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P51671 (CCL11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 142. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Eotaxin
Alternative name(s):
C-C motif chemokine 11
Eosinophil chemotactic protein
Small-inducible cytokine A11
Gene names
Name:CCL11
Synonyms:SCYA11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length97 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

In response to the presence of allergens, this protein directly promotes the accumulation of eosinophils, a prominent feature of allergic inflammatory reactions. Binds to CCR3.

Subcellular location

Secreted.

Induction

By TNF, IL1A/interleukin-1 alpha and IFNG/IFN-gamma.

Post-translational modification

O-linked glycan consists of a Gal-GalNAc disaccharide which is mofified with up to 2 sialic acid residues.

Sequence similarities

Belongs to the intercrine beta (chemokine CC) family.

Ontologies

Keywords
   Biological processChemotaxis
Inflammatory response
   Cellular componentSecreted
   Coding sequence diversityPolymorphism
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processERK1 and ERK2 cascade

Inferred from electronic annotation. Source: Ensembl

actin filament organization

Inferred from electronic annotation. Source: Ensembl

branching involved in mammary gland duct morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Traceable author statement PubMed 10201960. Source: ProtInc

cellular calcium ion homeostasis

Traceable author statement PubMed 10415069. Source: ProtInc

chemotaxis

Traceable author statement PubMed 10706854. Source: ProtInc

chronic inflammatory response

Inferred from electronic annotation. Source: Ensembl

cytoskeleton organization

Inferred from direct assay PubMed 10072545. Source: UniProtKB

eosinophil chemotaxis

Inferred from direct assay PubMed 10072545. Source: UniProtKB

immune response

Inferred from electronic annotation. Source: InterPro

inflammatory response

Traceable author statement PubMed 10708591. Source: ProtInc

mammary duct terminal end bud growth

Inferred from electronic annotation. Source: Ensembl

mast cell chemotaxis

Inferred from electronic annotation. Source: Ensembl

positive regulation of Rac GTPase activity

Inferred from direct assay PubMed 19525930. Source: BHF-UCL

positive regulation of actin filament polymerization

Inferred from direct assay PubMed 19525930. Source: BHF-UCL

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell migration

Inferred from direct assay PubMed 19525930. Source: BHF-UCL

positive regulation of endothelial cell proliferation

Inferred from direct assay PubMed 19525930. Source: BHF-UCL

protein phosphorylation

Traceable author statement PubMed 10706854. Source: ProtInc

regulation of cell shape

Inferred from direct assay PubMed 10072545. Source: UniProtKB

response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

response to radiation

Traceable author statement PubMed 10708591. Source: ProtInc

response to virus

Traceable author statement PubMed 9558100. Source: ProtInc

signal transduction

Traceable author statement PubMed 10706854. Source: ProtInc

   Cellular_componentextracellular region

Inferred from direct assay PubMed 20041150. Source: BHF-UCL

extracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionchemokine activity

Inferred from direct assay PubMed 10072545. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 18275857PubMed 21314817PubMed 23597562. Source: IntAct

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323
Chain24 – 9774Eotaxin
PRO_0000005195

Amino acid modifications

Glycosylation941O-linked (GalNAc...) Ref.8
Disulfide bond32 ↔ 57
Disulfide bond33 ↔ 73

Natural variations

Natural variant71L → P in clone 34.
VAR_001634
Natural variant231A → T in clone 53.
Corresponds to variant rs1129844 [ dbSNP | Ensembl ].
VAR_001635
Natural variant511R → S in clone 34.
VAR_001636
Natural variant791K → R in clone 53.
VAR_001637
Natural variant861K → T.
Corresponds to variant rs34262946 [ dbSNP | Ensembl ].
VAR_048705

Secondary structure

............. 97
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P51671 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: B433C30FDA4C71A7

FASTA9710,732
        10         20         30         40         50         60 
MKVSAALLWL LLIAAAFSPQ GLAGPASVPT TCCFNLANRK IPLQRLESYR RITSGKCPQK 

        70         80         90 
AVIFKTKLAK DICADPKKKW VQDSMKYLDQ KSPTPKP 

« Hide

References

« Hide 'large scale' references
[1]"Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia."
Garcia-Zepeda E.A., Rothenberg M.E., Ownbey T.R., Leder P., Luster A.D.
Nat. Med. 2:449-456(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of the human eosinophil chemoattractant, eotaxin. Expression, receptor binding, and functional properties suggest a mechanism for the selective recruitment of eosinophils."
Ponath P.D., Qin S., Ringler D.J., Clark-Lewis I., Wang J., Kassam N., Smith H., Shi X., Gonzalo J.A., Newman W., Gutierrez-Ramos J.-C., Mackay C.R.
J. Clin. Invest. 97:604-612(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Molecular cloning of human eotaxin, an eosinophil-selective CC chemokine, and identification of a specific eosinophil eotaxin receptor, CC chemokine receptor 3."
Kitaura M., Nakajima T., Imai T., Harada S., Combadiere C., Tiffany H.L., Murphy P.M., Yoshie O.
J. Biol. Chem. 271:7725-7730(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Small intestine.
[4]"Human dermal fibroblasts express eotaxin: molecular cloning, mRNA expression, and identification of eotaxin sequence variants."
Bartels J., Schlueter C., Richter E., Noso N., Kulke R., Christophers E., Schroeder J.-M.
Biochem. Biophys. Res. Commun. 225:1045-1051(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 60-65 AND 75-88, VARIANTS.
Tissue: Foreskin.
[5]"Genomic organization, complete sequence, and chromosomal location of the gene for human eotaxin (SCYA11), an eosinophil-specific CC chemokine."
Garcia-Zepeda E.A., Rothenberg M.E., Weremowicz S., Sarafi M.N., Morton C.C., Luster A.D.
Genomics 41:471-476(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[6]"Genomic organization, sequence, and transcriptional regulation of the human eotaxin gene."
Hein H., Schlueter C., Kulke R., Christophers E., Schroeder J.-M., Bartels J.
Biochem. Biophys. Res. Commun. 237:537-542(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Lung.
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung.
[8]"Delayed production of biologically active O-glycosylated forms of human eotaxin by tumor-necrosis-factor-alpha-stimulated dermal fibroblasts."
Noso N., Bartels J., Mallet A.I., Mochizuki M., Christophers E., Schroeder J.-M.
Eur. J. Biochem. 253:114-122(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT THR-94.
Tissue: Blood.
[9]"Solution structure of eotaxin, a chemokine that selectively recruits eosinophils in allergic inflammation."
Crump M.P., Rajarathnam K., Kim K.S., Clark-Lewis I., Sykes B.D.
J. Biol. Chem. 273:22471-22479(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U46573 mRNA. Translation: AAA98957.1.
U34780 Genomic DNA. Translation: AAC50369.1.
D49372 mRNA. Translation: BAA08370.1.
Z69291 mRNA. Translation: CAA93258.1.
Z75668 mRNA. Translation: CAA99997.1.
Z75669 mRNA. Translation: CAA99998.1.
U46572 Genomic DNA. Translation: AAC51297.1.
Z92709 Genomic DNA. Translation: CAB07027.1.
BC017850 mRNA. Translation: AAH17850.1.
CCDSCCDS11279.1.
PIRJC4912.
RefSeqNP_002977.1. NM_002986.2.
UniGeneHs.54460.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EOTNMR-A24-97[»]
2EOTNMR-A24-97[»]
DisProtDP00641.
ProteinModelPortalP51671.
SMRP51671. Positions 24-97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112259. 3 interactions.
DIPDIP-5858N.
IntActP51671. 4 interactions.
MINTMINT-103325.
STRING9606.ENSP00000302234.

PTM databases

PhosphoSiteP51671.

Polymorphism databases

DMDM1706661.

Proteomic databases

PaxDbP51671.
PRIDEP51671.

Protocols and materials databases

DNASU6356.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000305869; ENSP00000302234; ENSG00000172156.
GeneID6356.
KEGGhsa:6356.
UCSCuc002hia.1. human.

Organism-specific databases

CTD6356.
GeneCardsGC17P032612.
HGNCHGNC:10610. CCL11.
MIM601156. gene.
neXtProtNX_P51671.
PharmGKBPA35543.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46290.
HOGENOMHOG000036686.
HOVERGENHBG017871.
InParanoidP51671.
KOK16597.
OMAQSYRRIT.
OrthoDBEOG7C5MC2.
PhylomeDBP51671.
TreeFamTF334888.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressP51671.
BgeeP51671.
CleanExHS_CCL11.
GenevestigatorP51671.

Family and domain databases

InterProIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamPF00048. IL8. 1 hit.
[Graphical view]
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
PROSITEPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51671.
GeneWikiCCL11.
GenomeRNAi6356.
NextBio24688.
PMAP-CutDBP51671.
PROP51671.
SOURCESearch...

Entry information

Entry nameCCL11_HUMAN
AccessionPrimary (citable) accession number: P51671
Secondary accession number(s): P50877, Q92490, Q92491
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM