ID   CCL21_MACMU             Reviewed;         131 AA.
AC   Q8HYP5;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=C-C motif chemokine 21;
DE   AltName: Full=Small-inducible cytokine A21;
DE   Flags: Precursor;
GN   Name=CCL21;
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=12126650; DOI=10.1006/cyto.2002.0875;
RA   Basu S., Schaefer T.M., Ghosh M., Fuller C.L., Reinhart T.A.;
RT   "Molecular cloning and sequencing of 25 different rhesus macaque chemokine
RT   cDNAs reveals evolutionary conservation among C, CC, CXC, and CX3C families
RT   of chemokines.";
RL   Cytokine 18:140-148(2002).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Binds to CCR7. Interacts with PDPN; relocalizes PDPN
CC       to the basolateral membrane. Interacts with TNFAIP6 (via Link domain).
CC       Interacts with GPR174. {ECO:0000250|UniProtKB:O00585,
CC       ECO:0000250|UniProtKB:P84444}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
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DR   EMBL; AF449275; AAN76079.1; -; mRNA.
DR   RefSeq; NP_001028027.1; NM_001032855.1.
DR   AlphaFoldDB; Q8HYP5; -.
DR   SMR; Q8HYP5; -.
DR   STRING; 9544.ENSMMUP00000070168; -.
DR   PaxDb; 9544-ENSMMUP00000021721; -.
DR   Ensembl; ENSMMUT00000082253.1; ENSMMUP00000070168.1; ENSMMUG00000063081.1.
DR   GeneID; 574183; -.
DR   KEGG; mcc:574183; -.
DR   CTD; 6366; -.
DR   VEuPathDB; HostDB:ENSMMUG00000063081; -.
DR   VGNC; VGNC:104885; CCL21.
DR   eggNOG; ENOG502S8D1; Eukaryota.
DR   GeneTree; ENSGT01100000263557; -.
DR   HOGENOM; CLU_141716_3_2_1; -.
DR   InParanoid; Q8HYP5; -.
DR   OMA; CKRTEQP; -.
DR   OrthoDB; 5265378at2759; -.
DR   TreeFam; TF338224; -.
DR   Proteomes; UP000006718; Chromosome 15.
DR   Bgee; ENSMMUG00000063081; Expressed in spleen and 16 other cell types or tissues.
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:0008009; F:chemokine activity; IBA:GO_Central.
DR   GO; GO:0042379; F:chemokine receptor binding; ISS:UniProtKB.
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:0071346; P:cellular response to type II interferon; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0002407; P:dendritic cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0001768; P:establishment of T cell polarity; IEA:Ensembl.
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:0035759; P:mesangial cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IEA:Ensembl.
DR   GO; GO:1903237; P:negative regulation of leukocyte tethering or rolling; IEA:Ensembl.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR   GO; GO:0030838; P:positive regulation of actin filament polymerization; IEA:Ensembl.
DR   GO; GO:0043123; P:positive regulation of canonical NF-kappaB signal transduction; IEA:Ensembl.
DR   GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR   GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR   GO; GO:0051491; P:positive regulation of filopodium assembly; IEA:Ensembl.
DR   GO; GO:0046330; P:positive regulation of JNK cascade; IEA:Ensembl.
DR   GO; GO:2000529; P:positive regulation of myeloid dendritic cell chemotaxis; IEA:Ensembl.
DR   GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR   GO; GO:0051897; P:positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction; IEA:Ensembl.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; IEA:Ensembl.
DR   GO; GO:2000406; P:positive regulation of T cell migration; IEA:Ensembl.
DR   GO; GO:0051209; P:release of sequestered calcium ion into cytosol; IEA:Ensembl.
DR   GO; GO:0034695; P:response to prostaglandin E; IEA:Ensembl.
DR   GO; GO:0031529; P:ruffle organization; IEA:Ensembl.
DR   CDD; cd01119; Chemokine_CC_DCCL; 1.
DR   Gene3D; 2.40.50.40; -; 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:SF72; C-C MOTIF CHEMOKINE 21; 1.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   Pfam; PF00048; IL8; 1.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 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..131
FT                   /note="C-C motif chemokine 21"
FT                   /id="PRO_0000005221"
FT   REGION          89..131
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        31..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        32..75
FT                   /evidence="ECO:0000250"
FT   DISULFID        103..119
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   131 AA;  14368 MW;  B8FFF8A7E2FECC1D CRC64;
     MAQSLALSLL ILVLAFGIPG TQGSDGGAQD CCLKYSQRKI PAKVVRSYRK QEPSLGCSIP
     AILFLPRKRS QAELCADPKE LWVQQLMQHL DKTPTPRKPV QGCRKDRGVP KNGKKGKGCK
     RTEQSQTPKG P
//