CCL23_HUMAN
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 03-AUG-2022, entry version 185.
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;
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.
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 the small-inducible cytokine A23.
CC {ECO:0000269|PubMed:15905581}.
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 -!- 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";
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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_005064.5.
DR RefSeq; NP_665905.2; NM_145898.3.
DR PDB; 1G91; NMR; -; A=45-120.
DR PDBsum; 1G91; -.
DR AlphaFoldDB; P55773; -.
DR BioGRID; 112271; 4.
DR IntAct; P55773; 2.
DR PhosphoSitePlus; P55773; -.
DR BioMuta; CCL23; -.
DR DMDM; 308153623; -.
DR MassIVE; P55773; -.
DR PeptideAtlas; P55773; -.
DR PRIDE; P55773; -.
DR ProteomicsDB; 56861; -. [P55773-1]
DR ProteomicsDB; 56862; -. [P55773-2]
DR Antibodypedia; 73206; 298 antibodies from 30 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 CTD; 6368; -.
DR DisGeNET; 6368; -.
DR GeneCards; CCL23; -.
DR HGNC; HGNC:10622; CCL23.
DR HPA; ENSG00000274736; Low tissue specificity.
DR MIM; 602494; gene.
DR neXtProt; NX_P55773; -.
DR OpenTargets; ENSG00000274736; -.
DR PharmGKB; PA35554; -.
DR VEuPathDB; HostDB:ENSG00000274736; -.
DR GeneTree; ENSGT01050000244851; -.
DR HOGENOM; CLU_141716_4_1_1; -.
DR InParanoid; P55773; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; P55773; -.
DR TreeFam; TF334888; -.
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 BioGRID-ORCS; 6368; 12 hits in 1058 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 right lung and 83 other tissues.
DR ExpressionAtlas; P55773; baseline and differential.
DR Genevisible; P55773; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
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:0031726; F:CCR1 chemokine receptor binding; IPI:UniProtKB.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006874; P:cellular calcium ion homeostasis; 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: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:2001264; P:negative regulation of C-C chemokine binding; IDA:UniProtKB.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
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; PTHR12015; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 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; Reference proteome; 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 /id="PRO_0000041847"
FT CHAIN 43..120
FT /note="CCL23(22-99)"
FT /id="PRO_0000041848"
FT CHAIN 48..120
FT /note="CCL23(27-99)"
FT /id="PRO_0000041849"
FT CHAIN 51..120
FT /note="CCL23(30-99)"
FT /id="PRO_0000041850"
FT DISULFID 54..78
FT DISULFID 55..94
FT DISULFID 65..105
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
