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   24-JAN-2024, entry version 169.
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; 10090-ENSMUSP00000039107; -.
DR   ProteomicsDB; 281255; -.
DR   Antibodypedia; 3532; 897 antibodies from 42 providers.
DR   DNASU; 12771; -.
DR   Ensembl; ENSMUST00000039171.9; ENSMUSP00000039107.8; ENSMUSG00000035448.10.
DR   GeneID; 12771; -.
DR   KEGG; mmu:12771; -.
DR   UCSC; uc009sha.2; mouse.
DR   AGR; MGI:104616; -.
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; 4604454at2759; -.
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 77 CRISPR screens.
DR   ChiTaRS; Ccrl2; mouse.
DR   PRO; PR:P51678; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P51678; Protein.
DR   Bgee; ENSMUSG00000035448; Expressed in mesodermal cell in embryo and 17 other cell types or tissues.
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: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   CDD; cd15185; 7tmA_CCR3; 1.
DR   Gene3D; 1.20.1070.10; Rhodopsin 7-helix transmembrane proteins; 1.
DR   InterPro; IPR002238; Chemokine_CCR3.
DR   InterPro; IPR000355; Chemokine_rcpt.
DR   InterPro; IPR000276; GPCR_Rhodpsn.
DR   InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR   PANTHER; PTHR10489:SF649; C-C CHEMOKINE RECEPTOR TYPE 3; 1.
DR   PANTHER; PTHR10489; CELL ADHESION MOLECULE; 1.
DR   Pfam; PF00001; 7tm_1; 1.
DR   PRINTS; PR00657; CCCHEMOKINER.
DR   PRINTS; PR01108; CHEMOKINER3.
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.
DR   Genevisible; P51678; MM.
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
//