CCR3_MOUSE
ID CCR3_MOUSE Reviewed; 359 AA.
AC P51678; Q8K3M7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Probable C-C chemokine receptor type 3;
DE Short=C-C CKR-3;
DE Short=CC-CKR-3;
DE Short=CCR-3;
DE Short=CCR3;
DE Short=CKR3;
DE AltName: Full=Macrophage inflammatory protein 1-alpha receptor-like 2;
DE Short=MIP-1 alpha RL2;
DE AltName: CD_antigen=CD193;
GN Name=Ccr3; Synonyms=Cmkbr1l2, Cmkbr3;
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 [GENOMIC DNA].
RC STRAIN=129/Sv;
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 [GENOMIC DNA].
RC STRAIN=BALB/cJ;
RA Daugherty B.L.;
RT "Molecular Cloning of the Murine BALB/C CCR3 Gene.";
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Aorta, and Vein;
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 [5]
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 [6]
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).
RN [7]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=11830666; DOI=10.1073/pnas.261462598;
RA Humbles A.A., Lu B., Friend D.S., Okinaga S., Lora J., Al-Garawi A.,
RA Martin T.R., Gerard N.P., Gerard C.;
RT "The murine CCR3 receptor regulates both the role of eosinophils and mast
RT cells in allergen-induced airway inflammation and hyperresponsiveness.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:1479-1484(2002).
CC -!- FUNCTION: Receptor for C-C type chemokine. Binds and responds to a
CC variety of chemokines, including CCL11, CCL26, CCL7, CCL13,
CC RANTES(CCL5) and CCL15. Subsequently transduces a signal by increasing
CC the intracellular calcium ions level. In addition acts as a possible
CC functional receptor for NARS1. {ECO:0000250|UniProtKB:P51677}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Detected in skeletal muscle and in trace amounts in
CC leukocytes.
CC -!- DISRUPTION PHENOTYPE: Deficient mice with induced pulmonary
CC inflammation exhibit reduced trafficking of eosinophils from the blood
CC into the lung parenchyma and increased numbers of intraepithelial mast
CC cells in the trachea. Cholinergic stimulation resulted in airway
CC hyperresponsiveness. {ECO:0000269|PubMed:11830666}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U29677; AAA86118.1; -; Genomic_DNA.
DR EMBL; U28406; AAA89155.1; -; Genomic_DNA.
DR EMBL; AY049018; AAL13085.1; -; Genomic_DNA.
DR EMBL; AK041106; BAC30823.1; -; mRNA.
DR EMBL; CH466671; EDL37175.1; -; Genomic_DNA.
DR EMBL; BC108967; AAI08968.1; -; mRNA.
DR EMBL; BC108968; AAI08969.1; -; mRNA.
DR CCDS; CCDS23668.1; -.
DR PIR; I49341; I49341.
DR RefSeq; NP_034044.3; NM_009914.4.
DR RefSeq; XP_017168608.1; XM_017313119.1.
DR RefSeq; XP_017168609.1; XM_017313120.1.
DR AlphaFoldDB; P51678; -.
DR SMR; P51678; -.
DR STRING; 10090.ENSMUSP00000039107; -.
DR BindingDB; P51678; -.
DR ChEMBL; CHEMBL3406; -.
DR iPTMnet; P51678; -.
DR PhosphoSitePlus; P51678; -.
DR PaxDb; P51678; -.
DR PRIDE; P51678; -.
DR ProteomicsDB; 281255; -.
DR Antibodypedia; 3532; 848 antibodies from 42 providers.
DR DNASU; 12771; -.
DR Ensembl; ENSMUST00000039171; ENSMUSP00000039107; ENSMUSG00000035448.
DR GeneID; 12771; -.
DR KEGG; mmu:12771; -.
DR UCSC; uc009sha.2; mouse.
DR CTD; 1232; -.
DR MGI; MGI:104616; Ccr3.
DR VEuPathDB; HostDB:ENSMUSG00000035448; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01020000230359; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; P51678; -.
DR OMA; DMGLLCE; -.
DR OrthoDB; 900867at2759; -.
DR PhylomeDB; P51678; -.
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; 12771; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Ccrl2; mouse.
DR PRO; PR:P51678; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; P51678; protein.
DR Bgee; ENSMUSG00000035448; Expressed in spleen and 16 other tissues.
DR Genevisible; P51678; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0019957; F:C-C chemokine binding; IPI:UniProtKB.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IDA:MGI.
DR GO; GO:0035476; P:angioblast cell migration; 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:0006935; P:chemotaxis; IDA:MGI.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISO:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; 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:0002551; P:mast cell chemotaxis; ISO:MGI.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IMP:BHF-UCL.
DR InterPro; IPR002238; Chemokine_CCR3.
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; PR01108; CHEMOKINER3.
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..359
FT /note="Probable C-C chemokine receptor type 3"
FT /id="PRO_0000069242"
FT TOPO_DOM 1..38
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 39..64
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 65..68
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 69..95
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..111
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 112..133
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 134..150
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..175
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 176..201
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 202..227
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 228..243
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 244..268
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..309
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 310..359
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DISULFID 110..187
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CONFLICT 218
FT /note="I -> V (in Ref. 1; AAA86118 and 2; AAA89155)"
FT /evidence="ECO:0000305"
FT CONFLICT 270
FT /note="S -> R (in Ref. 1; AAA86118)"
FT /evidence="ECO:0000305"
FT CONFLICT 278
FT /note="Q -> E (in Ref. 1; AAA86118 and 2; AAA89155)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="I -> V (in Ref. 1; AAA86118 and 2; AAA89155)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 41783 MW; 40DA3C745B8C05A9 CRC64;
MAFNTDEIKT VVESFETTPY EYEWAPPCEK VRIKELGSWL LPPLYSLVFI IGLLGNMMVV
LILIKYRKLQ IMTNIYLFNL AISDLLFLFT VPFWIHYVLW NEWGFGHYMC KMLSGFYYLA
LYSEIFFIIL LTIDRYLAIV HAVFALRART VTFATITSII TWGLAGLAAL PEFIFHESQD
SFGEFSCSPR YPEGEEDSWK RFHALRMNIF GLALPLLIMV ICYSGIIKTL LRCPNKKKHK
AIRLIFVVMI VFFIFWTPYN LVLLFSAFHS TFLETSCQQS KHLDLAMQVT EVIAYTHCCI
NPVIYAFVGE RFRKHLRLFF HRNVAVYLGK YIPFLPGEKM ERTSSVSPST GEQEISVVF
