CCL11_MOUSE
ID CCL11_MOUSE Reviewed; 97 AA.
AC P48298;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Eotaxin;
DE AltName: Full=C-C motif chemokine 11;
DE AltName: Full=Eosinophil chemotactic protein;
DE AltName: Full=Small-inducible cytokine A11;
DE Flags: Precursor;
GN Name=Ccl11; Synonyms=Scya11;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INDUCTION.
RC TISSUE=Lung;
RX PubMed=7568052; DOI=10.1073/pnas.92.19.8960;
RA Rothenberg M.E., Luster A.D., Leder P.;
RT "Murine eotaxin: an eosinophil chemoattractant inducible in endothelial
RT cells and in interleukin 4-induced tumor suppression.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:8960-8964(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC STRAIN=C57BL/6J; TISSUE=Lung;
RX PubMed=8574847; DOI=10.1016/s1074-7613(00)80293-9;
RA Gonzalo J.-A., Jia G.-Q., Aguirre V., Friend D., Coyle A.J., Jenkins N.A.,
RA Lin G.-S., Katz H., Lichtman A., Copeland N.G., Kopf M.,
RA Gutierrez-Ramos J.-C.;
RT "Mouse eotaxin expression parallels eosinophil accumulation during lung
RT allergic inflammation but it is not restricted to a Th2-type response.";
RL Immunity 4:1-14(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=B10.S/J, BALB/cJ, DBA/2J, NOD/LtJ, and SJL/J; TISSUE=Spleen;
RX PubMed=10438970;
RA Teuscher C., Butterfield R.J., Ma R.Z., Zachary J.F., Doerge R.W.,
RA Blankenhorn E.P.;
RT "Sequence polymorphisms in the chemokines Scya1 (TCA-3), Scya2 (monocyte
RT chemoattractant protein (MCP)-1), and Scya12 (MCP-5) are candidates for
RT eae7, a locus controlling susceptibility to monophasic
RT remitting/nonrelapsing experimental allergic encephalomyelitis.";
RL J. Immunol. 163:2262-2266(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14.
RX PubMed=9169149; DOI=10.1006/geno.1997.4656;
RA Garcia-Zepeda E.A., Rothenberg M.E., Weremowicz S., Sarafi M.N.,
RA Morton C.C., Luster A.D.;
RT "Genomic organization, complete sequence, and chromosomal location of the
RT gene for human eotaxin (SCYA11), an eosinophil-specific CC chemokine.";
RL Genomics 41:471-476(1997).
RN [7]
RP INDUCTION.
RX PubMed=15647285; DOI=10.1074/jbc.m406037200;
RA Pope S.M., Fulkerson P.C., Blanchard C., Saito Akei H., Nikolaidis N.M.,
RA Zimmermann N., Molkentin J.D., Rothenberg M.E.;
RT "Identification of a cooperative mechanism involving interleukin-13 and
RT eotaxin-2 in experimental allergic lung inflammation.";
RL J. Biol. Chem. 280:13952-13961(2005).
CC -!- FUNCTION: In response to the presence of allergens, this protein
CC directly promotes the accumulation of eosinophils (a prominent feature
CC of allergic inflammatory reactions), but not lymphocytes, macrophages
CC or neutrophils (PubMed:7568052, PubMed:8574847). Binds to CCR3 (By
CC similarity). {ECO:0000250|UniProtKB:P51671, ECO:0000269|PubMed:7568052,
CC ECO:0000269|PubMed:8574847}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:7568052}.
CC -!- TISSUE SPECIFICITY: Expressed constitutively in the thymus. Expression
CC inducible in the lung (type I alveolar epithelial cells), intestine,
CC heart, spleen, kidney. {ECO:0000269|PubMed:7568052}.
CC -!- INDUCTION: By interferon gamma and lipopolysaccharides (LPS)
CC (PubMed:7568052). By interleukin-13 (IL13) (PubMed:15647285).
CC {ECO:0000269|PubMed:15647285, ECO:0000269|PubMed:7568052}.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; U26426; AAC52256.1; -; mRNA.
DR EMBL; U40672; AAA99776.1; -; mRNA.
DR EMBL; AF128205; AAF22546.1; -; mRNA.
DR EMBL; AF128206; AAF22547.1; -; mRNA.
DR EMBL; AF128207; AAF22548.1; -; mRNA.
DR EMBL; AF128208; AAF22549.1; -; mRNA.
DR EMBL; AF128209; AAF22550.1; -; mRNA.
DR EMBL; AK010146; BAB26731.1; -; mRNA.
DR EMBL; BC027521; AAH27521.1; -; mRNA.
DR EMBL; U77462; AAC53321.1; -; Genomic_DNA.
DR CCDS; CCDS36246.1; -.
DR RefSeq; NP_035460.1; NM_011330.3.
DR AlphaFoldDB; P48298; -.
DR SMR; P48298; -.
DR BioGRID; 203117; 1.
DR STRING; 10090.ENSMUSP00000000342; -.
DR GlyGen; P48298; 1 site.
DR iPTMnet; P48298; -.
DR PhosphoSitePlus; P48298; -.
DR PaxDb; P48298; -.
DR PRIDE; P48298; -.
DR ABCD; P48298; 1 sequenced antibody.
DR Antibodypedia; 15485; 400 antibodies from 43 providers.
DR DNASU; 20292; -.
DR Ensembl; ENSMUST00000000342; ENSMUSP00000000342; ENSMUSG00000020676.
DR GeneID; 20292; -.
DR KEGG; mmu:20292; -.
DR UCSC; uc007kmr.2; mouse.
DR CTD; 6356; -.
DR MGI; MGI:103576; Ccl11.
DR VEuPathDB; HostDB:ENSMUSG00000020676; -.
DR eggNOG; ENOG502S8M4; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_1_0_1; -.
DR InParanoid; P48298; -.
DR OMA; CFTLANR; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P48298; -.
DR TreeFam; TF334888; -.
DR BioGRID-ORCS; 20292; 2 hits in 73 CRISPR screens.
DR PRO; PR:P48298; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P48298; protein.
DR Bgee; ENSMUSG00000020676; Expressed in uterine cervix and 101 other tissues.
DR Genevisible; P48298; MM.
DR GO; GO:0005576; C:extracellular region; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0031728; F:CCR3 chemokine receptor binding; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; ISO:MGI.
DR GO; GO:0046983; F:protein dimerization activity; ISO:MGI.
DR GO; GO:0048018; F:receptor ligand activity; ISO:MGI.
DR GO; GO:0007015; P:actin filament organization; ISO:MGI.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
DR GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
DR GO; GO:0048245; P:eosinophil chemotaxis; ISO:MGI.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; ISO:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0007611; P:learning or memory; IDA:ARUK-UCL.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
DR GO; GO:0002551; P:mast cell chemotaxis; ISO:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0050768; P:negative regulation of neurogenesis; IDA:ARUK-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IMP:BHF-UCL.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR GO; GO:0035962; P:response to interleukin-13; IEA:Ensembl.
DR GO; GO:0070670; P:response to interleukin-4; IEA:Ensembl.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR000827; Chemokine_CC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE 2: Evidence at transcript level;
KW Chemotaxis; Cytokine; Disulfide bond; Glycoprotein; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..97
FT /note="Eotaxin"
FT /id="PRO_0000005197"
FT CARBOHYD 94
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250|UniProtKB:P51671"
FT DISULFID 32..57
FT /evidence="ECO:0000250|UniProtKB:P51671"
FT DISULFID 33..73
FT /evidence="ECO:0000250|UniProtKB:P51671"
SQ SEQUENCE 97 AA; 10893 MW; 36C9812107FC6CA7 CRC64;
MQSSTALLFL LLTVTSFTSQ VLAHPGSIPT SCCFIMTSKK IPNTLLKSYK RITNNRCTLK
AIVFKTRLGK EICADPKKKW VQDATKHLDQ KLQTPKP
