CCR5_RAT
ID CCR5_RAT Reviewed; 354 AA.
AC O08556;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 25-MAY-2022, entry version 143.
DE RecName: Full=C-C chemokine receptor type 5;
DE Short=C-C CKR-5;
DE Short=CC-CKR-5;
DE Short=CCR-5;
DE AltName: Full=MIP-1 alpha receptor;
DE AltName: CD_antigen=CD195;
GN Name=Ccr5; Synonyms=Cmkbr5;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Brain;
RX PubMed=9670989;
RX DOI=10.1002/(sici)1097-4547(19980701)53:1<16::aid-jnr3>3.0.co;2-m;
RA Spleiss O., Gourmala N., Boddeke H.W.G.M., Sauter A., Fiebich B.L.,
RA Berger M., Gebicke-Haerter P.J.;
RT "Cloning of rat HIV-1-chemokine coreceptor CKR5 from microglia and
RT upregulation of its mRNA in ischemic and endotoxinemic rat brain.";
RL J. Neurosci. Res. 53:16-28(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Sprague-Dawley;
RX PubMed=9655467; DOI=10.1016/s0165-5728(98)00005-8;
RA Jiang Y., Salafranca M.N., Adhikari S., Xia Y., Feng L., Sonntag M.K.,
RA deFiebre C.M., Pennell N.A., Streit W.J., Harrison J.K.;
RT "Chemokine receptor expression in cultured glia and rat experimental
RT allergic encephalomyelitis.";
RL J. Neuroimmunol. 86:1-12(1998).
CC -!- FUNCTION: Receptor for a number of inflammatory CC-chemokines including
CC CCL3/MIP-1-alpha, CCL4/MIP-1-beta and RANTES and subsequently
CC transduces a signal by increasing the intracellular calcium ion level.
CC May play a role in the control of granulocytic lineage proliferation or
CC differentiation. Participates in T-lymphocyte migration to the
CC infection site by acting as a chemotactic receptor.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- SUBUNIT: Interacts with PRAF2. Efficient ligand binding to CCL3/MIP-
CC 1alpha and CCL4/MIP-1beta requires sulfation, O-glycosylation and
CC sialic acid modifications. Glycosylation on Ser-6 is required for
CC efficient binding of CCL4. Interacts with GRK2. Interacts with ARRB1
CC and ARRB2. Interacts with CNIH4. Interacts with S100A4; this
CC interaction stimulates T-lymphocyte chemotaxis.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- PTM: Sulfated on at least 2 of the N-terminal tyrosines. Sulfation is
CC required for efficient binding of the chemokines, CCL3 and CCL4 (By
CC similarity). {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: O-glycosylated, but not N-glycosylated. Ser-6 appears to be the
CC major site. Also sialylated glycans present which contribute to
CC chemokine binding. Ser-17 may also be glycosylated and, if so, with
CC small moieties such as a T-antigen (By similarity).
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: Palmitoylation in the C-terminal is important for cell surface
CC expression. {ECO:0000250|UniProtKB:P51681}.
CC -!- PTM: Phosphorylation on serine residues in the C-terminal is stimulated
CC by binding CC chemokines especially by APO-RANTES.
CC {ECO:0000250|UniProtKB:P51681}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; Y12009; CAA72737.1; -; mRNA.
DR EMBL; U77350; AAC03243.1; -; Genomic_DNA.
DR RefSeq; NP_446412.2; NM_053960.3.
DR AlphaFoldDB; O08556; -.
DR SMR; O08556; -.
DR STRING; 10116.ENSRNOP00000066146; -.
DR BindingDB; O08556; -.
DR ChEMBL; CHEMBL1795146; -.
DR GlyGen; O08556; 2 sites.
DR iPTMnet; O08556; -.
DR PhosphoSitePlus; O08556; -.
DR SwissPalm; O08556; -.
DR PaxDb; O08556; -.
DR GeneID; 117029; -.
DR KEGG; rno:117029; -.
DR UCSC; RGD:620596; rat.
DR CTD; 1234; -.
DR RGD; 620596; Ccr5.
DR eggNOG; KOG3656; Eukaryota.
DR InParanoid; O08556; -.
DR OrthoDB; 937138at2759; -.
DR PhylomeDB; O08556; -.
DR Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:O08556; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0009986; C:cell surface; IDA:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0019957; F:C-C chemokine binding; ISO:RGD.
DR GO; GO:0016493; F:C-C chemokine receptor activity; ISS:UniProtKB.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; IPI:RGD.
DR GO; GO:0007568; P:aging; IEP:RGD.
DR GO; GO:0006816; P:calcium ion transport; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:RGD.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:RGD.
DR GO; GO:0006952; P:defense response; ISO:RGD.
DR GO; GO:0042742; P:defense response to bacterium; IEP:RGD.
DR GO; GO:0045444; P:fat cell differentiation; IEP:RGD.
DR GO; GO:0030900; P:forebrain development; IEP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IEP:RGD.
DR GO; GO:0002437; P:inflammatory response to antigenic stimulus; IEP:RGD.
DR GO; GO:0050900; P:leukocyte migration; TAS:RGD.
DR GO; GO:0000165; P:MAPK cascade; ISO:RGD.
DR GO; GO:0030517; P:negative regulation of axon extension; IMP:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:RGD.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; ISO:RGD.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; IMP:RGD.
DR GO; GO:0070997; P:neuron death; IMP:RGD.
DR GO; GO:0060139; P:positive regulation of apoptotic process by virus; IMP:RGD.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; IMP:RGD.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IMP:RGD.
DR GO; GO:0031622; P:positive regulation of fever generation; IMP:RGD.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:RGD.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IMP:RGD.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IMP:RGD.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IMP:RGD.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:RGD.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:RGD.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:RGD.
DR GO; GO:0070723; P:response to cholesterol; ISO:RGD.
DR GO; GO:0010212; P:response to ionizing radiation; IEP:RGD.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
DR GO; GO:0023052; P:signaling; ISO:RGD.
DR InterPro; IPR002240; Chemokine_CCR5.
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; PR01110; CHEMOKINER5.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; G-protein coupled receptor; Glycoprotein;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Receptor;
KW Reference proteome; Sulfation; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..354
FT /note="C-C chemokine receptor type 5"
FT /id="PRO_0000069280"
FT TOPO_DOM 1..32
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 33..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..70
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 71..91
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 92..104
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 105..126
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 127..143
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 144..168
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..200
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 201..220
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..262
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 263..279
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 280..303
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..354
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MOD_RES 10
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 16
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000255"
FT MOD_RES 338
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 339
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 344
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT MOD_RES 351
FT /note="Phosphoserine; by BARK1"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT LIPID 323
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT LIPID 326
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT CARBOHYD 6
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT DISULFID 22..271
FT /evidence="ECO:0000250|UniProtKB:P51681"
FT DISULFID 103..180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
SQ SEQUENCE 354 AA; 41031 MW; 77EDB368AA4C868D CRC64;
MDFQGSIPTY IYDIDYSMSA PCQKVNVKQI AAQLLPPLYS LVFIFGFVGN MMVFLILISC
KKLKSMTDIY LFNLAISDLL FLLTLPFWAH YAANEWVFGN IMCKLFTGIY HIGYFGGIFF
IILLTIDRYL AIVHAVFAIK ARTVNFGVIT SVVTWVVAVF VSLPEIIFMR SQKEGSHYTC
SPHFLHIQYR FWKHFQTLKM VILSLILPLL VMVICYSGIL NTLFRCRNEK KRHRAVRLIF
AIMIVYFLFW TPYNIVLLLT TFQEYFGLNN CSSSNRLDQA MQVTETLGMT HCCLNPVIYA
FVGEKFRNYL SVFFRKHIVK RFCKHCSIFQ QVNPDRVSSV YTRSTGEQEV STGL
