CCL11_HUMAN
ID CCL11_HUMAN Reviewed; 97 AA.
AC P51671; P50877; Q92490; Q92491;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 202.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=8597956; DOI=10.1038/nm0496-449;
RA Garcia-Zepeda E.A., Rothenberg M.E., Ownbey T.R., Leder P., Luster A.D.;
RT "Human eotaxin is a specific chemoattractant for eosinophil cells and
RT provides a new mechanism to explain tissue eosinophilia.";
RL Nat. Med. 2:449-456(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8609214; DOI=10.1172/jci118456;
RA Ponath P.D., Qin S., Ringler D.J., Clark-Lewis I., Wang J., Kassam N.,
RA Smith H., Shi X., Gonzalo J.A., Newman W., Gutierrez-Ramos J.-C.,
RA Mackay C.R.;
RT "Cloning of the human eosinophil chemoattractant, eotaxin. Expression,
RT receptor binding, and functional properties suggest a mechanism for the
RT selective recruitment of eosinophils.";
RL J. Clin. Invest. 97:604-612(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Small intestine;
RX PubMed=8631813; DOI=10.1074/jbc.271.13.7725;
RA Kitaura M., Nakajima T., Imai T., Harada S., Combadiere C., Tiffany H.L.,
RA Murphy P.M., Yoshie O.;
RT "Molecular cloning of human eotaxin, an eosinophil-selective CC chemokine,
RT and identification of a specific eosinophil eotaxin receptor, CC chemokine
RT receptor 3.";
RL J. Biol. Chem. 271:7725-7730(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-65 AND 75-88, AND
RP VARIANTS.
RC TISSUE=Foreskin;
RX PubMed=8780731; DOI=10.1006/bbrc.1996.1292;
RA Bartels J., Schlueter C., Richter E., Noso N., Kulke R., Christophers E.,
RA Schroeder J.-M.;
RT "Human dermal fibroblasts express eotaxin: molecular cloning, mRNA
RT expression, and identification of eotaxin sequence variants.";
RL Biochem. Biophys. Res. Commun. 225:1045-1051(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Lung;
RX PubMed=9299399; DOI=10.1006/bbrc.1997.7169;
RA Hein H., Schlueter C., Kulke R., Christophers E., Schroeder J.-M.,
RA Bartels J.;
RT "Genomic organization, sequence, and transcriptional regulation of the
RT human eotaxin gene.";
RL Biochem. Biophys. Res. Commun. 237:537-542(1997).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 [8]
RP GLYCOSYLATION AT THR-94.
RC TISSUE=Blood;
RX PubMed=9578468; DOI=10.1046/j.1432-1327.1998.2530114.x;
RA Noso N., Bartels J., Mallet A.I., Mochizuki M., Christophers E.,
RA Schroeder J.-M.;
RT "Delayed production of biologically active O-glycosylated forms of human
RT eotaxin by tumor-necrosis-factor-alpha-stimulated dermal fibroblasts.";
RL Eur. J. Biochem. 253:114-122(1998).
RN [9]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=9712872; DOI=10.1074/jbc.273.35.22471;
RA Crump M.P., Rajarathnam K., Kim K.S., Clark-Lewis I., Sykes B.D.;
RT "Solution structure of eotaxin, a chemokine that selectively recruits
RT eosinophils in allergic inflammation.";
RL J. Biol. Chem. 273:22471-22479(1998).
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 (PubMed:8597956). Binds to CCR3
CC (PubMed:8631813). {ECO:0000269|PubMed:8597956,
CC ECO:0000269|PubMed:8631813}.
CC -!- INTERACTION:
CC P51671; Q9Y4X3: CCL27; NbExp=2; IntAct=EBI-727357, EBI-16744026;
CC P51671; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-727357, EBI-7783254;
CC P51671; P13501: CCL5; NbExp=2; IntAct=EBI-727357, EBI-2848366;
CC P51671; P51677: CCR3; NbExp=2; IntAct=EBI-727357, EBI-6625120;
CC P51671; P02778: CXCL10; NbExp=2; IntAct=EBI-727357, EBI-7815386;
CC P51671; P48061: CXCL12; NbExp=2; IntAct=EBI-727357, EBI-3913254;
CC P51671; P27487: DPP4; NbExp=2; IntAct=EBI-727357, EBI-2871277;
CC P51671; P02776: PF4; NbExp=2; IntAct=EBI-727357, EBI-2565740;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:8597956}.
CC -!- INDUCTION: Induced by TNF, IL1A/interleukin-1 alpha and IFNG/IFN-gamma.
CC {ECO:0000269|PubMed:8597956}.
CC -!- PTM: O-linked glycan consists of a Gal-GalNAc disaccharide which is
CC modified with up to 2 sialic acid residues.
CC {ECO:0000269|PubMed:9578468}.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL11 entry;
CC URL="https://en.wikipedia.org/wiki/CCL11";
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DR EMBL; U46573; AAA98957.1; -; mRNA.
DR EMBL; U34780; AAC50369.1; -; Genomic_DNA.
DR EMBL; D49372; BAA08370.1; -; mRNA.
DR EMBL; Z69291; CAA93258.1; -; mRNA.
DR EMBL; Z75668; CAA99997.1; -; mRNA.
DR EMBL; Z75669; CAA99998.1; -; mRNA.
DR EMBL; U46572; AAC51297.1; -; Genomic_DNA.
DR EMBL; Z92709; CAB07027.1; -; Genomic_DNA.
DR EMBL; BC017850; AAH17850.1; -; mRNA.
DR CCDS; CCDS11279.1; -.
DR PIR; JC4912; JC4912.
DR RefSeq; NP_002977.1; NM_002986.2.
DR PDB; 1EOT; NMR; -; A=24-97.
DR PDB; 2EOT; NMR; -; A=24-97.
DR PDB; 2MPM; NMR; -; A=24-97.
DR PDBsum; 1EOT; -.
DR PDBsum; 2EOT; -.
DR PDBsum; 2MPM; -.
DR AlphaFoldDB; P51671; -.
DR BMRB; P51671; -.
DR SMR; P51671; -.
DR BioGRID; 112259; 28.
DR DIP; DIP-5858N; -.
DR IntAct; P51671; 28.
DR MINT; P51671; -.
DR STRING; 9606.ENSP00000302234; -.
DR BindingDB; P51671; -.
DR ChEMBL; CHEMBL3286077; -.
DR DrugBank; DB05429; CAT-213.
DR GlyGen; P51671; 1 site.
DR iPTMnet; P51671; -.
DR PhosphoSitePlus; P51671; -.
DR BioMuta; CCL11; -.
DR DMDM; 1706661; -.
DR MassIVE; P51671; -.
DR PaxDb; P51671; -.
DR PeptideAtlas; P51671; -.
DR PRIDE; P51671; -.
DR ABCD; P51671; 3 sequenced antibodies.
DR Antibodypedia; 15485; 400 antibodies from 43 providers.
DR DNASU; 6356; -.
DR Ensembl; ENST00000305869.4; ENSP00000302234.3; ENSG00000172156.4.
DR GeneID; 6356; -.
DR KEGG; hsa:6356; -.
DR MANE-Select; ENST00000305869.4; ENSP00000302234.3; NM_002986.3; NP_002977.1.
DR CTD; 6356; -.
DR DisGeNET; 6356; -.
DR GeneCards; CCL11; -.
DR HGNC; HGNC:10610; CCL11.
DR HPA; ENSG00000172156; Tissue enhanced (intestine, lymphoid tissue, stomach, urinary bladder).
DR MalaCards; CCL11; -.
DR MIM; 601156; gene.
DR neXtProt; NX_P51671; -.
DR OpenTargets; ENSG00000172156; -.
DR PharmGKB; PA35543; -.
DR VEuPathDB; HostDB:ENSG00000172156; -.
DR eggNOG; ENOG502S8M4; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_1_0_1; -.
DR InParanoid; P51671; -.
DR OMA; CFTLANR; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P51671; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P51671; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR SignaLink; P51671; -.
DR SIGNOR; P51671; -.
DR BioGRID-ORCS; 6356; 11 hits in 1059 CRISPR screens.
DR ChiTaRS; CCL11; human.
DR EvolutionaryTrace; P51671; -.
DR GeneWiki; CCL11; -.
DR GenomeRNAi; 6356; -.
DR Pharos; P51671; Tbio.
DR PRO; PR:P51671; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P51671; protein.
DR Bgee; ENSG00000172156; Expressed in pylorus and 87 other tissues.
DR ExpressionAtlas; P51671; baseline and differential.
DR Genevisible; P51671; HS.
DR GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0031728; F:CCR3 chemokine receptor binding; IDA:CAFA.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IDA:CAFA.
DR GO; GO:0048018; F:receptor ligand activity; IDA:CAFA.
DR GO; GO:0007015; P:actin filament organization; IEA:Ensembl.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; TAS:ProtInc.
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:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0002544; P:chronic inflammatory response; IEA:Ensembl.
DR GO; GO:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0070371; P:ERK1 and ERK2 cascade; IEA:Ensembl.
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:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0007611; P:learning or memory; ISS:ARUK-UCL.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0060763; P:mammary duct terminal end bud growth; IEA:Ensembl.
DR GO; GO:0002551; P:mast cell chemotaxis; IEA:Ensembl.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0050768; P:negative regulation of neurogenesis; ISS:ARUK-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IDA:BHF-UCL.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
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; IDA:BHF-UCL.
DR GO; GO:0006468; P:protein phosphorylation; TAS:ProtInc.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0035962; P:response to interleukin-13; IEA:Ensembl.
DR GO; GO:0070670; P:response to interleukin-4; IEA:Ensembl.
DR GO; GO:0009314; P:response to radiation; TAS:ProtInc.
DR GO; GO:0009615; P:response to virus; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR DisProt; DP00641; -.
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 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Glycoprotein; Inflammatory response; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..97
FT /note="Eotaxin"
FT /id="PRO_0000005195"
FT CARBOHYD 94
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:9578468"
FT DISULFID 32..57
FT /evidence="ECO:0000269|PubMed:9712872"
FT DISULFID 33..73
FT /evidence="ECO:0000269|PubMed:9712872"
FT VARIANT 7
FT /note="L -> P"
FT /id="VAR_001634"
FT VARIANT 23
FT /note="A -> T (in dbSNP:rs1129844)"
FT /id="VAR_001635"
FT VARIANT 51
FT /note="R -> S"
FT /id="VAR_001636"
FT VARIANT 79
FT /note="K -> R"
FT /id="VAR_001637"
FT VARIANT 86
FT /note="K -> T (in dbSNP:rs34262946)"
FT /id="VAR_048705"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1EOT"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:2MPM"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:1EOT"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1EOT"
FT STRAND 61..66
FT /evidence="ECO:0007829|PDB:1EOT"
FT STRAND 67..70
FT /evidence="ECO:0007829|PDB:2MPM"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1EOT"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:1EOT"
SQ SEQUENCE 97 AA; 10732 MW; B433C30FDA4C71A7 CRC64;
MKVSAALLWL LLIAAAFSPQ GLAGPASVPT TCCFNLANRK IPLQRLESYR RITSGKCPQK
AVIFKTKLAK DICADPKKKW VQDSMKYLDQ KSPTPKP
