CXL13_MOUSE
ID CXL13_MOUSE Reviewed; 109 AA.
AC O55038;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=C-X-C motif chemokine 13;
DE AltName: Full=B lymphocyte chemoattractant;
DE AltName: Full=CXC chemokine BLC;
DE AltName: Full=Small-inducible cytokine B13;
DE Flags: Precursor;
GN Name=Cxcl13; Synonyms=Blc, Scyb13;
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], AND PROTEIN SEQUENCE OF N-TERMINUS.
RC STRAIN=C57BL/6J;
RX PubMed=9486651; DOI=10.1038/35876;
RA Gunn M.D., Ngo V.N., Ansel K.M., Ekland E.H., Cyster J.G., Williams L.T.;
RT "A B-cell-homing chemokine made in lymphoid follicles activates Burkitt's
RT lymphoma receptor-1.";
RL Nature 391:799-803(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon;
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: Strongly chemotactic for B-lymphocytes, weakly for spleen
CC monocytes and macrophages but no chemotactic activity for granulocytes.
CC Binds to BLR1/CXCR5. May play a role in directing the migration of B-
CC lymphocytes to follicles in secondary lymphoid organs.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Found in spleen (B-cell-rich zone or follicles),
CC Peyer patches (strongest within germinal centers and extending to the
CC mantle zone) and lymph nodes (in reticular pattern in follicles).
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
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DR EMBL; AF044196; AAC14401.1; -; mRNA.
DR EMBL; BC012965; AAH12965.1; -; mRNA.
DR CCDS; CCDS19447.1; -.
DR RefSeq; NP_061354.1; NM_018866.2.
DR PDB; 5IZB; NMR; -; A=22-109.
DR PDB; 5L7M; NMR; -; A=22-109.
DR PDBsum; 5IZB; -.
DR PDBsum; 5L7M; -.
DR AlphaFoldDB; O55038; -.
DR BMRB; O55038; -.
DR SMR; O55038; -.
DR DIP; DIP-57395N; -.
DR IntAct; O55038; 4.
DR MINT; O55038; -.
DR STRING; 10090.ENSMUSP00000023840; -.
DR iPTMnet; O55038; -.
DR PhosphoSitePlus; O55038; -.
DR PaxDb; O55038; -.
DR PRIDE; O55038; -.
DR ProteomicsDB; 277932; -.
DR Antibodypedia; 13544; 556 antibodies from 39 providers.
DR DNASU; 55985; -.
DR Ensembl; ENSMUST00000023840; ENSMUSP00000023840; ENSMUSG00000023078.
DR GeneID; 55985; -.
DR KEGG; mmu:55985; -.
DR UCSC; uc008yfb.1; mouse.
DR CTD; 10563; -.
DR MGI; MGI:1888499; Cxcl13.
DR VEuPathDB; HostDB:ENSMUSG00000023078; -.
DR eggNOG; ENOG502SEXJ; Eukaryota.
DR GeneTree; ENSGT00530000064292; -.
DR HOGENOM; CLU_143902_2_0_1; -.
DR InParanoid; O55038; -.
DR OMA; VNPDAPW; -.
DR OrthoDB; 1510748at2759; -.
DR PhylomeDB; O55038; -.
DR TreeFam; TF335204; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 55985; 2 hits in 74 CRISPR screens.
DR PRO; PR:O55038; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O55038; protein.
DR Bgee; ENSMUSG00000023078; Expressed in peripheral lymph node and 133 other tissues.
DR ExpressionAtlas; O55038; baseline and differential.
DR Genevisible; O55038; MM.
DR GO; GO:0005576; C:extracellular region; ISS:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0031735; F:CCR10 chemokine receptor binding; ISS:BHF-UCL.
DR GO; GO:0008009; F:chemokine activity; IDA:BHF-UCL.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0048248; F:CXCR3 chemokine receptor binding; ISS:BHF-UCL.
DR GO; GO:0031724; F:CXCR5 chemokine receptor binding; IDA:BHF-UCL.
DR GO; GO:0017134; F:fibroblast growth factor binding; ISS:BHF-UCL.
DR GO; GO:0008201; F:heparin binding; ISS:BHF-UCL.
DR GO; GO:0048018; F:receptor ligand activity; ISS:BHF-UCL.
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; ISO:MGI.
DR GO; GO:0035754; P:B cell chemotaxis; IMP:BHF-UCL.
DR GO; GO:0035769; P:B cell chemotaxis across high endothelial venule; IDA:BHF-UCL.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; ISO:MGI.
DR GO; GO:0007267; P:cell-cell signaling; ISS:BHF-UCL.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0042742; P:defense response to bacterium; ISS:BHF-UCL.
DR GO; GO:0035768; P:endothelial cell chemotaxis to fibroblast growth factor; ISS:BHF-UCL.
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:0048535; P:lymph node development; IDA:BHF-UCL.
DR GO; GO:0002518; P:lymphocyte chemotaxis across high endothelial venule; IMP:BHF-UCL.
DR GO; GO:2000545; P:negative regulation of endothelial cell chemotaxis to fibroblast growth factor; ISO:MGI.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0033634; P:positive regulation of cell-cell adhesion mediated by integrin; IDA:BHF-UCL.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; ISS:BHF-UCL.
DR GO; GO:0033625; P:positive regulation of integrin activation; IDA:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; ISS:BHF-UCL.
DR CDD; cd00273; Chemokine_CXC; 1.
DR InterPro; IPR001089; Chemokine_CXC.
DR InterPro; IPR018048; Chemokine_CXC_CS.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR033899; CXC_Chemokine_domain.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR10179; PTHR10179; 1.
DR Pfam; PF00048; IL8; 1.
DR PRINTS; PR00437; SMALLCYTKCXC.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
DR PROSITE; PS00471; SMALL_CYTOKINES_CXC; 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..21
FT /evidence="ECO:0000269|PubMed:9486651"
FT CHAIN 22..109
FT /note="C-X-C motif chemokine 13"
FT /id="PRO_0000005114"
FT DISULFID 32..59
FT /evidence="ECO:0000250"
FT DISULFID 34..75
FT /evidence="ECO:0000250"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:5IZB"
FT TURN 44..46
FT /evidence="ECO:0007829|PDB:5IZB"
FT STRAND 47..53
FT /evidence="ECO:0007829|PDB:5IZB"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:5IZB"
FT STRAND 63..68
FT /evidence="ECO:0007829|PDB:5IZB"
FT STRAND 73..76
FT /evidence="ECO:0007829|PDB:5IZB"
FT HELIX 81..89
FT /evidence="ECO:0007829|PDB:5IZB"
SQ SEQUENCE 109 AA; 11927 MW; F5F8AF4411C56BD3 CRC64;
MRLSTATLLL LLASCLSPGH GILEAHYTNL KCRCSGVIST VVGLNIIDRI QVTPPGNGCP
KTEVVIWTKM KKVICVNPRA KWLQRLLRHV QSKSLSSTPQ APVSKRRAA
