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O00175 (CCL24_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C-C motif chemokine 24
Alternative name(s):
CK-beta-6
Eosinophil chemotactic protein 2
Eotaxin-2
Myeloid progenitor inhibitory factor 2
Short name=MPIF-2
Small-inducible cytokine A24
Gene names
Name:CCL24
Synonyms:MPIF2, SCYA24
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length119 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chemotactic for resting T-lymphocytes, and eosinophils. Has lower chemotactic activity for neutrophils but none for monocytes and activated lymphocytes. Is a strong suppressor of colony formation by a multipotential hematopoietic progenitor cell line. Binds to CCR3.

Subcellular location

Secreted.

Tissue specificity

Activated monocytes and activated T lymphocytes.

Post-translational modification

N-glycosylated.

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_processcell-cell signaling

Traceable author statement Ref.1. Source: ProtInc

chemotaxis

Traceable author statement Ref.1. Source: ProtInc

cytoskeleton organization

Inferred from direct assay PubMed 10072545. Source: UniProtKB

eosinophil chemotaxis

Inferred from direct assay PubMed 10072545. Source: UniProtKB

immune response

Traceable author statement PubMed 10713092. Source: ProtInc

inflammatory response

Traceable author statement Ref.1. Source: ProtInc

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

positive regulation of eosinophil migration

Inferred from electronic annotation. Source: Ensembl

positive regulation of inflammatory response

Inferred from electronic annotation. Source: Ensembl

regulation of cell shape

Inferred from direct assay PubMed 10072545. Source: UniProtKB

signal transduction

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentextracellular space

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionchemokine activity

Inferred from direct assay PubMed 10072545. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1 Ref.2 Ref.7
Chain27 – 11993C-C motif chemokine 24
PRO_0000005232

Amino acid modifications

Glycosylation1151N-linked (GlcNAc...)
Disulfide bond33 ↔ 58
Disulfide bond34 ↔ 74

Natural variations

Natural variant291I → L. Ref.3
Corresponds to variant rs2302006 [ dbSNP | Ensembl ].
VAR_018404
Natural variant311S → F.
Corresponds to variant rs11465293 [ dbSNP | Ensembl ].
VAR_048710
Natural variant1021A → T.
Corresponds to variant rs11465312 [ dbSNP | Ensembl ].
VAR_048711
Natural variant1101Q → E.
Corresponds to variant rs11465313 [ dbSNP | Ensembl ].
VAR_048712

Experimental info

Sequence conflict611A → G in AAB51135. Ref.1
Sequence conflict731F → S AA sequence Ref.1

Secondary structure

.............. 119
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00175 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 6CAACA61731FB393

FASTA11913,134
        10         20         30         40         50         60 
MAGLMTIVTS LLFLGVCAHH IIPTGSVVIP SPCCMFFVSK RIPENRVVSY QLSSRSTCLK 

        70         80         90        100        110 
AGVIFTTKKG QQFCGDPKQE WVQRYMKNLD AKQKKASPRA RAVAVKGPVQ RYPGNQTTC 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and functional characterization of two novel human C-C chemokines as inhibitors of two distinct classes of myeloid progenitors."
Patel V.P., Kreider B.L., Li Y., Li H., Leung K., Salcedo T., Nardelli B., Pippalla V., Gentz S., Thotakura R., Parmelee D., Gentz R., Garotta G.
J. Exp. Med. 185:1163-1172(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-41 AND 73.
Tissue: Monocyte.
[2]"Cloning and functional characterization of a novel human CC chemokine that binds to the CCR3 receptor and activates human eosinophils."
White J.R., Imburgia C., Dul E., Appelbaum E., O'Donnell K., O'Shannessy D.J., Brawner M., Fornwald J., Adamou J., Elshourbagy N.A., Kaiser K., Foley J.J., Schmidt D.B., Johanson K., Macphee C., Moores K., McNulty D., Scott G.F., Schleimer R.P., Sarau H.M.
J. Leukoc. Biol. 62:667-675(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS.
Tissue: Monocyte.
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-29.
Tissue: Colon.
[4]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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].
[6]"cDNA, genomic organisation and chromosomal location of the MPIF-2 (eotaxin-2) gene."
Hein H., Theran L.
Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-117.
[7]"Signal peptide prediction based on analysis of experimentally verified cleavage sites."
Zhang Z., Henzel W.J.
Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 27-41.
[8]"NMR solution structure and receptor peptide binding of the CC chemokine eotaxin-2."
Mayer K.L., Stone M.J.
Biochemistry 39:8382-8395(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
+Additional computationally mapped references.

Web resources

Wikipedia

CCL24 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U85768 mRNA. Translation: AAB51135.1.
AK312216 mRNA. Translation: BAG35149.1.
AC005102 Genomic DNA. Translation: AAD15410.1.
BC069072 mRNA. Translation: AAH69072.1.
BC069391 mRNA. Translation: AAH69391.1.
AJ223461 mRNA. Translation: CAA11383.1.
RefSeqNP_002982.2. NM_002991.2.
UniGeneHs.247838.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1EIGNMR-A27-99[»]
1EIHNMR-A27-99[»]
ProteinModelPortalO00175.
SMRO00175. Positions 27-99.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-5876N.
MINTMINT-105313.
STRING9606.ENSP00000222902.

Proteomic databases

PaxDbO00175.
PRIDEO00175.

Protocols and materials databases

DNASU6369.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222902; ENSP00000222902; ENSG00000106178.
ENST00000416943; ENSP00000400533; ENSG00000106178.
ENST00000573227; ENSP00000461512; ENSG00000262306.
ENST00000576649; ENSP00000461415; ENSG00000262306.
GeneID6369.
KEGGhsa:6369.
UCSCuc011kga.2. human.

Organism-specific databases

CTD6369.
GeneCardsGC07M075440.
HGNCHGNC:10623. CCL24.
MIM602495. gene.
neXtProtNX_O00175.
PharmGKBPA35555.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG41621.
HOGENOMHOG000036685.
HOVERGENHBG017871.
InParanoidO00175.
KOK05514.
OMAFCGDPKQ.
OrthoDBEOG73BVG4.
PhylomeDBO00175.
TreeFamTF334888.

Gene expression databases

BgeeO00175.
CleanExHS_CCL24.
GenevestigatorO00175.

Family and domain databases

InterProIPR001811. Chemokine_IL8-like_dom.
[Graphical view]
PfamPF00048. IL8. 1 hit.
[Graphical view]
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO00175.
GenomeRNAi6369.
NextBio24748.
PMAP-CutDBO00175.
PROO00175.
SOURCESearch...

Entry information

Entry nameCCL24_HUMAN
AccessionPrimary (citable) accession number: O00175
Secondary accession number(s): B2R5K2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 30, 2000
Last modified: April 16, 2014
This is version 131 of the entry and version 2 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 7

Human chromosome 7: entries, gene names and cross-references to MIM