CCR5_MOUSE
ID CCR5_MOUSE Reviewed; 354 AA.
AC P51682; O35313; O35891; P97308; P97405; Q3ZAZ8; Q61867;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 181.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/SvJ; TISSUE=Spleen;
RX PubMed=8631787; DOI=10.1074/jbc.271.13.7551;
RA Boring L., Gosling J., Monteclaro F.S., Lusis A.J., Tsou C.-L., Charo I.F.;
RT "Molecular cloning and functional expression of murine JE (monocyte
RT chemoattractant protein 1) and murine macrophage inflammatory protein
RT 1alpha receptors: evidence for two closely linked C-C chemokine receptors
RT on chromosome 9.";
RL J. Biol. Chem. 271:7551-7558(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus;
RX PubMed=8662890; DOI=10.1074/jbc.271.24.14445;
RA Meyer A., Coyle A.J., Proudfoot A.E.I., Wells T.N.C., Power C.A.;
RT "Cloning and characterization of a novel murine macrophage inflammatory
RT protein-1 alpha receptor.";
RL J. Biol. Chem. 271:14445-14451(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Ola;
RA Kuziel W.A., Beck M.A., Dawson T.C., Maeda N.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J, and NIH Swiss; TISSUE=Kidney, Liver, and Spleen;
RX PubMed=9343222; DOI=10.1128/jvi.71.11.8642-8656.1997;
RA Kuhmann S.E., Platt E.J., Kozak S.L., Kabat D.;
RT "Polymorphisms in the CCR5 genes of African green monkeys and mice
RT implicate specific amino acids in infections by simian and human
RT immunodeficiency viruses.";
RL J. Virol. 71:8642-8656(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129;
RX PubMed=9261347; DOI=10.1128/jvi.71.9.6305-6314.1997;
RA Doranz B.J., Lu Z.H., Rucker J., Zhang T.Y., Sharron M., Cen Y.H.,
RA Wang Z.X., Guo H.H., Du J.G., Accavitti M.A., Doms R.W., Peiper S.C.;
RT "Two distinct CCR5 domains can mediate coreceptor usage by human
RT immunodeficiency virus type 1.";
RL J. Virol. 71:6305-6314(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Guo B., Kuno K., Harada A., Matsushima K.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
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 (By similarity). {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; U47036; AAC52454.1; -; mRNA.
DR EMBL; X94151; CAA63867.1; -; mRNA.
DR EMBL; U68565; AAB37273.1; -; Genomic_DNA.
DR EMBL; U83327; AAC53386.1; -; Genomic_DNA.
DR EMBL; AF022990; AAC53389.1; -; Genomic_DNA.
DR EMBL; AF019772; AAB71183.1; -; Genomic_DNA.
DR EMBL; D83648; BAA12024.1; -; mRNA.
DR EMBL; AK141906; BAE24879.1; -; mRNA.
DR EMBL; AK154595; BAE32698.1; -; mRNA.
DR EMBL; AK155628; BAE33354.1; -; mRNA.
DR EMBL; AK155867; BAE33471.1; -; mRNA.
DR EMBL; CH466671; EDL37177.1; -; Genomic_DNA.
DR EMBL; BC103574; AAI03575.1; -; mRNA.
DR EMBL; BC103586; AAI03587.1; -; mRNA.
DR EMBL; BC103587; AAI03588.1; -; mRNA.
DR CCDS; CCDS40821.1; -.
DR RefSeq; NP_034047.2; NM_009917.5.
DR AlphaFoldDB; P51682; -.
DR SMR; P51682; -.
DR IntAct; P51682; 4.
DR STRING; 10090.ENSMUSP00000107069; -.
DR BindingDB; P51682; -.
DR ChEMBL; CHEMBL3676; -.
DR DrugCentral; P51682; -.
DR GlyGen; P51682; 1 site.
DR iPTMnet; P51682; -.
DR PhosphoSitePlus; P51682; -.
DR EPD; P51682; -.
DR MaxQB; P51682; -.
DR PaxDb; P51682; -.
DR PRIDE; P51682; -.
DR ProteomicsDB; 281256; -.
DR ABCD; P51682; 6 sequenced antibodies.
DR Antibodypedia; 29674; 1809 antibodies from 49 providers.
DR DNASU; 12774; -.
DR Ensembl; ENSMUST00000111442; ENSMUSP00000107069; ENSMUSG00000079227.
DR GeneID; 12774; -.
DR KEGG; mmu:12774; -.
DR UCSC; uc009shd.2; mouse.
DR CTD; 1234; -.
DR MGI; MGI:107182; Ccr5.
DR VEuPathDB; HostDB:ENSMUSG00000079227; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P51682; -.
DR OMA; HYTCSPH; -.
DR OrthoDB; 937138at2759; -.
DR PhylomeDB; P51682; -.
DR TreeFam; TF330966; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 12774; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Ccr5; mouse.
DR PRO; PR:P51682; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P51682; protein.
DR Bgee; ENSMUSG00000079227; Expressed in lumbar subsegment of spinal cord and 108 other tissues.
DR ExpressionAtlas; P51682; baseline and differential.
DR Genevisible; P51682; MM.
DR GO; GO:0009986; C:cell surface; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; ISO:MGI.
DR GO; GO:0019957; F:C-C chemokine binding; IPI:BHF-UCL.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IDA:MGI.
DR GO; GO:0071791; F:chemokine (C-C motif) ligand 5 binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0006952; P:defense response; IMP:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0030517; P:negative regulation of axon extension; ISO:MGI.
DR GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IDA:BHF-UCL.
DR GO; GO:2000178; P:negative regulation of neural precursor cell proliferation; ISO:MGI.
DR GO; GO:0070997; P:neuron death; ISO:MGI.
DR GO; GO:0060139; P:positive regulation of apoptotic process by virus; ISO:MGI.
DR GO; GO:0022409; P:positive regulation of cell-cell adhesion; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0031622; P:positive regulation of fever generation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR GO; GO:0032731; P:positive regulation of interleukin-1 beta production; ISO:MGI.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISO:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISO:MGI.
DR GO; GO:0014808; P:release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0070723; P:response to cholesterol; ISO:MGI.
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_0000069269"
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 12
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"
FT VARIANT 11
FT /note="S -> I"
FT VARIANT 97
FT /note="V -> I"
FT VARIANT 109
FT /note="L -> V"
FT VARIANT 156
FT /note="A -> V"
FT VARIANT 213
FT /note="V -> I"
FT VARIANT 318
FT /note="M -> I"
FT VARIANT 337
FT /note="A -> V"
FT CONFLICT 3
FT /note="F -> L (in Ref. 2; CAA63867)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="K -> R (in Ref. 4; AAC53386)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="V -> M (in Ref. 4; AAC53386)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="L -> F (in Ref. 2; CAA63867)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="N -> I (in Ref. 5; AAB71183)"
FT /evidence="ECO:0000305"
FT CONFLICT 160
FT /note="F -> S (in Ref. 4; AAC53386)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="P -> L (in Ref. 4; AAC53386)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="H -> Y (in Ref. 3; AAB37273)"
FT /evidence="ECO:0000305"
FT CONFLICT 208
FT /note="P -> S (in Ref. 1; AAC52454)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 354 AA; 40785 MW; D91F50EC9C956795 CRC64;
MDFQGSVPTY SYDIDYGMSA PCQKINVKQI AAQLLPPLYS LVFIFGFVGN MMVFLILISC
KKLKSVTDIY LLNLAISDLL FLLTLPFWAH YAANEWVFGN IMCKVFTGLY HIGYFGGIFF
IILLTIDRYL AIVHAVFALK VRTVNFGVIT SVVTWAVAVF ASLPEIIFTR SQKEGFHYTC
SPHFPHTQYH FWKSFQTLKM VILSLILPLL VMVICYSGIL HTLFRCRNEK KRHRAVRLIF
AIMIVYFLFW TPYNIVLLLT TFQEFFGLNN CSSSNRLDQA MQATETLGMT HCCLNPVIYA
FVGEKFRSYL SVFFRKHMVK RFCKRCSIFQ QDNPDRASSV YTRSTGEHEV STGL
