ID CCL25_HUMAN Reviewed; 150 AA. AC O15444; A1L4J4; A6NI52; A8K9E7; B5MCA5; Q96KJ7; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 22-JUL-2008, sequence version 2. DT 13-FEB-2019, entry version 148. 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 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] (ISOFORM 1), AND VARIANT MET-104. 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] (ISOFORM 2). RC TISSUE=Thymus; RA Hieshima K., Nakayama T., Fujisawa R., Izawa D., Yoshie O.; RT "Molecular cloning and characterization of a splicing variant of RT chemokine TECK: a natural antagonist of human TECK."; RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Thymus; 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=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Lung; 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 [7] RP RECEPTOR INTERACTION. RX PubMed=10229797; RA Zaballos A., Gutierrez J., Varona R., Ardavin C., Marquez G.; RT "Identification of the orphan chemokine receptor GPR-9-6 as CCR9, the RT receptor for the chemokine TECK."; RL J. Immunol. 162:5671-5675(1999). RN [8] RP RECEPTOR INTERACTION. RX PubMed=23341447; DOI=10.1074/jbc.M112.406108; RA Watts A.O., Verkaar F., van der Lee M.M., Timmerman C.A., Kuijer M., RA van Offenbeek J., van Lith L.H., Smit M.J., Leurs R., Zaman G.J., RA Vischer H.F.; RT "Beta-arrestin recruitment and G protein signaling by the atypical RT human chemokine decoy receptor CCX-CKR."; RL J. Biol. Chem. 288:7169-7181(2013). CC -!- FUNCTION: Potentially involved in T-cell development. Recombinant CC protein shows chemotactic activity on thymocytes, macrophages, CC THP-1 cells, and dendritics cells but is inactive on peripheral CC blood lymphocytes and neutrophils. Binds to CCR9. Isoform 2 is an CC antagonist of isoform 1. Binds to atypical chemokine receptor CC ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2) to CC ACKR4. CC -!- INTERACTION: CC Q92583:CCL17; NbExp=2; IntAct=EBI-7783341, EBI-16640146; CC P13501:CCL5; NbExp=2; IntAct=EBI-7783341, EBI-2848366; CC P48061:CXCL12; NbExp=2; IntAct=EBI-7783341, EBI-3913254; CC P02776:PF4; NbExp=3; IntAct=EBI-7783341, EBI-2565740; CC P10720:PF4V1; NbExp=2; IntAct=EBI-7783341, EBI-1223944; CC -!- SUBCELLULAR LOCATION: Secreted. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=O15444-1; Sequence=Displayed; CC Name=2; Synonyms=TECKvar; CC IsoId=O15444-2; Sequence=VSP_001064; CC Note=May be produced at very low levels due to a premature stop CC codon in the mRNA, leading to nonsense-mediated mRNA decay.; CC Name=3; CC IsoId=O15444-3; Sequence=VSP_043199; CC -!- TISSUE SPECIFICITY: Specifically expressed by thymic dendritic CC cells. High levels in thymus and small intestine. CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL25 entry; CC URL="https://en.wikipedia.org/wiki/CCL25"; 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; U86358; AAB69981.1; -; mRNA. DR EMBL; AB046579; BAB62257.1; -; mRNA. DR EMBL; AK292662; BAF85351.1; -; mRNA. DR EMBL; AC008946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471139; EAW68952.1; -; Genomic_DNA. DR EMBL; BC130561; AAI30562.1; -; mRNA. DR EMBL; BC144463; AAI44464.1; -; mRNA. DR CCDS; CCDS12194.1; -. [O15444-1] DR CCDS; CCDS56080.1; -. [O15444-3] DR RefSeq; NP_001188288.1; NM_001201359.1. [O15444-3] DR RefSeq; NP_005615.2; NM_005624.3. [O15444-1] DR RefSeq; XP_011526479.1; XM_011528177.2. [O15444-1] DR RefSeq; XP_016882609.1; XM_017027120.1. [O15444-1] DR RefSeq; XP_016882610.1; XM_017027121.1. [O15444-1] DR RefSeq; XP_016882611.1; XM_017027122.1. [O15444-3] DR UniGene; Hs.310511; -. DR ProteinModelPortal; O15444; -. DR SMR; O15444; -. DR BioGrid; 112273; 3. DR DIP; DIP-5883N; -. DR IntAct; O15444; 10. DR MINT; O15444; -. DR STRING; 9606.ENSP00000375086; -. DR iPTMnet; O15444; -. DR PhosphoSitePlus; O15444; -. DR BioMuta; CCL25; -. DR PaxDb; O15444; -. DR PRIDE; O15444; -. DR ProteomicsDB; 48672; -. DR ProteomicsDB; 48673; -. [O15444-2] DR ProteomicsDB; 48674; -. [O15444-3] DR DNASU; 6370; -. DR Ensembl; ENST00000253451; ENSP00000253451; ENSG00000131142. [O15444-3] DR Ensembl; ENST00000390669; ENSP00000375086; ENSG00000131142. [O15444-1] DR GeneID; 6370; -. DR KEGG; hsa:6370; -. DR UCSC; uc002mjc.5; human. [O15444-1] DR CTD; 6370; -. DR DisGeNET; 6370; -. DR EuPathDB; HostDB:ENSG00000131142.13; -. DR GeneCards; CCL25; -. DR H-InvDB; HIX0039931; -. DR HGNC; HGNC:10624; CCL25. DR HPA; HPA055883; -. DR MIM; 602565; gene. DR neXtProt; NX_O15444; -. DR OpenTargets; ENSG00000131142; -. DR PharmGKB; PA35556; -. DR eggNOG; ENOG410J09B; Eukaryota. DR eggNOG; ENOG410Z7F2; LUCA. DR GeneTree; ENSGT00940000154040; -. DR HOGENOM; HOG000293281; -. DR HOVERGEN; HBG050832; -. DR InParanoid; O15444; -. DR KO; K13072; -. DR OMA; CCLAYHR; -. DR OrthoDB; 1542802at2759; -. DR PhylomeDB; O15444; -. DR TreeFam; TF353160; -. DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines. DR Reactome; R-HSA-418594; G alpha (i) signalling events. DR SIGNOR; O15444; -. DR GenomeRNAi; 6370; -. DR PRO; PR:O15444; -. DR Proteomes; UP000005640; Chromosome 19. DR Bgee; ENSG00000131142; Expressed in 59 organ(s), highest expression level in intestine. DR ExpressionAtlas; O15444; baseline and differential. DR Genevisible; O15444; 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:0031735; F:CCR10 chemokine receptor binding; IDA:BHF-UCL. DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB. DR GO; GO:0042379; F:chemokine receptor binding; IDA:UniProtKB. DR GO; GO:0005179; F:hormone activity; TAS:ProtInc. DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB. DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB. DR GO; GO:0007166; P:cell surface receptor signaling pathway; 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; IDA:UniProtKB. DR GO; GO:0006955; P:immune response; TAS:ProtInc. DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central. DR GO; GO:0031640; P:killing of cells of other organism; IDA:UniProtKB. DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central. DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central. DR GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IDA:UniProtKB. DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central. DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:UniProtKB. 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 1: Evidence at protein level; KW Alternative splicing; Chemotaxis; Complete proteome; Cytokine; KW Disulfide bond; Inflammatory response; Polymorphism; KW Reference proteome; Secreted; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 150 C-C motif chemokine 25. FT /FTId=PRO_0000005235. FT DISULFID 30 58 {ECO:0000250}. FT DISULFID 31 75 {ECO:0000250}. FT VAR_SEQ 65 150 FYLPKRHRKVCGNPKSREVQRAMKLLDARNKVFAKLHHNTQ FT TFQAGPHAVKKLSSGNSKLSSSKFSNPISSSKRNVSLLISA FT NSGL -> RPSCCKEVEFWKLQVIIIQV (in isoform FT 2). {ECO:0000303|Ref.2}. FT /FTId=VSP_001064. FT VAR_SEQ 109 109 Missing (in isoform 3). FT {ECO:0000303|PubMed:14702039, FT ECO:0000303|PubMed:15489334}. FT /FTId=VSP_043199. FT VARIANT 23 23 T -> A (in dbSNP:rs960173). FT /FTId=VAR_044519. FT VARIANT 101 101 H -> R (in dbSNP:rs2032887). FT /FTId=VAR_044520. FT VARIANT 104 104 T -> M (in dbSNP:rs1129763). FT {ECO:0000269|PubMed:9285413}. FT /FTId=VAR_044521. SQ SEQUENCE 150 AA; 16609 MW; 91D0810F137FBC7B CRC64; MNLWLLACLV AGFLGAWAPA VHTQGVFEDC CLAYHYPIGW AVLRRAWTYR IQEVSGSCNL PAAIFYLPKR HRKVCGNPKS REVQRAMKLL DARNKVFAKL HHNTQTFQAG PHAVKKLSSG NSKLSSSKFS NPISSSKRNV SLLISANSGL //