CCL25_MOUSE
ID CCL25_MOUSE Reviewed; 144 AA.
AC O35903; Q9QYY6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 18-SEP-2013, sequence version 2.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=C-C motif chemokine 25;
DE AltName: Full=Chemokine TECK;
DE AltName: Full=Small-inducible cytokine A25;
DE AltName: Full=Thymus-expressed chemokine;
DE Flags: Precursor;
GN Name=Ccl25; Synonyms=Scya25, Teck;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Thymus;
RX PubMed=9285413; DOI=10.1016/s1074-7613(00)80531-2;
RA Vicari A.P., Figueroa D.J., Hedrick J.A., Foster J.S., Singh K.P.,
RA Menon S., Copeland N.G., Gilbert D.J., Jenkins N.A., Bacon K.B.,
RA Zlotnik A.;
RT "TECK: a novel CC chemokine specifically expressed by thymic dendritic
RT cells and potentially involved in T cell development.";
RL Immunity 7:291-301(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10602049;
RX DOI=10.1002/1521-4141(200001)30:1<262::aid-immu262>3.0.co;2-0;
RA Wurbel M.A., Philippe J.-M., Nguyen C., Victorero G., Freeman T.,
RA Wooding P., Miazek A., Mattei M.-G., Malissen M., Jordan B.R., Malissen B.,
RA Carrier A., Naquet P.;
RT "The chemokine TECK is expressed by thymic and intestinal epithelial cells
RT and attracts double- and single-positive thymocytes expressing the TECK
RT receptor CCR9.";
RL Eur. J. Immunol. 30:262-271(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Small intestine;
RX PubMed=16517733; DOI=10.4049/jimmunol.176.6.3642;
RA Ericsson A., Kotarsky K., Svensson M., Sigvardsson M., Agace W.;
RT "Functional characterization of the CCL25 promoter in small intestinal
RT epithelial cells suggests a regulatory role for caudal-related homeobox
RT (Cdx) transcription factors.";
RL J. Immunol. 176:3642-3651(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: Potentially involved in T-cell development. Recombinant
CC protein shows chemotactic activity on thymocytes, macrophages, THP-1
CC cells, and dendritics cells but is inactive on peripheral blood
CC lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine
CC receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2)
CC to ACKR4.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Specifically expressed by thymic dendritic cells.
CC High levels in thymus and small intestine.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
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DR EMBL; U86357; AAB69982.1; -; mRNA.
DR EMBL; AJ249480; CAB55762.1; -; mRNA.
DR EMBL; DQ158256; AAZ99719.1; -; mRNA.
DR EMBL; AK134138; BAE22030.1; -; mRNA.
DR EMBL; AC155164; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC117033; AAI17034.1; -; mRNA.
DR EMBL; BC117037; AAI17038.1; -; mRNA.
DR CCDS; CCDS22085.1; -.
DR RefSeq; NP_033164.1; NM_009138.3.
DR RefSeq; XP_011240345.2; XM_011242043.2.
DR RefSeq; XP_011240346.2; XM_011242044.2.
DR AlphaFoldDB; O35903; -.
DR SMR; O35903; -.
DR DIP; DIP-5885N; -.
DR IntAct; O35903; 5.
DR MINT; O35903; -.
DR STRING; 10090.ENSMUSP00000024004; -.
DR PhosphoSitePlus; O35903; -.
DR PaxDb; O35903; -.
DR PRIDE; O35903; -.
DR ProteomicsDB; 281329; -.
DR DNASU; 20300; -.
DR Ensembl; ENSMUST00000024004; ENSMUSP00000024004; ENSMUSG00000023235.
DR GeneID; 20300; -.
DR KEGG; mmu:20300; -.
DR UCSC; uc009ktw.2; mouse.
DR CTD; 6370; -.
DR MGI; MGI:1099448; Ccl25.
DR VEuPathDB; HostDB:ENSMUSG00000023235; -.
DR eggNOG; ENOG502S8D1; Eukaryota.
DR GeneTree; ENSGT01010000222539; -.
DR InParanoid; O35903; -.
DR OrthoDB; 1542802at2759; -.
DR TreeFam; TF353160; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 20300; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Ccl25; mouse.
DR PRO; PR:O35903; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; O35903; protein.
DR Bgee; ENSMUSG00000023235; Expressed in small intestine Peyer's patch and 174 other tissues.
DR ExpressionAtlas; O35903; baseline and differential.
DR Genevisible; O35903; MM.
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:0031735; F:CCR10 chemokine receptor binding; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; IDA:MGI.
DR GO; GO:0042379; F:chemokine receptor binding; ISS:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; ISO:MGI.
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; IDA:MGI.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:MGI.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:0050900; P:leukocyte migration; IDA:MGI.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0097534; P:lymphoid lineage cell migration; IDA:MGI.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; ISO:MGI.
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 CDD; cd01119; Chemokine_CC_DCCL; 1.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR034133; Chemokine_CC_DCCL.
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 2: Evidence at transcript level;
KW Chemotaxis; Cytokine; Disulfide bond; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..144
FT /note="C-C motif chemokine 25"
FT /id="PRO_0000005236"
FT REGION 98..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 30..58
FT /evidence="ECO:0000250"
FT DISULFID 31..73
FT /evidence="ECO:0000250"
FT CONFLICT 85
FT /note="M -> I (in Ref. 1; AAB69982)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 144 AA; 16733 MW; CEC1924B320B4408 CRC64;
MKLWLFACLV ACFVGAWMPV VHAQGAFEDC CLGYQHRIKW NVLRHARNYH QQEVSGSCNL
RAVRFYFRQK VVCGNPEDMN VKRAMRILTA RKRLVHWKSA SDSQTERKKS NHMKSKVENP
NSTSVRSATL GHPRMVMMPR KTNN
