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 13-FEB-2019, entry version 161. DE RecName: Full=C-C motif chemokine 24; DE AltName: Full=CK-beta-6; DE AltName: Full=Eosinophil chemotactic protein 2; DE AltName: Full=Eotaxin-2; DE AltName: Full=Myeloid progenitor inhibitory factor 2; DE Short=MPIF-2; DE AltName: Full=Small-inducible cytokine A24; DE Flags: Precursor; GN Name=CCL24; Synonyms=MPIF2, SCYA24; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 27-41 AND 73. 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., RA Nardelli B., Pippalla V., Gentz S., Thotakura R., Parmelee D., RA 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 RT progenitors."; RL J. Exp. Med. 185:1163-1172(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF N-TERMINUS. RC TISSUE=Monocyte; RX PubMed=9365122; RA White J.R., Imburgia C., Dul E., Appelbaum E., O'Donnell K., RA O'Shannessy D.J., Brawner M., Fornwald J., Adamou J., RA Elshourbagy N.A., Kaiser K., Foley J.J., Schmidt D.B., Johanson K., RA Macphee C., Moores K., McNulty D., Scott G.F., Schleimer R.P., RA Sarau H.M.; RT "Cloning and functional characterization of a novel human CC chemokine RT that 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA 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., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., 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 RT project: 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 RT verified cleavage sites."; RL Protein Sci. 13:2819-2824(2004). RN [8] RP STRUCTURE BY NMR. 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 RT chemokine eotaxin-2."; RL Biochemistry 39:8382-8395(2000). CC -!- FUNCTION: Chemotactic for resting T-lymphocytes, and eosinophils. CC Has lower chemotactic activity for neutrophils but none for CC monocytes and activated lymphocytes. Is a strong suppressor of CC colony formation by a multipotential hematopoietic progenitor cell CC line. Binds to CCR3. CC -!- INTERACTION: CC P13501:CCL5; NbExp=3; IntAct=EBI-16803966, EBI-2848366; CC O14625:CXCL11; NbExp=2; IntAct=EBI-16803966, EBI-2871971; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- TISSUE SPECIFICITY: Activated monocytes and activated T CC lymphocytes. CC -!- PTM: N-glycosylated. 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 UniGene; Hs.247838; -. DR PDB; 1EIG; NMR; -; A=27-99. DR PDB; 1EIH; NMR; -; A=27-99. DR PDBsum; 1EIG; -. DR PDBsum; 1EIH; -. DR ProteinModelPortal; O00175; -. DR SMR; O00175; -. DR DIP; DIP-5876N; -. DR IntAct; O00175; 5. DR STRING; 9606.ENSP00000222902; -. DR BioMuta; CCL24; -. DR jPOST; O00175; -. DR PaxDb; O00175; -. DR PeptideAtlas; O00175; -. DR PRIDE; O00175; -. DR ProteomicsDB; 47761; -. DR DNASU; 6369; -. DR Ensembl; ENST00000222902; ENSP00000222902; ENSG00000106178. DR Ensembl; ENST00000416943; ENSP00000400533; ENSG00000106178. DR GeneID; 6369; -. DR KEGG; hsa:6369; -. DR UCSC; uc011kga.3; human. DR CTD; 6369; -. DR DisGeNET; 6369; -. DR EuPathDB; HostDB:ENSG00000106178.6; -. DR GeneCards; CCL24; -. DR HGNC; HGNC:10623; CCL24. DR MIM; 602495; gene. DR neXtProt; NX_O00175; -. DR OpenTargets; ENSG00000106178; -. DR PharmGKB; PA35555; -. DR eggNOG; ENOG410JCGF; Eukaryota. DR eggNOG; ENOG41119KC; LUCA. DR GeneTree; ENSGT00940000153494; -. DR HOGENOM; HOG000036685; -. DR HOVERGEN; HBG017871; -. DR InParanoid; O00175; -. DR KO; K21097; -. DR OMA; GQKFCGD; -. DR OrthoDB; 1575018at2759; -. DR PhylomeDB; O00175; -. DR TreeFam; TF334888; -. DR EvolutionaryTrace; O00175; -. DR GenomeRNAi; 6369; -. DR PMAP-CutDB; O00175; -. DR PRO; PR:O00175; -. DR Proteomes; UP000005640; Chromosome 7. DR Bgee; ENSG00000106178; Expressed in 78 organ(s), highest expression level in spleen. 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; Complete proteome; Cytokine; KW Direct protein sequencing; Disulfide bond; Glycoprotein; KW Inflammatory response; Polymorphism; Reference proteome; Secreted; KW Signal. FT SIGNAL 1 26 {ECO:0000269|PubMed:15340161, FT ECO:0000269|PubMed:9104803, FT ECO:0000269|PubMed:9365122}. FT CHAIN 27 119 C-C motif chemokine 24. FT /FTId=PRO_0000005232. FT CARBOHYD 115 115 N-linked (GlcNAc...) asparagine. FT DISULFID 33 58 FT DISULFID 34 74 FT VARIANT 29 29 I -> L (in dbSNP:rs2302006). FT {ECO:0000269|PubMed:14702039}. FT /FTId=VAR_018404. FT VARIANT 31 31 S -> F (in dbSNP:rs11465293). FT /FTId=VAR_048710. FT VARIANT 102 102 A -> T (in dbSNP:rs11465312). FT /FTId=VAR_048711. FT VARIANT 110 110 Q -> E (in dbSNP:rs11465313). FT /FTId=VAR_048712. FT CONFLICT 61 61 A -> G (in Ref. 1; AAB51135). FT {ECO:0000305}. FT CONFLICT 73 73 F -> S (in Ref. 1; AA sequence). FT {ECO:0000305}. FT STRAND 35 37 {ECO:0000244|PDB:1EIH}. FT TURN 44 46 {ECO:0000244|PDB:1EIG}. FT STRAND 47 52 {ECO:0000244|PDB:1EIG}. FT STRAND 56 60 {ECO:0000244|PDB:1EIG}. FT STRAND 63 67 {ECO:0000244|PDB:1EIG}. FT STRAND 73 75 {ECO:0000244|PDB:1EIG}. FT HELIX 80 92 {ECO:0000244|PDB:1EIG}. SQ SEQUENCE 119 AA; 13134 MW; 6CAACA61731FB393 CRC64; MAGLMTIVTS LLFLGVCAHH IIPTGSVVIP SPCCMFFVSK RIPENRVVSY QLSSRSTCLK AGVIFTTKKG QQFCGDPKQE WVQRYMKNLD AKQKKASPRA RAVAVKGPVQ RYPGNQTTC //