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Protein

Eotaxin

Gene

CCL11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  1. chemokine activity Source: UniProtKB

GO - Biological processi

  1. actin filament organization Source: Ensembl
  2. branching involved in mammary gland duct morphogenesis Source: Ensembl
  3. cell adhesion Source: ProtInc
  4. cellular calcium ion homeostasis Source: ProtInc
  5. chemotaxis Source: ProtInc
  6. chronic inflammatory response Source: Ensembl
  7. cytoskeleton organization Source: UniProtKB
  8. eosinophil chemotaxis Source: UniProtKB
  9. ERK1 and ERK2 cascade Source: Ensembl
  10. immune response Source: InterPro
  11. inflammatory response Source: ProtInc
  12. mammary duct terminal end bud growth Source: Ensembl
  13. mast cell chemotaxis Source: Ensembl
  14. positive regulation of actin filament polymerization Source: BHF-UCL
  15. positive regulation of angiogenesis Source: Ensembl
  16. positive regulation of cell migration Source: BHF-UCL
  17. positive regulation of endothelial cell proliferation Source: BHF-UCL
  18. positive regulation of Rac GTPase activity Source: BHF-UCL
  19. protein phosphorylation Source: ProtInc
  20. regulation of cell shape Source: UniProtKB
  21. response to interleukin-4 Source: Ensembl
  22. response to radiation Source: ProtInc
  23. response to virus Source: ProtInc
  24. signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Cytokine

Keywords - Biological processi

Chemotaxis, Inflammatory response

Enzyme and pathway databases

ReactomeiREACT_15344. Chemokine receptors bind chemokines.

Names & Taxonomyi

Protein namesi
Recommended name:
Eotaxin
Alternative name(s):
C-C motif chemokine 11
Eosinophil chemotactic protein
Small-inducible cytokine A11
Gene namesi
Name:CCL11
Synonyms:SCYA11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:10610. CCL11.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: BHF-UCL
  2. extracellular space Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA35543.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Add
BLAST
Chaini24 – 9774EotaxinPRO_0000005195Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi32 ↔ 57
Disulfide bondi33 ↔ 73
Glycosylationi94 – 941O-linked (GalNAc...)1 Publication

Post-translational modificationi

O-linked glycan consists of a Gal-GalNAc disaccharide which is mofified with up to 2 sialic acid residues.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP51671.
PRIDEiP51671.

PTM databases

PhosphoSiteiP51671.

Miscellaneous databases

PMAP-CutDBP51671.

Expressioni

Inductioni

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

Gene expression databases

BgeeiP51671.
CleanExiHS_CCL11.
ExpressionAtlasiP51671. baseline and differential.
GenevestigatoriP51671.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCR3P516772EBI-727357,EBI-6625120
DPP4P274872EBI-727357,EBI-2871277

Protein-protein interaction databases

BioGridi112259. 3 interactions.
DIPiDIP-5858N.
IntActiP51671. 4 interactions.
MINTiMINT-103325.
STRINGi9606.ENSP00000302234.

Structurei

Secondary structure

1
97
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi26 – 294Combined sources
Turni43 – 453Combined sources
Beta strandi46 – 527Combined sources
Beta strandi55 – 595Combined sources
Beta strandi61 – 666Combined sources
Beta strandi67 – 704Combined sources
Beta strandi71 – 744Combined sources
Helixi79 – 9113Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EOTNMR-A24-97[»]
2EOTNMR-A24-97[»]
2MPMNMR-A24-97[»]
DisProtiDP00641.
ProteinModelPortaliP51671.
SMRiP51671. Positions 24-97.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP51671.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG46290.
HOGENOMiHOG000036686.
HOVERGENiHBG017871.
InParanoidiP51671.
KOiK16597.
OMAiGSKCPQK.
OrthoDBiEOG7C5MC2.
PhylomeDBiP51671.
TreeFamiTF334888.

Family and domain databases

InterProiIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P51671-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKVSAALLWL LLIAAAFSPQ GLAGPASVPT TCCFNLANRK IPLQRLESYR
60 70 80 90
RITSGKCPQK AVIFKTKLAK DICADPKKKW VQDSMKYLDQ KSPTPKP
Length:97
Mass (Da):10,732
Last modified:October 1, 1996 - v1
Checksum:iB433C30FDA4C71A7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71L → P in clone 34.
VAR_001634
Natural varianti23 – 231A → T in clone 53.
Corresponds to variant rs1129844 [ dbSNP | Ensembl ].
VAR_001635
Natural varianti51 – 511R → S in clone 34.
VAR_001636
Natural varianti79 – 791K → R in clone 53.
VAR_001637
Natural varianti86 – 861K → T.
Corresponds to variant rs34262946 [ dbSNP | Ensembl ].
VAR_048705

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11279.1.
PIRiJC4912.
RefSeqiNP_002977.1. NM_002986.2.
UniGeneiHs.54460.

Genome annotation databases

EnsembliENST00000305869; ENSP00000302234; ENSG00000172156.
GeneIDi6356.
KEGGihsa:6356.
UCSCiuc002hia.1. human.

Polymorphism databases

DMDMi1706661.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

R&D Systems' cytokine source book: CCL11
Wikipedia

CCL11 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS11279.1.
PIRiJC4912.
RefSeqiNP_002977.1. NM_002986.2.
UniGeneiHs.54460.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EOTNMR-A24-97[»]
2EOTNMR-A24-97[»]
2MPMNMR-A24-97[»]
DisProtiDP00641.
ProteinModelPortaliP51671.
SMRiP51671. Positions 24-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112259. 3 interactions.
DIPiDIP-5858N.
IntActiP51671. 4 interactions.
MINTiMINT-103325.
STRINGi9606.ENSP00000302234.

PTM databases

PhosphoSiteiP51671.

Polymorphism databases

DMDMi1706661.

Proteomic databases

PaxDbiP51671.
PRIDEiP51671.

Protocols and materials databases

DNASUi6356.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305869; ENSP00000302234; ENSG00000172156.
GeneIDi6356.
KEGGihsa:6356.
UCSCiuc002hia.1. human.

Organism-specific databases

CTDi6356.
GeneCardsiGC17P032612.
HGNCiHGNC:10610. CCL11.
MIMi601156. gene.
neXtProtiNX_P51671.
PharmGKBiPA35543.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG46290.
HOGENOMiHOG000036686.
HOVERGENiHBG017871.
InParanoidiP51671.
KOiK16597.
OMAiGSKCPQK.
OrthoDBiEOG7C5MC2.
PhylomeDBiP51671.
TreeFamiTF334888.

Enzyme and pathway databases

ReactomeiREACT_15344. Chemokine receptors bind chemokines.

Miscellaneous databases

EvolutionaryTraceiP51671.
GeneWikiiCCL11.
GenomeRNAii6356.
NextBioi24688.
PMAP-CutDBP51671.
PROiP51671.
SOURCEiSearch...

Gene expression databases

BgeeiP51671.
CleanExiHS_CCL11.
ExpressionAtlasiP51671. baseline and differential.
GenevestigatoriP51671.

Family and domain databases

InterProiIPR000827. Chemokine_CC_CS.
IPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamiPF00048. IL8. 1 hit.
[Graphical view]
SMARTiSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMiSSF54117. SSF54117. 1 hit.
PROSITEiPS00472. SMALL_CYTOKINES_CC. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiCCL11_HUMAN
AccessioniPrimary (citable) accession number: P51671
Secondary accession number(s): P50877, Q92490, Q92491
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: March 4, 2015
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.