ID I3N2N1_ICTTR Unreviewed; 133 AA.
AC I3N2N1;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 58.
DE SubName: Full=C-C motif chemokine ligand 21 {ECO:0000313|Ensembl:ENSSTOP00000018627.2};
GN Name=CCL21 {ECO:0000313|Ensembl:ENSSTOP00000018627.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000018627.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000018627.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000256|ARBA:ARBA00010868}.
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DR EMBL; AGTP01043530; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; I3N2N1; -.
DR STRING; 43179.ENSSTOP00000018627; -.
DR Ensembl; ENSSTOT00000028015.2; ENSSTOP00000018627.2; ENSSTOG00000021913.2.
DR eggNOG; ENOG502S8D1; Eukaryota.
DR GeneTree; ENSGT01100000263557; -.
DR HOGENOM; CLU_141716_3_2_1; -.
DR InParanoid; I3N2N1; -.
DR OMA; CKRTEQP; -.
DR TreeFam; TF338224; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0008009; F:chemokine activity; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0035759; P:mesangial cell-matrix adhesion; IEA:Ensembl.
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: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; IEA:Ensembl.
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 Gene3D; 2.40.50.40; -; 1.
DR InterPro; IPR039809; Chemokine_b/g/d.
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 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Cytokine {ECO:0000256|ARBA:ARBA00022514};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..133
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012113213"
FT DOMAIN 28..90
FT /note="Chemokine interleukin-8-like"
FT /evidence="ECO:0000259|SMART:SM00199"
FT REGION 88..133
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 133 AA; 14874 MW; F11F08EF1E2F0FDA CRC64;
MAQTLALSLL ILVLALCVPW TQGSDGGAQD CCLKYSQRKI PYKVVRGYRK QEASLGCPIP
AILFLPQKRS QPELCGDPKE AWVQQLMKRL DKPPAPRKEG QGCRKDRETQ KPGKKRKGSK
GCKRTEEPRT PKG
//