ID CCR1_MOUSE Reviewed; 355 AA. AC P51675; Q6ZWR7; Q91VP9; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 2. DT 04-NOV-2026, entry version 186. DE RecName: Full=C-C chemokine receptor type 1; DE Short=C-C CKR-1; DE Short=CC-CKR-1; DE Short=CCR-1; DE Short=CCR1; DE AltName: Full=Macrophage inflammatory protein 1-alpha receptor; DE Short=MIP-1alpha-R; DE AltName: Full=RANTES-R; DE AltName: CD_antigen=CD191; GN Name=Ccr1; Synonyms=Cmkbr1; 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/Sv; TISSUE=Peritoneal macrophage; RX PubMed=7594543; DOI=10.4049/jimmunol.155.11.5299; RA Post T.W., Bozic C.R., Rothenberg M.E., Luster A.D., Gerard N., Gerard C.; RT "Molecular characterization of two murine eosinophil beta chemokine RT receptors."; RL J. Immunol. 155:5299-5305(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=129/SvJ; RX PubMed=7542241; DOI=10.1074/jbc.270.29.17494; RA Gao J.-L., Murphy P.M.; RT "Cloning and differential tissue-specific expression of three mouse beta RT chemokine receptor-like genes, including the gene for a functional RT macrophage inflammatory protein-1 alpha receptor."; RL J. Biol. Chem. 270:17494-17501(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Bone; 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 [4] 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Mammary gland; 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). RN [6] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=9166425; DOI=10.1084/jem.185.11.1959; RA Gao J.L., Wynn T.A., Chang Y., Lee E.J., Broxmeyer H.E., Cooper S., RA Tiffany H.L., Westphal H., Kwon-Chung J., Murphy P.M.; RT "Impaired host defense, hematopoiesis, granulomatous inflammation and type RT 1-type 2 cytokine balance in mice lacking CC chemokine receptor 1."; RL J. Exp. Med. 185:1959-1968(1997). RN [7] RP FUNCTION. RX PubMed=15831559; DOI=10.1189/jlb.0404237; RA Ramos C.D., Canetti C., Souto J.T., Silva J.S., Hogaboam C.M., RA Ferreira S.H., Cunha F.Q.; RT "MIP-1alpha[CCL3] acting on the CCR1 receptor mediates neutrophil migration RT in immune inflammation via sequential release of TNF-alpha and LTB4."; RL J. Leukoc. Biol. 78:167-177(2005). RN [8] RP FUNCTION. RX PubMed=31898284; DOI=10.1007/s13311-019-00821-5; RA Yan J., Zuo G., Sherchan P., Huang L., Ocak U., Xu W., Travis Z.D., RA Wang W., Zhang J.H., Tang J.; RT "CCR1 Activation Promotes Neuroinflammation Through CCR1/TPR1/ERK1/2 RT Signaling Pathway After Intracerebral Hemorrhage in Mice."; RL Neurotherapeutics 17:1170-1183(2020). CC -!- FUNCTION: Chemokine receptor that plays a crucial role in regulating CC immune cell migration, inflammation, and immune responses CC (PubMed:9166425). Contributes to the inflammatory response by CC recruiting immune cells, such as monocytes, macrophages, T-cells, and CC dendritic cells, to sites of inflammation for the clearance of CC pathogens and the resolution of tissue damage. When activated by its CC ligands including CCL3, CCL5-9, CCL13-16 and CCL23, triggers a CC signaling cascade within immune cells, leading to their migration CC towards the source of the chemokine (By similarity). For example, CC mediates neutrophil migration after activation by CCL3 leading to the CC sequential release of TNF and leukotriene B4 (PubMed:15831559). Also CC mediates monocyte migration upon CXCL4 binding (By similarity). CC Activation by CCL5 results in neuroinflammation through the ERK1/2 CC signaling pathway (PubMed:31898284). {ECO:0000250|UniProtKB:P32246, CC ECO:0000269|PubMed:15831559, ECO:0000269|PubMed:31898284, CC ECO:0000269|PubMed:9166425}. CC -!- SUBUNIT: Interacts with CREB3. Interacts with CCL3. Interacts with CC CCL15. Interacts with CCL23. Interacts with GNAI1. Interacts with CC PF4/CXCL4. {ECO:0000250|UniProtKB:P32246}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P32246}; CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P32246}. CC -!- TISSUE SPECIFICITY: Detected in the heart, spleen, lung, peritoneal CC exudate cells and leukocytes. CC -!- DISRUPTION PHENOTYPE: Deletion mice are viable and fertile, and exhibit CC normal growth, development, anatomy and behavior compared to wild-type CC littermates. However, mature neutrophils from mutant mice fail to CC chemotax in vitro and fail to mobilize into peripheral blood in vivo in CC response to CCL3. They also have accelerated mortality when challenged CC with Aspergillus fumigatus, a fungus controlled principally by CC neutrophil. {ECO:0000269|PubMed:9166425}. CC -!- SIMILARITY: Belongs to the G protein-coupled receptor 1 family. CC {ECO:0000255|PROSITE-ProRule:PRU00521}. 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; U29678; AAA86119.1; -; mRNA. DR EMBL; U28404; AAA89153.1; -; Genomic_DNA. DR EMBL; AK036597; BAC29500.1; -; mRNA. DR EMBL; AK036690; BAC29535.1; -; mRNA. DR EMBL; CH466671; EDL37173.1; -; Genomic_DNA. DR EMBL; BC011092; AAH11092.1; -; mRNA. DR CCDS; CCDS23666.1; -. DR PIR; I49339; I49339. DR RefSeq; NP_034042.3; NM_009912.4. DR AlphaFoldDB; P51675; -. DR SMR; P51675; -. DR BioGRID; 198768; 1. DR FunCoup; P51675; 514. DR STRING; 10090.ENSMUSP00000026911; -. DR BindingDB; P51675; -. DR ChEMBL; CHEMBL3872; -. DR iPTMnet; P51675; -. DR PhosphoSitePlus; P51675; -. DR jPOST; P51675; -. DR PaxDb; 10090-ENSMUSP00000026911; -. DR ProteomicsDB; 279949; -. DR DNASU; 12768; -. DR Ensembl; ENSMUST00000026911.6; ENSMUSP00000026911.5; ENSMUSG00000025804.6. DR GeneID; 12768; -. DR KEGG; mmu:12768; -. DR UCSC; uc009sgy.2; mouse. DR AGR; MGI:104618; -. DR CTD; 1230; -. DR MGI; MGI:104618; Ccr1. DR VEuPathDB; HostDB:ENSMUSG00000025804; -. DR eggNOG; KOG3656; Eukaryota. DR GeneTree; ENSGT01020000230359; -. DR HOGENOM; CLU_009579_8_3_1; -. DR InParanoid; P51675; -. DR OMA; AASPCYK; -. DR OrthoDB; 5970631at2759; -. DR PhylomeDB; P51675; -. DR Reactome; R-MMU-418594; G alpha (i) signalling events. DR BioGRID-ORCS; 12768; 4 hits in 78 CRISPR screens. DR PRO; PR:P51675; -. DR Proteomes; UP000000589; Chromosome 9. DR RNAct; P51675; protein. DR Bgee; ENSMUSG00000025804; Expressed in granulocyte and 75 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009897; C:external side of plasma membrane; ISO:GO_Central. DR GO; GO:0043025; C:neuronal cell body; IEA:Ensembl. DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB. DR GO; GO:0019957; F:C-C chemokine binding; ISO:GO_Central. 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:GO_Central. DR GO; GO:0035717; F:chemokine (C-C motif) ligand 7 binding; ISO:GO_Central. DR GO; GO:0004950; F:chemokine receptor activity; ISO:GO_Central. DR GO; GO:0004435; F:phosphatidylinositol-4,5-bisphosphate phospholipase C activity; ISO:GO_Central. DR GO; GO:0006816; P:calcium ion transport; ISO:GO_Central. DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central. DR GO; GO:0007249; P:canonical NF-kappaB signal transduction; ISO:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; ISO:GO_Central. DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; IEA:Ensembl. DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl. DR GO; GO:0021549; P:cerebellum development; IEA:Ensembl. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISO:GO_Central. DR GO; GO:0006887; P:exocytosis; ISO:GO_Central. DR GO; GO:0006955; P:immune response; ISO:GO_Central. DR GO; GO:0006954; P:inflammatory response; IMP:MGI. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; ISO:GO_Central. DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI. DR GO; GO:0002548; P:monocyte chemotaxis; ISO:GO_Central. DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI. DR GO; GO:0030502; P:negative regulation of bone mineralization; ISO:GO_Central. DR GO; GO:1900016; P:negative regulation of cytokine production involved in inflammatory response; ISO:GO_Central. DR GO; GO:0010629; P:negative regulation of gene expression; ISO:GO_Central. DR GO; GO:0045824; P:negative regulation of innate immune response; IMP:BHF-UCL. DR GO; GO:0051928; P:positive regulation of calcium ion transport; ISO:GO_Central. DR GO; GO:0030335; P:positive regulation of cell migration; ISO:GO_Central. DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:GO_Central. DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:GO_Central. DR GO; GO:0050729; P:positive regulation of inflammatory response; ISO:GO_Central. DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB. DR GO; GO:0150078; P:positive regulation of neuroinflammatory response; IDA:UniProtKB. DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:GO_Central. DR GO; GO:0023019; P:signal transduction involved in regulation of gene expression; ISO:GO_Central. DR CDD; cd15183; 7tmA_CCR1; 1. DR FunFam; 1.20.1070.10:FF:000026; C-C chemokine receptor type 5; 1. DR Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1. DR InterPro; IPR050119; CCR1-9-like. DR InterPro; IPR002236; Chemokine_CCR1. DR InterPro; IPR000355; Chemokine_rcpt. DR InterPro; IPR000276; GPCR_Rhodpsn. DR InterPro; IPR017452; GPCR_Rhodpsn_7TM. DR PANTHER; PTHR10489:SF711; C-C CHEMOKINE RECEPTOR TYPE 1; 1. DR PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1. DR Pfam; PF00001; 7tm_1; 1. DR PRINTS; PR00657; CCCHEMOKINER. DR PRINTS; PR01106; CHEMOKINER1. DR PRINTS; PR00237; GPCRRHODOPSN. DR SUPFAM; SSF81321; Family A G protein-coupled receptor-like; 1. 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; Membrane; KW Receptor; Reference proteome; Transducer; Transmembrane; KW Transmembrane helix. FT CHAIN 1..355 FT /note="C-C chemokine receptor type 1" FT /id="PRO_0000069231" FT TOPO_DOM 1..34 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 35..60 FT /note="Helical; Name=1" FT /evidence="ECO:0000255" FT TOPO_DOM 61..64 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 65..91 FT /note="Helical; Name=2" FT /evidence="ECO:0000255" FT TOPO_DOM 92..107 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 108..129 FT /note="Helical; Name=3" FT /evidence="ECO:0000255" FT TOPO_DOM 130..146 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 147..171 FT /note="Helical; Name=4" FT /evidence="ECO:0000255" FT TOPO_DOM 172..197 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 198..223 FT /note="Helical; Name=5" FT /evidence="ECO:0000255" FT TOPO_DOM 224..239 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 240..264 FT /note="Helical; Name=6" FT /evidence="ECO:0000255" FT TOPO_DOM 265..281 FT /note="Extracellular" FT /evidence="ECO:0000255" FT TRANSMEM 282..305 FT /note="Helical; Name=7" FT /evidence="ECO:0000255" FT TOPO_DOM 306..355 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT DISULFID 106..183 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521" FT CONFLICT 55 FT /note="V -> M (in Ref. 1; AAA86119)" FT /evidence="ECO:0000305" FT CONFLICT 149 FT /note="F -> L (in Ref. 1; AAA86119 and 2; AAA89153)" FT /evidence="ECO:0000305" FT CONFLICT 278 FT /note="Q -> H (in Ref. 1; AAA86119 and 2; AAA89153)" FT /evidence="ECO:0000305" SQ SEQUENCE 355 AA; 40895 MW; 41B0D566A56BC4F7 CRC64; MEISDFTEAY PTTTEFDYGD STPCQKTAVR AFGAGLLPPL YSLVFIIGVV GNVLVILVLM QHRRLQSMTS IYLFNLAVSD LVFLFTLPFW IDYKLKDDWI FGDAMCKLLS GFYYLGLYSE IFFIILLTID RYLAIVHAVF ALRARTVTFG IITSIITWAL AILASMPALY FFKAQWEFTH RTCSPHFPYK SLKQWKRFQA LKLNLLGLIL PLLVMIICYA GIIRILLRRP SEKKVKAVRL IFAITLLFFL LWTPYNLSVF VSAFQDVLFT NQCEQSKQLD LAMQVTEVIA YTHCCVNPII YVFVGERFWK YLRQLFQRHV AIPLAKWLPF LSVDQLERTS SISPSTGEHE LSAGF //