US28_HCMVM
ID US28_HCMVM Reviewed; 354 AA.
AC F5HF62;
DT 11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 39.
DE RecName: Full=Envelope protein US28;
GN Name=US28;
OS Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=295027;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15105547; DOI=10.1099/vir.0.79888-0;
RA Dolan A., Cunningham C., Hector R.D., Hassan-Walker A.F., Lee L.,
RA Addison C., Dargan D.J., McGeoch D.J., Gatherer D., Emery V.C.,
RA Griffiths P.D., Sinzger C., McSharry B.P., Wilkinson G.W.G., Davison A.J.;
RT "Genetic content of wild-type human cytomegalovirus.";
RL J. Gen. Virol. 85:1301-1312(2004).
CC -!- FUNCTION: Receptor for a C-C type chemokine. Binds to a great number of
CC different CC-chemokines including CCL5/RANTES, CCL2/MCP-1, CCL3/MIP-1-
CC alpha as well as CX3CL1/Fractalkine. Transduces signals resulting in
CC the activation of MAP kinase signaling pathways and augmentation of
CC intracellular calcium ion levels, leading to alterations in chemotactic
CC behavior of vascular smooth muscle cells and macrophages. The US28
CC receptor also exhibits high levels of agonist-independent signaling
CC activity and agonist-independent endocytosis. Interacts with the host
CC Gi complex without activating it, thereby probably interfering with the
CC chemokine-Gi signaling. May also function as a G protein sink to
CC sequester G protein from the cell surface via internalization.
CC Interacts with endogenous Gaq/11 subunits and thereby constitutively
CC activates phospholipase C. {ECO:0000250|UniProtKB:P69332}.
CC -!- SUBUNIT: Interacts with host GPRASP1; this interaction targets US28 to
CC lysosomes for degradation (By similarity). Interacts with host
CC CX3CL1/Fractalkine (via N-terminus) (By similarity).
CC {ECO:0000250|UniProtKB:P69332}.
CC -!- SUBCELLULAR LOCATION: Host cell membrane
CC {ECO:0000250|UniProtKB:P69332}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P69332}.
CC -!- PTM: Phosphorylated. High phosphorylation occurs concomitantly with
CC receptor endocytosis and correlate with low receptor presence at the
CC plasma membrane. {ECO:0000250|UniProtKB:P69332}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AY446894; AAR31716.1; -; Genomic_DNA.
DR RefSeq; YP_081612.1; NC_006273.2.
DR SMR; F5HF62; -.
DR PRIDE; F5HF62; -.
DR DNASU; 3077536; -.
DR GeneID; 3077536; -.
DR KEGG; vg:3077536; -.
DR Reactome; R-HSA-9609690; HCMV Early Events.
DR Proteomes; UP000000938; 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: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 3: Inferred from homology;
KW 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="Envelope protein US28"
FT /id="PRO_0000418264"
FT TOPO_DOM 1..37
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 38..58
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 59..69
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 70..90
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 91..101
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 102..122
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 123..145
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 167..183
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 184..204
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 205..228
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 250..273
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 274..294
FT /note="Helical"
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"
SQ SEQUENCE 354 AA; 41034 MW; 3C1B7B7C54DF7AAD 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 YHSMSFSRRG SPSRRETSSD TLSDEVCRVS QIIP
