CCL26_HUMAN
ID CCL26_HUMAN Reviewed; 94 AA.
AC Q9Y258; A0N0Q5; Q52LV8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=C-C motif chemokine 26;
DE AltName: Full=CC chemokine IMAC {ECO:0000303|Ref.5};
DE AltName: Full=Eotaxin-3 {ECO:0000303|PubMed:10415065};
DE AltName: Full=Macrophage inflammatory protein 4-alpha;
DE Short=MIP-4-alpha;
DE AltName: Full=Small-inducible cytokine A26 {ECO:0000303|PubMed:10373330};
DE AltName: Full=Thymic stroma chemokine-1 {ECO:0000303|Ref.4};
DE Short=TSC-1 {ECO:0000303|Ref.4};
DE Flags: Precursor;
GN Name=CCL26 {ECO:0000312|HGNC:HGNC:10625};
GN Synonyms=SCYA26 {ECO:0000303|PubMed:10373330};
GN ORFNames=UNQ216/PRO242 {ECO:0000303|PubMed:12975309};
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], AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=10373330; DOI=10.1006/geno.1999.5837;
RA Guo R.F., Ward P.A., Hu S.M., McDuffie J.E., Huber-Lang M., Shi M.M.;
RT "Molecular cloning and characterization of a novel human CC chemokine,
RT SCYA26.";
RL Genomics 58:313-317(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=10415065;
RA Shinkai A., Yoshisue H., Koike M., Shoji E., Nakagawa S., Saito A.,
RA Takeda T., Imabeppu S., Kato Y., Hanai N., Anazawa H., Kuga T., Nishi T.;
RT "A novel human CC chemokine, eotaxin-3, which is expressed in IL-4-
RT stimulated vascular endothelial cells, exhibits potent activity toward
RT eosinophils.";
RL J. Immunol. 163:1602-1610(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION,
RP SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=10488147; DOI=10.1074/jbc.274.39.27975;
RA Kitaura M., Suzuki N., Imai T., Takagi S., Suzuki R., Nakajima T.,
RA Hirai K., Nomiyama H., Yoshie O.;
RT "Molecular cloning of a novel human CC chemokine (Eotaxin-3) that is a
RT functional ligand of CC chemokine receptor 3.";
RL J. Biol. Chem. 274:27975-27980(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Z., Scadden D.T.;
RT "A novel CC chemokine expressed in thymic stroma.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Berg E.L., Melrose J., Fu H., Tsurushita N.;
RT "Molecular cloning and characterization of a new human CC chemokine IMAC.";
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Livingston R.J., Shaffer T., McFarland I., Nguyen C.P., Stanaway I.B.,
RA Rajkumar N., Johnson E.J., da Ponte S.H., Willa H., Ahearn M.O.,
RA Bertucci C., Acklestad J., Carroll A., Swanson J., Gildersleeve H.I.,
RA Nickerson D.A.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [8]
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 [9]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Colon;
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 [11]
RP STRUCTURE BY NMR, FUNCTION, AND DISULFIDE BONDS.
RX PubMed=11425309; DOI=10.1021/bi010252s;
RA Ye J., Mayer K.L., Mayer M.R., Stone M.J.;
RT "NMR solution structure and backbone dynamics of the CC chemokine eotaxin-
RT 3.";
RL Biochemistry 40:7820-7831(2001).
RN [12]
RP FUNCTION.
RX PubMed=20974991; DOI=10.4049/jimmunol.0904126;
RA Nakayama T., Watanabe Y., Oiso N., Higuchi T., Shigeta A., Mizuguchi N.,
RA Katou F., Hashimoto K., Kawada A., Yoshie O.;
RT "Eotaxin-3/CC chemokine ligand 26 is a functional ligand for CX3CR1.";
RL J. Immunol. 185:6472-6479(2010).
CC -!- FUNCTION: Chemoattractant for eosinophils and basophils
CC (PubMed:10415065, PubMed:10488147). Acts as a ligand for C-C chemokine
CC receptor CCR3 which triggers Ca(2+) mobilization in eosinophils
CC (PubMed:10415065, PubMed:10488147, PubMed:11425309). Also acts as a
CC ligand for CX3C chemokine receptor CX3CR1, inducing cell chemotaxis
CC (PubMed:20974991). {ECO:0000269|PubMed:10415065,
CC ECO:0000269|PubMed:10488147, ECO:0000269|PubMed:11425309,
CC ECO:0000269|PubMed:20974991}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10488147}.
CC -!- INTERACTION:
CC Q9Y258; Q99616: CCL13; NbExp=2; IntAct=EBI-7783416, EBI-725342;
CC Q9Y258; Q92583: CCL17; NbExp=2; IntAct=EBI-7783416, EBI-16640146;
CC Q9Y258; O00585: CCL21; NbExp=2; IntAct=EBI-7783416, EBI-953695;
CC Q9Y258; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-7783416, EBI-7783254;
CC Q9Y258; P13501: CCL5; NbExp=4; IntAct=EBI-7783416, EBI-2848366;
CC Q9Y258; P02778: CXCL10; NbExp=2; IntAct=EBI-7783416, EBI-7815386;
CC Q9Y258; O14625: CXCL11; NbExp=2; IntAct=EBI-7783416, EBI-2871971;
CC Q9Y258; P48061: CXCL12; NbExp=2; IntAct=EBI-7783416, EBI-3913254;
CC Q9Y258; O95715: CXCL14; NbExp=2; IntAct=EBI-7783416, EBI-2798068;
CC Q9Y258; Q07325: CXCL9; NbExp=2; IntAct=EBI-7783416, EBI-3911467;
CC Q9Y258; P26367: PAX6; NbExp=3; IntAct=EBI-7783416, EBI-747278;
CC Q9Y258; P02776: PF4; NbExp=3; IntAct=EBI-7783416, EBI-2565740;
CC Q9Y258; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-7783416, EBI-10243654;
CC Q9Y258; P47992: XCL1; NbExp=2; IntAct=EBI-7783416, EBI-10209901;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10488147}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed at low levels in various
CC tissues including heart and ovary. {ECO:0000269|PubMed:10373330,
CC ECO:0000269|PubMed:10488147}.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL26 entry;
CC URL="https://en.wikipedia.org/wiki/CCL26";
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DR EMBL; AF124601; AAD22197.1; -; mRNA.
DR EMBL; AB016542; BAA36704.1; -; mRNA.
DR EMBL; AB010447; BAA84579.1; -; mRNA.
DR EMBL; AF096296; AAF09265.1; -; mRNA.
DR EMBL; AF142434; AAD46495.1; -; mRNA.
DR EMBL; EF064763; ABK41946.1; -; Genomic_DNA.
DR EMBL; AY358893; AAQ89252.1; -; mRNA.
DR EMBL; AC005102; AAD15411.1; -; Genomic_DNA.
DR EMBL; CH471220; EAW71771.1; -; Genomic_DNA.
DR EMBL; BC069394; AAH69394.1; -; mRNA.
DR EMBL; BC093773; AAH93773.1; -; mRNA.
DR EMBL; BC101665; AAI01666.1; -; mRNA.
DR CCDS; CCDS5578.1; -.
DR RefSeq; NP_006063.1; NM_006072.4.
DR RefSeq; XP_016867161.1; XM_017011672.1.
DR PDB; 1G2S; NMR; -; A=24-94.
DR PDB; 1G2T; NMR; -; A=24-94.
DR PDBsum; 1G2S; -.
DR PDBsum; 1G2T; -.
DR AlphaFoldDB; Q9Y258; -.
DR SMR; Q9Y258; -.
DR BioGRID; 115626; 48.
DR DIP; DIP-5877N; -.
DR IntAct; Q9Y258; 22.
DR MINT; Q9Y258; -.
DR STRING; 9606.ENSP00000378365; -.
DR iPTMnet; Q9Y258; -.
DR PhosphoSitePlus; Q9Y258; -.
DR BioMuta; CCL26; -.
DR DMDM; 6685990; -.
DR MassIVE; Q9Y258; -.
DR PaxDb; Q9Y258; -.
DR PeptideAtlas; Q9Y258; -.
DR PRIDE; Q9Y258; -.
DR ProteomicsDB; 85661; -.
DR Antibodypedia; 29148; 339 antibodies from 26 providers.
DR DNASU; 10344; -.
DR Ensembl; ENST00000005180.9; ENSP00000005180.4; ENSG00000006606.9.
DR Ensembl; ENST00000394905.2; ENSP00000378365.2; ENSG00000006606.9.
DR GeneID; 10344; -.
DR KEGG; hsa:10344; -.
DR MANE-Select; ENST00000005180.9; ENSP00000005180.4; NM_001371938.1; NP_001358867.1.
DR UCSC; uc003udt.2; human.
DR CTD; 10344; -.
DR DisGeNET; 10344; -.
DR GeneCards; CCL26; -.
DR HGNC; HGNC:10625; CCL26.
DR HPA; ENSG00000006606; Tissue enhanced (ovary, pituitary gland).
DR MIM; 604697; gene.
DR neXtProt; NX_Q9Y258; -.
DR OpenTargets; ENSG00000006606; -.
DR PharmGKB; PA35557; -.
DR VEuPathDB; HostDB:ENSG00000006606; -.
DR eggNOG; ENOG502T082; Eukaryota.
DR GeneTree; ENSGT01050000244920; -.
DR HOGENOM; CLU_141716_6_0_1; -.
DR InParanoid; Q9Y258; -.
DR OMA; CAHPKEK; -.
DR OrthoDB; 1575018at2759; -.
DR PhylomeDB; Q9Y258; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; Q9Y258; -.
DR SignaLink; Q9Y258; -.
DR BioGRID-ORCS; 10344; 18 hits in 1071 CRISPR screens.
DR EvolutionaryTrace; Q9Y258; -.
DR GenomeRNAi; 10344; -.
DR Pharos; Q9Y258; Tbio.
DR PRO; PR:Q9Y258; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q9Y258; protein.
DR Bgee; ENSG00000006606; Expressed in right ovary and 94 other tissues.
DR Genevisible; Q9Y258; HS.
DR GO; GO:0005615; C:extracellular space; IDA:CAFA.
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:CAFA.
DR GO; GO:0031737; F:CX3C chemokine receptor binding; 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; IDA:CAFA.
DR GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR GO; GO:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
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; IDA:CAFA.
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:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IDA:CAFA.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:BHF-UCL.
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:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0010818; P:T cell chemotaxis; IDA:CAFA.
DR DisProt; DP00696; -.
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; Chemotaxis; Cytokine; Direct protein sequencing;
KW Disulfide bond; Inflammatory response; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:10488147"
FT CHAIN 24..94
FT /note="C-C motif chemokine 26"
FT /id="PRO_0000005238"
FT DISULFID 33..57
FT /evidence="ECO:0000269|PubMed:11425309"
FT DISULFID 34..73
FT /evidence="ECO:0000269|PubMed:11425309"
FT VARIANT 18
FT /note="L -> R (in dbSNP:rs11465333)"
FT /id="VAR_029192"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:1G2S"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:1G2S"
FT STRAND 55..59
FT /evidence="ECO:0007829|PDB:1G2S"
FT STRAND 62..66
FT /evidence="ECO:0007829|PDB:1G2S"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:1G2S"
FT STRAND 76..78
FT /evidence="ECO:0007829|PDB:1G2S"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:1G2S"
SQ SEQUENCE 94 AA; 10648 MW; 8525B1E4BDD39A5F CRC64;
MMGLSLASAV LLASLLSLHL GTATRGSDIS KTCCFQYSHK PLPWTWVRSY EFTSNSCSQR
AVIFTTKRGK KVCTHPRKKW VQKYISLLKT PKQL
