CXL11_HUMAN
ID CXL11_HUMAN Reviewed; 94 AA.
AC O14625; Q53YA3; Q92840;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 195.
DE RecName: Full=C-X-C motif chemokine 11;
DE AltName: Full=Beta-R1;
DE AltName: Full=H174;
DE AltName: Full=Interferon gamma-inducible protein 9;
DE Short=IP-9;
DE AltName: Full=Interferon-inducible T-cell alpha chemoattractant;
DE Short=I-TAC;
DE AltName: Full=Small-inducible cytokine B11;
DE Flags: Precursor;
GN Name=CXCL11; Synonyms=ITAC, SCYB11, SCYB9B;
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].
RC TISSUE=Astrocyte;
RX PubMed=8798467; DOI=10.1074/jbc.271.37.22878;
RA Rani M.R.S., Foster G.R., Leung S., Leaman D., Stark G.R., Ransohoff R.M.;
RT "Characterization of beta-R1, a gene that is selectively induced by
RT interferon beta (IFN-beta) compared with IFN-alpha.";
RL J. Biol. Chem. 271:22878-22884(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood monocyte;
RX PubMed=9370294; DOI=10.1016/s0378-1119(97)00330-2;
RA Jacobs K.A., Collins-Racie L.A., Colbert M., Duckett M., Golden-Fleet M.,
RA Kelleher K., Kriz R., LaVallie E.R., Merberg D., Spaulding V., Stover J.,
RA Williamson M.J., McCoy J.M.;
RT "A genetic selection for isolating cDNAs encoding secreted proteins.";
RL Gene 198:289-296(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Fetal astrocyte;
RX PubMed=9625760; DOI=10.1084/jem.187.12.2009;
RA Cole K.E., Strick C.A., Paradis T.J., Ogborne K.T., Loetscher M.,
RA Gladue R.P., Lin W., Boyd J.G., Moser B., Wood D.E., Sahagan B.G.,
RA Neote K.;
RT "Interferon-inducible T cell alpha chemoattractant (I-TAC): a novel non-ELR
RT CXC chemokine with potent activity on activated T cells through selective
RT high affinity binding to CXCR3.";
RL J. Exp. Med. 187:2009-2021(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 22-38, AND MASS
RP SPECTROMETRY.
RC TISSUE=Keratinocyte;
RX PubMed=10233762; DOI=10.1046/j.1523-1747.1999.00581.x;
RA Tensen C.P., Flier J., van der Raaij-Helmer E.M.H.,
RA Sampat-Sardjoepersad S., van der Schors R.C., Leurs R., Scheper R.J.,
RA Boorsma D.M., Willemze R.;
RT "Human IP-9: a keratinocyte derived high affinity CXC-chemokine ligand for
RT the IP-10/Mig receptor (CXCR3).";
RL J. Invest. Dermatol. 112:716-722(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Myeloma;
RX PubMed=10386863; DOI=10.1089/107999099313956;
RA Laich A.M., Meyer M., Werner E.R., Werner-Felmayer G.;
RT "Structure and expression of the human small cytokine B subfamily member 11
RT (SCYB11/formerly SCYB9B, alias I-TAC) gene cloned from IFN-gamma-treated
RT human monocytes (THP-1).";
RL J. Interferon Cytokine Res. 19:505-513(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Keratinocyte;
RX PubMed=10395932; DOI=10.1016/s0167-4781(99)00084-6;
RA Tensen C.P., Flier J., Rampersad S., Sampat-Sardjoepersad S., Scheper R.J.,
RA Boorsma D.M., Willemze R.;
RT "Genomic organization, sequence and transcriptional regulation of the human
RT CXCL 11 gene.";
RL Biochim. Biophys. Acta 1446:167-172(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow, Brain, and Liver;
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 [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 28-84.
RX PubMed=9730616; DOI=10.1159/000015043;
RA Erdel M., Laich A., Utermann G., Werner E.R., Werner-Felmayer G.;
RT "The human gene encoding SCYB9B, a putative novel CXC chemokine, maps to
RT human chromosome 4q21 like the closely related genes for MIG (SCYB9) and
RT INP10 (SCYB10).";
RL Cytogenet. Cell Genet. 81:271-272(1998).
RN [10]
RP CITRULLINATION AT ARG-27.
RX PubMed=18645041; DOI=10.1182/blood-2008-04-149039;
RA Loos T., Mortier A., Gouwy M., Ronsse I., Put W., Lenaerts J.P.,
RA Van Damme J., Proost P.;
RT "Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a
RT naturally occurring posttranslational modification of chemokines and new
RT dimension of immunoregulation.";
RL Blood 112:2648-2656(2008).
RN [11]
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 [12]
RP STRUCTURE BY NMR OF 22-94, AND DISULFIDE BONDS.
RX PubMed=15273303; DOI=10.1110/ps.04791404;
RA Booth V., Clark-Lewis I., Sykes B.D.;
RT "NMR structure of CXCR3 binding chemokine CXCL11 (ITAC).";
RL Protein Sci. 13:2022-2028(2004).
CC -!- FUNCTION: Chemotactic for interleukin-activated T-cells but not
CC unstimulated T-cells, neutrophils or monocytes. Induces calcium release
CC in activated T-cells. Binds to CXCR3. May play an important role in CNS
CC diseases which involve T-cell recruitment. May play a role in skin
CC immune responses.
CC -!- SUBUNIT: Interacts with TNFAIP6 (via Link domain).
CC {ECO:0000269|PubMed:27044744}.
CC -!- INTERACTION:
CC O14625; Q99616: CCL13; NbExp=2; IntAct=EBI-2871971, EBI-725342;
CC O14625; O00175: CCL24; NbExp=2; IntAct=EBI-2871971, EBI-16803966;
CC O14625; Q9Y258: CCL26; NbExp=2; IntAct=EBI-2871971, EBI-7783416;
CC O14625; P13501: CCL5; NbExp=2; IntAct=EBI-2871971, EBI-2848366;
CC O14625; P48061: CXCL12; NbExp=3; IntAct=EBI-2871971, EBI-3913254;
CC O14625; O95715: CXCL14; NbExp=2; IntAct=EBI-2871971, EBI-2798068;
CC O14625; P27487: DPP4; NbExp=2; IntAct=EBI-2871971, EBI-2871277;
CC O14625; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-2871971, EBI-742948;
CC O14625; P02776: PF4; NbExp=2; IntAct=EBI-2871971, EBI-2565740;
CC O14625; P10720: PF4V1; NbExp=2; IntAct=EBI-2871971, EBI-1223944;
CC PRO_0000005106; P98066: TNFAIP6; NbExp=2; IntAct=EBI-11711364, EBI-11700693;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: High levels in peripheral blood leukocytes,
CC pancreas and liver astrocytes. Moderate levels in thymus, spleen and
CC lung. Low levels in placenta, prostate and small intestine. Also found
CC in epidermal basal layer keratinocytes in skin disorders.
CC -!- INDUCTION: By IFNG/IFN-gamma and IFNB1/IFN-beta. Induction by IFNG/IFN-
CC gamma is enhanced by TNF in monocytes, dermal fibroblasts and
CC endothelial cells, and by IL1/interleukin-1 in astrocytes.
CC -!- MASS SPECTROMETRY: Mass=8303; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:10233762};
CC -!- SIMILARITY: Belongs to the intercrine alpha (chemokine CxC) family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB17374.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Wikipedia; Note=CXCL11 entry;
CC URL="https://en.wikipedia.org/wiki/CXCL11";
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DR EMBL; U59286; AAB17374.1; ALT_INIT; mRNA.
DR EMBL; AF002985; AAC51845.1; -; mRNA.
DR EMBL; AF030514; AAC39775.1; -; mRNA.
DR EMBL; Y15220; CAA75510.1; -; mRNA.
DR EMBL; U66096; AAD38867.1; -; mRNA.
DR EMBL; AF077867; AAD38327.1; -; Genomic_DNA.
DR EMBL; Y15221; CAB51859.1; -; Genomic_DNA.
DR EMBL; BT006787; AAP35433.1; -; mRNA.
DR EMBL; BC005292; AAH05292.1; -; mRNA.
DR EMBL; BC012532; AAH12532.1; -; mRNA.
DR EMBL; BC110986; AAI10987.1; -; mRNA.
DR EMBL; AF053972; AAD10206.1; -; Genomic_DNA.
DR CCDS; CCDS3574.1; -.
DR RefSeq; NP_001289052.1; NM_001302123.1.
DR RefSeq; NP_005400.1; NM_005409.4.
DR PDB; 1RJT; NMR; -; A=22-94.
DR PDBsum; 1RJT; -.
DR AlphaFoldDB; O14625; -.
DR SMR; O14625; -.
DR BioGRID; 112275; 23.
DR DIP; DIP-5890N; -.
DR IntAct; O14625; 26.
DR MINT; O14625; -.
DR STRING; 9606.ENSP00000306884; -.
DR iPTMnet; O14625; -.
DR PhosphoSitePlus; O14625; -.
DR BioMuta; CXCL11; -.
DR MassIVE; O14625; -.
DR PaxDb; O14625; -.
DR PeptideAtlas; O14625; -.
DR PRIDE; O14625; -.
DR ProteomicsDB; 48123; -.
DR ABCD; O14625; 31 sequenced antibodies.
DR Antibodypedia; 4090; 581 antibodies from 33 providers.
DR DNASU; 6373; -.
DR Ensembl; ENST00000306621.8; ENSP00000306884.3; ENSG00000169248.13.
DR Ensembl; ENST00000503860.1; ENSP00000425819.1; ENSG00000169248.13.
DR GeneID; 6373; -.
DR KEGG; hsa:6373; -.
DR MANE-Select; ENST00000306621.8; ENSP00000306884.3; NM_005409.5; NP_005400.1.
DR UCSC; uc003hjm.4; human.
DR CTD; 6373; -.
DR DisGeNET; 6373; -.
DR GeneCards; CXCL11; -.
DR HGNC; HGNC:10638; CXCL11.
DR HPA; ENSG00000169248; Tissue enhanced (lymphoid).
DR MIM; 604852; gene.
DR neXtProt; NX_O14625; -.
DR OpenTargets; ENSG00000169248; -.
DR PharmGKB; PA35569; -.
DR VEuPathDB; HostDB:ENSG00000169248; -.
DR eggNOG; ENOG502SGFE; Eukaryota.
DR GeneTree; ENSGT00530000064263; -.
DR HOGENOM; CLU_143902_2_3_1; -.
DR InParanoid; O14625; -.
DR OMA; IFCATIA; -.
DR OrthoDB; 1542450at2759; -.
DR PhylomeDB; O14625; -.
DR TreeFam; TF333433; -.
DR PathwayCommons; O14625; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-418594; G alpha (i) signalling events.
DR SignaLink; O14625; -.
DR SIGNOR; O14625; -.
DR BioGRID-ORCS; 6373; 29 hits in 1074 CRISPR screens.
DR EvolutionaryTrace; O14625; -.
DR GeneWiki; CXCL11; -.
DR GenomeRNAi; 6373; -.
DR Pharos; O14625; Tbio.
DR PRO; PR:O14625; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; O14625; protein.
DR Bgee; ENSG00000169248; Expressed in vermiform appendix and 117 other tissues.
DR Genevisible; O14625; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0045236; F:CXCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0048248; F:CXCR3 chemokine receptor binding; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IMP:UniProtKB.
DR GO; GO:0007189; P:adenylate cyclase-activating G protein-coupled receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0006935; P:chemotaxis; IDA:UniProtKB.
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:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:UniProtKB.
DR GO; GO:0042127; P:regulation of cell population proliferation; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0010818; P:T cell chemotaxis; IMP:UniProtKB.
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; IPR027221; CXCL11.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR10179; PTHR10179; 1.
DR PANTHER; PTHR10179:SF28; PTHR10179:SF28; 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; Citrullination; Cytokine;
KW Direct protein sequencing; Disulfide bond; Inflammatory response;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000269|PubMed:10233762"
FT CHAIN 22..94
FT /note="C-X-C motif chemokine 11"
FT /id="PRO_0000005106"
FT MOD_RES 27
FT /note="Citrulline; by PAD2"
FT /evidence="ECO:0000269|PubMed:18645041"
FT DISULFID 30..57
FT /evidence="ECO:0000269|PubMed:15273303"
FT DISULFID 32..74
FT /evidence="ECO:0000269|PubMed:15273303"
FT VARIANT 55
FT /note="N -> S (in dbSNP:rs4859596)"
FT /id="VAR_048700"
FT CONFLICT 69..72
FT /note="NKGQ -> IRK (in Ref. 1; AAB17374)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="K -> NRA (in Ref. 1; AAB17374)"
FT /evidence="ECO:0000305"
FT CONFLICT 89
FT /note="V -> A (in Ref. 1; AAB17374)"
FT /evidence="ECO:0000305"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1RJT"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:1RJT"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:1RJT"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:1RJT"
SQ SEQUENCE 94 AA; 10365 MW; 9D9D8585749EA4CE CRC64;
MSVKGMAIAL AVILCATVVQ GFPMFKRGRC LCIGPGVKAV KVADIEKASI MYPSNNCDKI
EVIITLKENK GQRCLNPKSK QARLIIKKVE RKNF
