ID CCL23_HUMAN Reviewed; 120 AA. AC P55773; B7ZKQ3; O00174; O75950; Q52LD4; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-FEB-2022, sequence version 4. DT 04-NOV-2026, entry version 204. DE RecName: Full=C-C motif chemokine 23; DE AltName: Full=CK-beta-8; DE Short=CKB-8; DE AltName: Full=Macrophage inflammatory protein 3; DE Short=MIP-3; DE AltName: Full=Myeloid progenitor inhibitory factor 1; DE Short=MPIF-1; DE AltName: Full=Small-inducible cytokine A23; DE Contains: DE RecName: Full=CCL23(19-99); DE Contains: DE RecName: Full=CCL23(22-99); DE Contains: DE RecName: Full=CCL23(27-99); DE Contains: DE RecName: Full=CCL23(30-99); DE Flags: Precursor; GN Name=CCL23; Synonyms=MIP3, MPIF1, SCYA23; 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]. RA Li H., Ruben S.; RT "Macrophage inflammatory protein-3 and -4."; RL Patent number US5504003, 02-APR-1996. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT), AND PROTEIN SEQUENCE OF 22-36. RC TISSUE=Aortic endothelium; 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS SHORT AND LONG), AND ALTERNATIVE RP SPLICING. RC TISSUE=Monocyte; RX PubMed=9558365; DOI=10.1182/blood.v91.9.3118.3118_3118_3126; RA Youn B.-S., Zhang S.M., Broxmeyer H.E., Cooper S., Antol K., Fraser M. Jr., RA Kwon B.S.; RT "Characterization of CKbeta8 and CKbeta8-1: two alternatively spliced forms RT of human beta-chemokine, chemoattractants for neutrophils, monocytes, and RT lymphocytes, and potent agonists at CC chemokine receptor 1."; RL Blood 91:3118-3126(1998). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING. RX PubMed=10213461; DOI=10.1089/107999099314153; RA Nomiyama H., Fukuda S., Iio M., Tanase S., Miura R., Yoshie O.; RT "Organization of the chemokine gene cluster on human chromosome 17q11.2 RT containing the genes for CC chemokine MPIF-1, HCC-2, LEC, and RANTES."; RL J. Interferon Cytokine Res. 19:227-234(1999). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS LONG AND SHORT). RC TISSUE=Liver; 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 [8] RP DISCUSSION OF SEQUENCE. RX PubMed=9129202; DOI=10.1002/jlb.61.5.545; RA Wells T.N.C., Peitsch M.C.; RT "The chemokine information source: identification and characterization of RT novel chemokines using the WorldWideWeb and expressed sequence tag RT databases."; RL J. Leukoc. Biol. 61:545-550(1997). RN [9] RP IDENTIFICATION OF CCL23(19-99); CCL23(22-99); CCL23(27-99) AND RP CCL23(30-99), PROTEOLYTIC PROCESSING OF N-TERMINUS, TISSUE SPECIFICITY, AND RP FUNCTION. RX PubMed=15905581; DOI=10.4049/jimmunol.174.11.7341; RA Berahovich R.D., Miao Z., Wang Y., Premack B., Howard M.C., Schall T.J.; RT "Proteolytic activation of alternative CCR1 ligands in inflammation."; RL J. Immunol. 174:7341-7351(2005). RN [10] RP STRUCTURE BY NMR OF 45-120, AND DISULFIDE BOND. RX PubMed=11060285; DOI=10.1074/jbc.m005085200; RA Rajarathnam K., Li Y., Rohrer T., Gentz R.; RT "Solution structure and dynamics of myeloid progenitor inhibitory factor-1 RT (MPIF-1), a novel monomeric CC chemokine."; RL J. Biol. Chem. 276:4909-4916(2001). CC -!- FUNCTION: Shows chemotactic activity for monocytes, resting T- CC lymphocytes, and neutrophils, but not for activated lymphocytes. CC Inhibits proliferation of myeloid progenitor cells in colony formation CC assays. This protein can bind heparin. Binds CCR1. CCL23(19-99), CC CCL23(22-99), CCL23(27-99), CCL23(30-99) are more potent CC chemoattractants than CCL23. {ECO:0000269|PubMed:15905581}. CC -!- INTERACTION: CC P55773; P14735: IDE; NbExp=2; IntAct=EBI-16805602, EBI-2556886; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=Short; Synonyms=CKB-8; CC IsoId=P55773-1; Sequence=Displayed; CC Name=Long; Synonyms=CKB-8-1; CC IsoId=P55773-2; Sequence=VSP_001063; CC -!- TISSUE SPECIFICITY: High levels in adult lung, liver, skeletal muscle CC and pancreas. Moderate levels in fetal liver, adult bone marrow and CC placenta. The short form is the major species and the longer form was CC detected only in very low abundance. CCL23(19-99), CCL23(22-99), CC CCL23(27-99), CCL23(30-99) are found in high levels in synovial fluids CC from rheumatoid patients. {ECO:0000269|PubMed:15905581}. CC -!- PTM: The N-terminal is proteolytically cleaved by proteases associated CC with inflammatory responses. The processed forms, CCL23(19-99), CC CCL23(22-99), CCL23(27-99) and CCL23(30-99) exhibit increase in CCR1- CC mediated signaling and chemotaxis assays in vitro. CC {ECO:0000269|PubMed:15905581}. CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL23 entry; CC URL="https://en.wikipedia.org/wiki/CCL23"; 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; U85767; AAB51134.1; -; mRNA. DR EMBL; U58913; AAD10846.1; -; mRNA. DR EMBL; U67128; AAD00161.1; -; mRNA. DR EMBL; AF088219; AAC63326.1; -; Genomic_DNA. DR EMBL; AF088219; AAC63327.1; -; Genomic_DNA. DR EMBL; AC244100; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471147; EAW80103.1; -; Genomic_DNA. DR EMBL; BC093970; AAH93970.1; -; mRNA. DR EMBL; BC143310; AAI43311.1; -; mRNA. DR CCDS; CCDS11305.1; -. [P55773-2] DR CCDS; CCDS59282.1; -. [P55773-1] DR RefSeq; NP_005055.3; NM_005064.6. [P55773-2] DR RefSeq; NP_665905.2; NM_145898.4. [P55773-1] DR PDB; 1G91; NMR; -; A=44-120. DR AlphaFoldDB; P55773; -. DR SMR; P55773; -. DR BioGRID; 112271; 4. DR FunCoup; P55773; 608. DR IntAct; P55773; 2. DR NDEx; IQUERY-CP-CCL23; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000481357; -. DR PhosphoSitePlus; P55773; -. DR BioMuta; CCL23; -. DR DMDM; 308153623; -. DR MassIVE; P55773; -. DR PaxDb; 9606-ENSP00000481357; -. DR PeptideAtlas; P55773; -. DR ProteomicsDB; 56861; -. [P55773-1] DR ProteomicsDB; 56862; -. [P55773-2] DR Antibodypedia; 73206; 377 antibodies from 36 providers. DR DNASU; 6368; -. DR Ensembl; ENST00000610342.2; ENSP00000483546.1; ENSG00000276114.2. DR Ensembl; ENST00000612516.4; ENSP00000484748.1; ENSG00000274736.5. [P55773-1] DR Ensembl; ENST00000615050.2; ENSP00000481357.1; ENSG00000274736.5. [P55773-2] DR Ensembl; ENST00000632633.1; ENSP00000488270.1; ENSG00000276114.2. DR GeneID; 6368; -. DR KEGG; hsa:6368; -. DR MANE-Select; ENST00000615050.2; ENSP00000481357.1; NM_005064.6; NP_005055.3. [P55773-2] DR UCSC; uc002hks.3; human. [P55773-1] DR AGR; HGNC:10622; -. DR ClinPGx; PA35554; -. DR CTD; 6368; -. DR DisGeNET; 6368; -. DR GeneCards; CCL23; -. DR HGNC; HGNC:10622; CCL23. DR HPA; ENSG00000274736; Low tissue specificity. DR MIM; 602494; gene. DR OpenTargets; ENSG00000274736; -. DR VEuPathDB; HostDB:ENSG00000274736; -. DR GeneTree; ENSGT01100000263482; -. DR HOGENOM; CLU_141716_4_1_1; -. DR InParanoid; P55773; -. DR OrthoDB; 9447832at2759; -. DR PAN-GO; P55773; 8 GO annotations based on evolutionary models. DR PhylomeDB; P55773; -. DR PathwayCommons; P55773; -. DR Reactome; R-HSA-416476; G alpha (q) signalling events. [P55773-2] DR Reactome; R-HSA-418594; G alpha (i) signalling events. [P55773-2] DR Reactome; R-HSA-444473; Formyl peptide receptors bind formyl peptides and many other ligands. [P55773-2] DR SignaLink; P55773; -. DR Agora; ENSG00000274736; -. DR BioGRID-ORCS; 6368; 13 hits in 1136 CRISPR screens. DR EvolutionaryTrace; P55773; -. DR GenomeRNAi; 6368; -. DR Pharos; P55773; Tbio. DR PRO; PR:P55773; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; P55773; protein. DR Bgee; ENSG00000274736; Expressed in male germ line stem cell (sensu Vertebrata) in testis and 85 other cell types or tissues. DR ExpressionAtlas; P55773; baseline and differential. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central. DR GO; GO:0031726; F:CCR1 chemokine receptor binding; IPI:UniProtKB. DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IBA:GO_Central. DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central. DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc. DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central. DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc. DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:ProtInc. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0006874; P:intracellular calcium ion homeostasis; TAS:ProtInc. DR GO; GO:0002548; P:monocyte chemotaxis; IC:UniProtKB. DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc. DR GO; GO:0030335; P:positive regulation of cell migration; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; NAS:ProtInc. DR CDD; cd00272; Chemokine_CC; 1. DR FunFam; 2.40.50.40:FF:000002; C-C motif chemokine; 1. DR Gene3D; 2.40.50.40; -; 1. DR InterPro; IPR039809; Chemokine_b/g/d. DR InterPro; IPR000827; Chemokine_CC_CS. DR InterPro; IPR001811; Chemokine_IL8-like_dom. DR InterPro; IPR036048; Interleukin_8-like_sf. DR PANTHER; PTHR12015:SF157; C-C MOTIF CHEMOKINE 23; 1. DR PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1. DR Pfam; PF00048; IL8; 1. DR SMART; SM00199; SCY; 1. DR SUPFAM; SSF54117; Interleukin 8-like chemokines; 1. DR PROSITE; PS00472; SMALL_CYTOKINES_CC; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Chemotaxis; Cytokine; KW Direct protein sequencing; Disulfide bond; Heparin-binding; KW Inflammatory response; Proteomics identification; Reference proteome; KW Secreted; Signal. FT SIGNAL 1..21 FT /evidence="ECO:0000269|PubMed:9104803" FT CHAIN 22..120 FT /note="C-C motif chemokine 23" FT /id="PRO_0000005229" FT CHAIN 40..120 FT /note="CCL23(19-99)" FT /evidence="ECO:0000269|PubMed:15905581" FT /id="PRO_0000041847" FT CHAIN 43..120 FT /note="CCL23(22-99)" FT /evidence="ECO:0000269|PubMed:15905581" FT /id="PRO_0000041848" FT CHAIN 48..120 FT /note="CCL23(27-99)" FT /evidence="ECO:0000269|PubMed:15905581" FT /id="PRO_0000041849" FT CHAIN 51..120 FT /note="CCL23(30-99)" FT /evidence="ECO:0000269|PubMed:15905581" FT /id="PRO_0000041850" FT DISULFID 54..78 FT /evidence="ECO:0000269|PubMed:11060285" FT DISULFID 55..94 FT /evidence="ECO:0000269|PubMed:11060285" FT DISULFID 65..105 FT /evidence="ECO:0000269|PubMed:11060285" FT VAR_SEQ 46 FT /note="R -> MLWRRKIGPQMTLSHAAG (in isoform Long)" FT /evidence="ECO:0000303|PubMed:15489334, FT ECO:0000303|PubMed:9558365" FT /id="VSP_001063" FT VARIANT 106 FT /note="M -> V (in dbSNP:rs1003645)" FT /id="VAR_011916" FT CONFLICT 12..44 FT /note="MLVTALGSQARVTKDAETEFMMSKLPLENPVLL -> HAFLLPLVPGPGHKR FT CRDRVHECQSFHWKIQYFW (in Ref. 1)" FT /evidence="ECO:0000305" FT STRAND 48..50 FT /evidence="ECO:0007829|PDB:1G91" FT HELIX 65..67 FT /evidence="ECO:0007829|PDB:1G91" FT STRAND 70..73 FT /evidence="ECO:0007829|PDB:1G91" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:1G91" FT STRAND 83..86 FT /evidence="ECO:0007829|PDB:1G91" FT STRAND 92..95 FT /evidence="ECO:0007829|PDB:1G91" FT HELIX 100..109 FT /evidence="ECO:0007829|PDB:1G91" FT TURN 113..115 FT /evidence="ECO:0007829|PDB:1G91" SQ SEQUENCE 120 AA; 13443 MW; 6CA622DD3A4B27AD CRC64; MKVSVAALSC LMLVTALGSQ ARVTKDAETE FMMSKLPLEN PVLLDRFHAT SADCCISYTP RSIPCSLLES YFETNSECSK PGVIFLTKKG RRFCANPSDK QVQVCMRMLK LDTRIKTRKN //