CCL21_HUMAN
ID CCL21_HUMAN Reviewed; 134 AA.
AC O00585; Q6ICR7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=C-C motif chemokine 21;
DE AltName: Full=6Ckine;
DE AltName: Full=Beta-chemokine exodus-2;
DE AltName: Full=Secondary lymphoid-tissue chemokine;
DE Short=SLC;
DE AltName: Full=Small-inducible cytokine A21;
DE Flags: Precursor;
GN Name=CCL21; Synonyms=SCYA21; ORFNames=UNQ784/PRO1600;
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].
RX PubMed=9235955; DOI=10.1074/jbc.272.31.19518;
RA Nagira M., Imai T., Hieshima K., Kusuda J., Ridanpaeae M., Takagi S.,
RA Nishimura M., Kakizaki M., Nomiyama H., Yoshie O.;
RT "Molecular cloning of a novel human CC chemokine secondary lymphoid-tissue
RT chemokine that is a potent chemoattractant for lymphocytes and mapped to
RT chromosome 9p13.";
RL J. Biol. Chem. 272:19518-19524(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9257816;
RA Hedrick J.A., Zlotnik A.;
RT "Identification and characterization of a novel beta chemokine containing
RT six conserved cysteines.";
RL J. Immunol. 159:1589-1593(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 24-33.
RX PubMed=9300671;
RA Hromas R., Kim C.H., Klemsz M., Krathwohl M., Fife K., Cooper S.,
RA Schnizlein-Bick C., Broxmeyer H.E.;
RT "Isolation and characterization of Exodus-2, a novel C-C chemokine with a
RT unique 37-amino acid carboxyl-terminal extension.";
RL J. Immunol. 159:2554-2558(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
RX PubMed=9419363; DOI=10.1073/pnas.95.1.258;
RA Gunn M.D., Tangemann K., Tam C., Cyster J.G., Rosen S.D., Williams L.T.;
RT "A chemokine expressed in lymphoid high endothelial venules promotes the
RT adhesion and chemotaxis of naive T lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:258-263(1998).
RN [5] {ECO:0000312|EMBL:AAQ13417.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Fu Q., Yu L., Bi A., Zhang Q.;
RT "Isolation of human genomic DNA fragment coding an efficient
RT chemoattractant for lymphocytes.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Reiterer P., Bernhardt G., Lipp M.;
RT "Genomic organisation of human SLC.";
RL Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN [7] {ECO:0000312|EMBL:ABK41948.1}
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 [8]
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 [9] {ECO:0000312|EMBL:BAG34842.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen {ECO:0000312|EMBL:BAG34842.1};
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [10] {ECO:0000312|EMBL:CAG29322.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
RN [11]
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 [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Pancreas, and Spleen;
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 [13]
RP RECEPTOR INTERACTION.
RX PubMed=9507024; DOI=10.1074/jbc.273.12.7118;
RA Yoshida R., Nagira M., Kitaura M., Imagawa N., Imai T., Yoshie O.;
RT "Secondary lymphoid-tissue chemokine is a functional ligand for the CC
RT chemokine receptor CCR7.";
RL J. Biol. Chem. 273:7118-7122(1998).
RN [14]
RP INTERACTION WITH PDPN.
RX PubMed=14978162; DOI=10.1097/01.asn.0000113316.52371.2e;
RA Kerjaschki D., Regele H.M., Moosberger I., Nagy-Bojarski K.,
RA Watschinger B., Soleiman A., Birner P., Krieger S., Hovorka A.,
RA Silberhumer G., Laakkonen P., Petrova T., Langer B., Raab I.;
RT "Lymphatic neoangiogenesis in human kidney transplants is associated with
RT immunologically active lymphocytic infiltrates.";
RL J. Am. Soc. Nephrol. 15:603-612(2004).
RN [15]
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 human
RT chemokine decoy receptor CCX-CKR.";
RL J. Biol. Chem. 288:7169-7181(2013).
RN [16]
RP INTERACTION WITH TNFAIP6.
RX PubMed=27044744; DOI=10.1074/jbc.m116.720953;
RA Dyer D.P., Salanga C.L., Johns S.C., Valdambrini E., Fuster M.M.,
RA Milner C.M., Day A.J., Handel T.M.;
RT "The Anti-inflammatory Protein TSG-6 Regulates Chemokine Function by
RT Inhibiting Chemokine/Glycosaminoglycan Interactions.";
RL J. Biol. Chem. 291:12627-12640(2016).
RN [17]
RP STRUCTURE BY NMR OF 24-134, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22221265; DOI=10.1021/bi201601k;
RA Love M., Sandberg J.L., Ziarek J.J., Gerarden K.P., Rode R.R., Jensen D.R.,
RA McCaslin D.R., Peterson F.C., Veldkamp C.T.;
RT "Solution structure of CCL21 and identification of a putative CCR7 binding
RT site.";
RL Biochemistry 51:733-735(2012).
CC -!- FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic
CC in vitro for thymocytes and activated T-cells, but not for B-cells,
CC macrophages, or neutrophils. Shows preferential activity towards naive
CC T-cells. May play a role in mediating homing of lymphocytes to
CC secondary lymphoid organs. Binds to atypical chemokine receptor ACKR4
CC and mediates the recruitment of beta-arrestin (ARRB1/2) to ACKR4.
CC -!- SUBUNIT: Monomer. Binds to CCR7. Interacts with PDPN; relocalizes PDPN
CC to the basolateral membrane (PubMed:14978162). Interacts with TNFAIP6
CC (via Link domain). {ECO:0000269|PubMed:14978162,
CC ECO:0000269|PubMed:22221265, ECO:0000269|PubMed:27044744}.
CC -!- INTERACTION:
CC O00585; Q99616: CCL13; NbExp=2; IntAct=EBI-953695, EBI-725342;
CC O00585; Q92583: CCL17; NbExp=2; IntAct=EBI-953695, EBI-16640146;
CC O00585; Q9Y258: CCL26; NbExp=2; IntAct=EBI-953695, EBI-7783416;
CC O00585; Q9NRJ3: CCL28; NbExp=2; IntAct=EBI-953695, EBI-7783254;
CC O00585; P13501: CCL5; NbExp=2; IntAct=EBI-953695, EBI-2848366;
CC O00585; P02778: CXCL10; NbExp=2; IntAct=EBI-953695, EBI-7815386;
CC O00585; P48061: CXCL12; NbExp=2; IntAct=EBI-953695, EBI-3913254;
CC O00585; O95715: CXCL14; NbExp=2; IntAct=EBI-953695, EBI-2798068;
CC O00585; Q07325: CXCL9; NbExp=2; IntAct=EBI-953695, EBI-3911467;
CC O00585; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-953695, EBI-1055254;
CC O00585; Q5XKR4: OTP; NbExp=3; IntAct=EBI-953695, EBI-12865884;
CC O00585; P02776: PF4; NbExp=2; IntAct=EBI-953695, EBI-2565740;
CC O00585; P10720: PF4V1; NbExp=2; IntAct=EBI-953695, EBI-1223944;
CC O00585; Q6UX40: TMEM107; NbExp=3; IntAct=EBI-953695, EBI-12845616;
CC O00585; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-953695, EBI-10243654;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highly expressed in high endothelial venules of
CC lymph nodes, spleen and appendix. Intermediate levels found in small
CC intestine, thyroid gland and trachea. Low level expression in thymus,
CC bone marrow, liver, and pancreas. Also found in tonsil, fetal heart and
CC fetal spleen.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CCL21 entry;
CC URL="https://en.wikipedia.org/wiki/CCL21";
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DR EMBL; AB002409; BAA21817.1; -; mRNA.
DR EMBL; AF001979; AAB86594.1; -; mRNA.
DR EMBL; U88320; AAB91454.1; -; mRNA.
DR EMBL; AF030572; AAQ13417.1; -; Genomic_DNA.
DR EMBL; AJ005654; CAA06653.1; -; Genomic_DNA.
DR EMBL; EF064765; ABK41948.1; -; Genomic_DNA.
DR EMBL; AY358887; AAQ89246.1; -; mRNA.
DR EMBL; AK311901; BAG34842.1; -; mRNA.
DR EMBL; CR450326; CAG29322.1; -; mRNA.
DR EMBL; CH471071; EAW58415.1; -; Genomic_DNA.
DR EMBL; BC027918; AAH27918.1; -; mRNA.
DR CCDS; CCDS6571.1; -.
DR RefSeq; NP_002980.1; NM_002989.3.
DR PDB; 2L4N; NMR; -; A=24-134.
DR PDB; 5EKI; X-ray; 1.90 A; A/B/C/D/E/F=24-102.
DR PDBsum; 2L4N; -.
DR PDBsum; 5EKI; -.
DR AlphaFoldDB; O00585; -.
DR BMRB; O00585; -.
DR SMR; O00585; -.
DR BioGRID; 112269; 36.
DR DIP; DIP-5854N; -.
DR IntAct; O00585; 37.
DR MINT; O00585; -.
DR STRING; 9606.ENSP00000259607; -.
DR iPTMnet; O00585; -.
DR PhosphoSitePlus; O00585; -.
DR BioMuta; CCL21; -.
DR jPOST; O00585; -.
DR MassIVE; O00585; -.
DR PaxDb; O00585; -.
DR PeptideAtlas; O00585; -.
DR PRIDE; O00585; -.
DR ProteomicsDB; 47987; -.
DR Antibodypedia; 3907; 567 antibodies from 38 providers.
DR DNASU; 6366; -.
DR Ensembl; ENST00000259607.7; ENSP00000259607.2; ENSG00000137077.8.
DR GeneID; 6366; -.
DR KEGG; hsa:6366; -.
DR MANE-Select; ENST00000259607.7; ENSP00000259607.2; NM_002989.4; NP_002980.1.
DR UCSC; uc003zvo.5; human.
DR CTD; 6366; -.
DR DisGeNET; 6366; -.
DR GeneCards; CCL21; -.
DR HGNC; HGNC:10620; CCL21.
DR HPA; ENSG00000137077; Tissue enriched (lymphoid).
DR MIM; 602737; gene.
DR neXtProt; NX_O00585; -.
DR OpenTargets; ENSG00000137077; -.
DR PharmGKB; PA35552; -.
DR VEuPathDB; HostDB:ENSG00000137077; -.
DR eggNOG; ENOG502S8D1; Eukaryota.
DR GeneTree; ENSGT01050000244920; -.
DR InParanoid; O00585; -.
DR OMA; CKRTEQP; -.
DR OrthoDB; 1542802at2759; -.
DR PhylomeDB; O00585; -.
DR TreeFam; TF338224; -.
DR PathwayCommons; O00585; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O00585; -.
DR SIGNOR; O00585; -.
DR BioGRID-ORCS; 6366; 15 hits in 1070 CRISPR screens.
DR ChiTaRS; CCL21; human.
DR GeneWiki; CCL21; -.
DR GenomeRNAi; 6366; -.
DR Pharos; O00585; Tbio.
DR PRO; PR:O00585; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O00585; protein.
DR Bgee; ENSG00000137077; Expressed in lymph node and 145 other tissues.
DR ExpressionAtlas; O00585; baseline and differential.
DR Genevisible; O00585; 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:0031732; F:CCR7 chemokine receptor binding; ISS:BHF-UCL.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0042379; F:chemokine receptor binding; IDA:UniProtKB.
DR GO; GO:0090630; P:activation of GTPase activity; IDA:BHF-UCL.
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:0048469; P:cell maturation; ISS:BHF-UCL.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:1990869; P:cellular response to chemokine; ISS:BHF-UCL.
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:0038116; P:chemokine (C-C motif) ligand 21 signaling pathway; ISS:BHF-UCL.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0002407; P:dendritic cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0097026; P:dendritic cell dendrite assembly; ISS:BHF-UCL.
DR GO; GO:0048245; P:eosinophil chemotaxis; IBA:GO_Central.
DR GO; GO:0001768; P:establishment of T cell polarity; IDA:BHF-UCL.
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:0001771; P:immunological synapse formation; ISS:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0035759; P:mesangial cell-matrix adhesion; IDA:BHF-UCL.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:2000548; P:negative regulation of dendritic cell dendrite assembly; ISS:BHF-UCL.
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:0030838; P:positive regulation of actin filament polymerization; IDA:BHF-UCL.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IDA:BHF-UCL.
DR GO; GO:2000147; P:positive regulation of cell motility; IDA:BHF-UCL.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:UniProtKB.
DR GO; GO:0050921; P:positive regulation of chemotaxis; ISS:BHF-UCL.
DR GO; GO:0002606; P:positive regulation of dendritic cell antigen processing and presentation; ISS:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
DR GO; GO:0051491; P:positive regulation of filopodium assembly; IDA:BHF-UCL.
DR GO; GO:0010560; P:positive regulation of glycoprotein biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
DR GO; GO:0046330; P:positive regulation of JNK cascade; IDA:BHF-UCL.
DR GO; GO:2000529; P:positive regulation of myeloid dendritic cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IDA:BHF-UCL.
DR GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IDA:BHF-UCL.
DR GO; GO:0045860; P:positive regulation of protein kinase activity; IDA:BHF-UCL.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
DR GO; GO:0031274; P:positive regulation of pseudopodium assembly; IDA:BHF-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; ISS:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISS:BHF-UCL.
DR GO; GO:2000406; P:positive regulation of T cell migration; IDA:MGI.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0034695; P:response to prostaglandin E; IDA:BHF-UCL.
DR GO; GO:0031529; P:ruffle organization; IDA:BHF-UCL.
DR GO; GO:0031295; P:T cell costimulation; ISS:BHF-UCL.
DR CDD; cd01119; Chemokine_CC_DCCL; 1.
DR DisProt; DP00765; -.
DR InterPro; IPR030593; CCL21.
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 PANTHER; PTHR12015:SF72; PTHR12015:SF72; 1.
DR Pfam; PF00048; IL8; 1.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 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:9300671"
FT CHAIN 24..134
FT /note="C-C motif chemokine 21"
FT /id="PRO_0000005220"
FT REGION 88..134
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..134
FT /note="C-terminal basic extension"
FT DISULFID 31..57
FT /evidence="ECO:0000269|PubMed:22221265"
FT DISULFID 32..75
FT /evidence="ECO:0000269|PubMed:22221265"
FT DISULFID 103..122
FT /evidence="ECO:0000255"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:5EKI"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:5EKI"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:2L4N"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:5EKI"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:5EKI"
FT HELIX 81..90
FT /evidence="ECO:0007829|PDB:5EKI"
SQ SEQUENCE 134 AA; 14646 MW; FB48C2F71CB4A9D2 CRC64;
MAQSLALSLL ILVLAFGIPR TQGSDGGAQD CCLKYSQRKI PAKVVRSYRK QEPSLGCSIP
AILFLPRKRS QAELCADPKE LWVQQLMQHL DKTPSPQKPA QGCRKDRGAS KTGKKGKGSK
GCKRTERSQT PKGP
