PDB:4XT3}
RP   X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) IN COMPLEX WITH HOST CX3CL1,
RP   INTERACTION WITH HOST CX3CL1, AND FUNCTION.
RX   PubMed=25745166; DOI=10.1126/science.aaa5026;
RA   Burg J.S., Ingram J.R., Venkatakrishnan A.J., Jude K.M., Dukkipati A.,
RA   Feinberg E.N., Angelini A., Waghray D., Dror R.O., Ploegh H.L.,
RA   Garcia K.C.;
RT   "Structural basis for chemokine recognition and activation of a viral G
RT   protein-coupled receptor.";
RL   Science 347:1113-1117(2015).
RN   [12] {ECO:0007744|PDB:7RKF, ECO:0007744|PDB:7RKM, ECO:0007744|PDB:7RKN}
RP   STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS) IN COMPLEX WITH HOST
RP   GNB1; GNA11; CX3CL1 AND GNG2, INTERACTION WITH HOST GNA11, STRUCTURE BY
RP   ELECTRON MICROSCOPY (3.50 ANGSTROMS) IN COMPLEX WITH HOST GNB1; GNAI1;
RP   CX3CL1 AND GNG2, AND FUNCTION.
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: Binds to a great number of different CC-chemokines including
CC       CCL5/RANTES, CCL2/MCP-1, CCL3/MIP-1-alpha as well as CX3CL1/Fractalkine
CC       (PubMed:7961796, PubMed:25745166, PubMed:7540006). Transduces signals
CC       resulting in the activation of MAP kinase signaling pathways and
CC       augmentation of intracellular calcium ion levels, leading to
CC       alterations in chemotactic behavior of vascular smooth muscle cells and
CC       macrophages. The US28 receptor also exhibits high levels of agonist-
CC       independent signaling activity and agonist-independent endocytosis
CC       (PubMed:11050102, PubMed:25745166). Interacts with the host Gi complex
CC       without activating it, thereby probably interfering with the chemokine-
CC       Gi signaling (PubMed:35061538). May also function as a G protein sink
CC       to sequester G protein from the cell surface via internalization
CC       (PubMed:35061538). Interacts with endogenous Gaq/11 subunits and
CC       thereby constitutively activates phospholipase C (PubMed:11050102).
CC       {ECO:0000269|PubMed:11050102, ECO:0000269|PubMed:25745166,
CC       ECO:0000269|PubMed:35061538, ECO:0000269|PubMed:7540006,
CC       ECO:0000269|PubMed:7961796}.
CC   -!- SUBUNIT: Interacts with host GPRASP1; this interaction targets US28 to
CC       lysosomes for degradation (PubMed:20102549). Interacts with host
CC       CX3CL1/Fractalkine (via N-terminus) (PubMed:25745166). Interacts with
CC       host Gi alpha-1 subunit GNAI1; this interaction does not lead to the
CC       catalytic activation of Gi complex (PubMed:35061538).
CC       {ECO:0000269|PubMed:20102549, ECO:0000269|PubMed:25745166,
CC       ECO:0000269|PubMed:35061538}.
CC   -!- INTERACTION:
CC       P69332; P78423: CX3CL1; Xeno; NbExp=4; IntAct=EBI-16147206, EBI-15188013;
CC   -!- SUBCELLULAR LOCATION: Host cell membrane; Multi-pass membrane protein.
CC   -!- PTM: Phosphorylated. High phosphorylation occurs concomitantly with
CC       receptor endocytosis and correlate with low receptor presence at the
CC       plasma membrane. {ECO:0000269|PubMed:12244063}.
CC   -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU00521}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA28338.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=CAA35260.1; Type=Frameshift; Evidence={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; X04650; CAA28338.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; X17403; CAA35260.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; L20501; AAA98741.1; -; Genomic_DNA.
DR   PIR; C27216; QQBED3.
DR   PDB; 4XT1; X-ray; 2.89 A; A=1-354.
DR   PDB; 4XT3; X-ray; 3.80 A; A=1-354.
DR   PDB; 7RKF; EM; 4.00 A; F=1-354.
DR   PDB; 7RKM; EM; 3.50 A; F=1-354.
DR   PDB; 7RKN; EM; 3.60 A; F=1-354.
DR   PDBsum; 4XT1; -.
DR   PDBsum; 4XT3; -.
DR   PDBsum; 7RKF; -.
DR   PDBsum; 7RKM; -.
DR   PDBsum; 7RKN; -.
DR   SMR; P69332; -.
DR   DIP; DIP-61489N; -.
DR   IntAct; P69332; 1.
DR   BindingDB; P69332; -.
DR   ChEMBL; CHEMBL4259; -.
DR   iPTMnet; P69332; -.
DR   ABCD; P69332; 1 sequenced antibody.
DR   Proteomes; UP000008991; 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:0004950; F:chemokine receptor activity; IEA:InterPro.
DR   GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR   GO; GO:0044864; P:positive regulation by virus of host cell division; IDA:CACAO.
DR   GO; GO:0039553; P:suppression by virus of host chemokine activity; IEA:UniProtKB-KW.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
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.
FT   CHAIN           1..354
FT                   /note="G-protein coupled receptor homolog US28"
FT                   /id="PRO_0000070246"
FT   TOPO_DOM        1..37
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical; Name=1"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..69
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        70..90
FT                   /note="Helical; Name=2"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        91..101
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        102..122
FT                   /note="Helical; Name=3"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        123..145
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        146..166
FT                   /note="Helical; Name=4"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        167..183
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        184..204
FT                   /note="Helical; Name=5"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        205..228
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        229..249
FT                   /note="Helical; Name=6"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        250..273
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical; Name=7"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        295..354
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine; by host"
FT                   /evidence="ECO:0000255"
FT   VARIANT         18..19
FT                   /note="ED -> DE (in strain: Isolate clinical VHL/E)"
FT   VARIANT         25
FT                   /note="F -> L (in strain: Isolate clinical VHL/E)"
FT   VARIANT         267
FT                   /note="R -> K (in strain: Isolate clinical VHL/E)"
FT   VARIANT         346
FT                   /note="V -> A (in strain: Isolate clinical VHL/E)"
FT   HELIX           26..59
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           67..83
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           86..94
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           104..133
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           141..157
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           160..163
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   STRAND          166..169
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   STRAND          172..175
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   STRAND          177..180
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           184..196
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           198..215
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           223..255
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           263..280
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           283..290
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   TURN            291..294
FT                   /evidence="ECO:0007829|PDB:4XT1"
FT   HELIX           296..308
FT                   /evidence="ECO:0007829|PDB:4XT1"
SQ   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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024