CCR1_MOUSE
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 03-AUG-2022, entry version 169.
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;
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).
CC -!- FUNCTION: Receptor for a C-C type chemokine. Binds to MIP-1-alpha,
CC RANTES, and less efficiently, to MIP-1-beta or MCP-1 and subsequently
CC transduces a signal by increasing the intracellular calcium ions level.
CC Responsible for affecting stem cell proliferation.
CC -!- SUBUNIT: Interacts with CREB3. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- TISSUE SPECIFICITY: Detected in the heart, spleen, lung, peritoneal
CC exudate cells and leukocytes.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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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 STRING; 10090.ENSMUSP00000026911; -.
DR BindingDB; P51675; -.
DR ChEMBL; CHEMBL3872; -.
DR iPTMnet; P51675; -.
DR PhosphoSitePlus; P51675; -.
DR jPOST; P51675; -.
DR MaxQB; P51675; -.
DR PaxDb; P51675; -.
DR PRIDE; P51675; -.
DR ProteomicsDB; 279949; -.
DR DNASU; 12768; -.
DR Ensembl; ENSMUST00000026911; ENSMUSP00000026911; ENSMUSG00000025804.
DR GeneID; 12768; -.
DR KEGG; mmu:12768; -.
DR UCSC; uc009sgy.2; mouse.
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; CYTGIIN; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P51675; -.
DR TreeFam; TF330966; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 12768; 4 hits in 73 CRISPR screens.
DR PRO; PR:P51675; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P51675; protein.
DR Bgee; ENSMUSG00000025804; Expressed in granulocyte and 75 other tissues.
DR Genevisible; P51675; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0019957; F:C-C chemokine binding; ISO:MGI.
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:0035717; F:chemokine (C-C motif) ligand 7 binding; ISO:MGI.
DR GO; GO:0004950; F:chemokine receptor activity; ISO:MGI.
DR GO; GO:0004435; F:phosphatidylinositol phospholipase C activity; ISO:MGI.
DR GO; GO:0006816; P:calcium ion transport; ISO:MGI.
DR GO; GO:0019722; P:calcium-mediated signaling; IBA:GO_Central.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0007267; P:cell-cell signaling; ISO:MGI.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; ISO:MGI.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; ISO:MGI.
DR GO; GO:0006887; P:exocytosis; ISO:MGI.
DR GO; GO:0006955; P:immune response; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR GO; GO:0030099; P:myeloid cell differentiation; IMP:MGI.
DR GO; GO:0030502; P:negative regulation of bone mineralization; ISO:MGI.
DR GO; GO:0010629; P:negative regulation of gene expression; ISO:MGI.
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:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISO:MGI.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0090026; P:positive regulation of monocyte chemotaxis; ISS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; ISO:MGI.
DR InterPro; IPR002236; Chemokine_CCR1.
DR InterPro; IPR034321; Chemokine_CCR1_euk.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR PANTHER; PTHR10489:SF711; PTHR10489:SF711; 1.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR01106; CHEMOKINER1.
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; 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
