CCL24_HUMAN
ID CCL24_HUMAN Reviewed; 119 AA.
AC O00175; B2R5K2;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=C-C motif chemokine 24;
DE AltName: Full=CK-beta-6;
DE AltName: Full=Eosinophil chemotactic protein 2 {ECO:0000303|Ref.6};
DE Short=Eotaxin-2 {ECO:0000303|Ref.6};
DE AltName: Full=Myeloid progenitor inhibitory factor 2 {ECO:0000303|PubMed:9104803};
DE Short=MPIF-2 {ECO:0000303|PubMed:9104803};
DE AltName: Full=Small-inducible cytokine A24;
DE Flags: Precursor;
GN Name=CCL24 {ECO:0000312|HGNC:HGNC:10623};
GN Synonyms=MPIF2 {ECO:0000303|PubMed:9104803}, SCYA24;
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], PROTEIN SEQUENCE OF 27-41 AND 73, FUNCTION,
RP SUBCELLULAR LOCATION, GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Monocyte;
RX PubMed=9104803; DOI=10.1084/jem.185.7.1163;
RA Patel V.P., Kreider B.L., Li Y., Li H., Leung K., Salcedo T., Nardelli B.,
RA Pippalla V., Gentz S., Thotakura R., Parmelee D., Gentz R., Garotta G.;
RT "Molecular and functional characterization of two novel human C-C
RT chemokines as inhibitors of two distinct classes of myeloid progenitors.";
RL J. Exp. Med. 185:1163-1172(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Monocyte;
RX PubMed=9365122; DOI=10.1002/jlb.62.5.667;
RA White J.R., Imburgia C., Dul E., Appelbaum E., O'Donnell K.,
RA O'Shannessy D.J., Brawner M., Fornwald J., Adamou J., Elshourbagy N.A.,
RA Kaiser K., Foley J.J., Schmidt D.B., Johanson K., Macphee C., Moores K.,
RA McNulty D., Scott G.F., Schleimer R.P., Sarau H.M.;
RT "Cloning and functional characterization of a novel human CC chemokine that
RT binds to the CCR3 receptor and activates human eosinophils.";
RL J. Leukoc. Biol. 62:667-675(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT LEU-29.
RC TISSUE=Colon;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [MRNA] OF 3-117.
RA Hein H., Theran L.;
RT "cDNA, genomic organisation and chromosomal location of the MPIF-2
RT (eotaxin-2) gene.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP STRUCTURE BY NMR, AND DISULFIDE BONDS.
RX PubMed=10913244; DOI=10.1021/bi000523j;
RA Mayer K.L., Stone M.J.;
RT "NMR solution structure and receptor peptide binding of the CC chemokine
RT eotaxin-2.";
RL Biochemistry 39:8382-8395(2000).
CC -!- FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils
CC (PubMed:9104803, PubMed:9365122). Has lower chemotactic activity for
CC neutrophils but none for monocytes and activated lymphocytes
CC (PubMed:9104803, PubMed:9365122). Is a strong suppressor of colony
CC formation by a multipotential hematopoietic progenitor cell line
CC (PubMed:9104803, PubMed:9365122). Binds to CCR3 (PubMed:9104803,
CC PubMed:9365122). {ECO:0000269|PubMed:9104803,
CC ECO:0000269|PubMed:9365122}.
CC -!- INTERACTION:
CC O00175; P13501: CCL5; NbExp=3; IntAct=EBI-16803966, EBI-2848366;
CC O00175; O14625: CXCL11; NbExp=2; IntAct=EBI-16803966, EBI-2871971;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9104803,
CC ECO:0000269|PubMed:9365122}.
CC -!- TISSUE SPECIFICITY: Activated monocytes and activated T lymphocytes.
CC {ECO:0000269|PubMed:9104803}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:9104803}.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL24 entry;
CC URL="https://en.wikipedia.org/wiki/CCL24";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U85768; AAB51135.1; -; mRNA.
DR EMBL; AK312216; BAG35149.1; -; mRNA.
DR EMBL; AC005102; AAD15410.1; -; Genomic_DNA.
DR EMBL; BC069072; AAH69072.1; -; mRNA.
DR EMBL; BC069391; AAH69391.1; -; mRNA.
DR EMBL; AJ223461; CAA11383.1; -; mRNA.
DR CCDS; CCDS34670.1; -.
DR RefSeq; NP_002982.2; NM_002991.2.
DR RefSeq; XP_011514761.1; XM_011516459.2.
DR RefSeq; XP_011514762.1; XM_011516460.2.
DR PDB; 1EIG; NMR; -; A=27-99.
DR PDB; 1EIH; NMR; -; A=27-99.
DR PDBsum; 1EIG; -.
DR PDBsum; 1EIH; -.
DR AlphaFoldDB; O00175; -.
DR BMRB; O00175; -.
DR SMR; O00175; -.
DR BioGRID; 112272; 6.
DR DIP; DIP-5876N; -.
DR IntAct; O00175; 5.
DR STRING; 9606.ENSP00000400533; -.
DR GlyConnect; 2007; 1 N-Linked glycan (1 site).
DR GlyGen; O00175; 1 site, 1 N-linked glycan (1 site).
DR BioMuta; CCL24; -.
DR jPOST; O00175; -.
DR MassIVE; O00175; -.
DR PaxDb; O00175; -.
DR PeptideAtlas; O00175; -.
DR PRIDE; O00175; -.
DR ProteomicsDB; 47761; -.
DR Antibodypedia; 14858; 489 antibodies from 31 providers.
DR DNASU; 6369; -.
DR Ensembl; ENST00000222902.7; ENSP00000222902.2; ENSG00000106178.7.
DR Ensembl; ENST00000416943.1; ENSP00000400533.1; ENSG00000106178.7.
DR GeneID; 6369; -.
DR KEGG; hsa:6369; -.
DR MANE-Select; ENST00000222902.7; ENSP00000222902.2; NM_002991.3; NP_002982.2.
DR UCSC; uc011kga.3; human.
DR CTD; 6369; -.
DR DisGeNET; 6369; -.
DR GeneCards; CCL24; -.
DR HGNC; HGNC:10623; CCL24.
DR HPA; ENSG00000106178; Group enriched (intestine, lymphoid tissue).
DR MIM; 602495; gene.
DR neXtProt; NX_O00175; -.
DR OpenTargets; ENSG00000106178; -.
DR PharmGKB; PA35555; -.
DR VEuPathDB; HostDB:ENSG00000106178; -.
DR eggNOG; ENOG502S6ZP; Eukaryota.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_1_1_1; -.
DR InParanoid; O00175; -.
DR OMA; KLPWVQK; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; O00175; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; O00175; -.
DR SignaLink; O00175; -.
DR BioGRID-ORCS; 6369; 10 hits in 1059 CRISPR screens.
DR ChiTaRS; CCL24; human.
DR EvolutionaryTrace; O00175; -.
DR GenomeRNAi; 6369; -.
DR Pharos; O00175; Tbio.
DR PRO; PR:O00175; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; O00175; protein.
DR Bgee; ENSG00000106178; Expressed in rectum and 105 other tissues.
DR Genevisible; O00175; HS.
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:0048018; F:receptor ligand activity; IDA:CAFA.
DR GO; GO:0007267; P:cell-cell signaling; 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:0007010; P:cytoskeleton organization; IDA:UniProtKB.
DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
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:2000418; P:positive regulation of eosinophil migration; 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; IDA:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IDA:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR InterPro; IPR039809; Chemokine_b/g/d.
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.
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..26
FT /evidence="ECO:0000269|PubMed:15340161,
FT ECO:0000269|PubMed:9104803, ECO:0000269|PubMed:9365122"
FT CHAIN 27..119
FT /note="C-C motif chemokine 24"
FT /id="PRO_0000005232"
FT CARBOHYD 115
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 33..58
FT /evidence="ECO:0000269|PubMed:10913244"
FT DISULFID 34..74
FT /evidence="ECO:0000269|PubMed:10913244"
FT VARIANT 29
FT /note="I -> L (in dbSNP:rs2302006)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_018404"
FT VARIANT 31
FT /note="S -> F (in dbSNP:rs11465293)"
FT /id="VAR_048710"
FT VARIANT 102
FT /note="A -> T (in dbSNP:rs11465312)"
FT /id="VAR_048711"
FT VARIANT 110
FT /note="Q -> E (in dbSNP:rs11465313)"
FT /id="VAR_048712"
FT CONFLICT 61
FT /note="A -> G (in Ref. 1; AAB51135)"
FT /evidence="ECO:0000305"
FT CONFLICT 73
FT /note="F -> S (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 35..37
FT /evidence="ECO:0007829|PDB:1EIH"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:1EIG"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1EIG"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:1EIG"
FT STRAND 63..67
FT /evidence="ECO:0007829|PDB:1EIG"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:1EIG"
FT HELIX 80..92
FT /evidence="ECO:0007829|PDB:1EIG"
SQ SEQUENCE 119 AA; 13134 MW; 6CAACA61731FB393 CRC64;
MAGLMTIVTS LLFLGVCAHH IIPTGSVVIP SPCCMFFVSK RIPENRVVSY QLSSRSTCLK
AGVIFTTKKG QQFCGDPKQE WVQRYMKNLD AKQKKASPRA RAVAVKGPVQ RYPGNQTTC
