XCL1_HUMAN
ID XCL1_HUMAN Reviewed; 114 AA.
AC P47992; Q52MA8;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Lymphotactin;
DE AltName: Full=ATAC;
DE AltName: Full=C motif chemokine 1;
DE AltName: Full=Cytokine SCM-1;
DE AltName: Full=Lymphotaxin;
DE AltName: Full=SCM-1-alpha;
DE AltName: Full=Small-inducible cytokine C1;
DE AltName: Full=XC chemokine ligand 1;
DE Flags: Precursor;
GN Name=XCL1; Synonyms=LTN, SCYC1;
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=7602097;
RA Kennedy J., Kelner G.S., Kleyensteuber S., Schall T.J., Weiss M.C.,
RA Yssel H., Schneider P.V., Cocks B.G., Bacon K.B., Zlotnik A.;
RT "Molecular cloning and functional characterization of human lymphotactin.";
RL J. Immunol. 155:203-209(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=7875320; DOI=10.1016/0014-5793(95)00093-o;
RA Yoshida T., Imai T., Kakizaki M., Nishimura M., Yoshie O.;
RT "Molecular cloning of a novel C or gamma type chemokine, SCM-1.";
RL FEBS Lett. 360:155-159(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Peripheral blood;
RX PubMed=7615002; DOI=10.1002/eji.1830250638;
RA Mueller S., Dorner B., Korthauer U., Mages H.W., D'Apuzzo M., Senger G.,
RA Kroczek R.A.;
RT "Cloning of ATAC, an activation-induced, chemokine-related molecule
RT exclusively expressed in CD8+ T lymphocytes.";
RL Eur. J. Immunol. 25:1744-1748(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Placenta;
RX PubMed=8849694; DOI=10.1016/0014-5793(96)01004-6;
RA Yoshida T., Imai T., Takagi S., Nishimura M., Ishikawa I., Yaoi T.,
RA Yoshie O.;
RT "Structure and expression of two highly related genes encoding SCM-1/human
RT lymphotactin.";
RL FEBS Lett. 395:82-88(1996).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 [7]
RP STRUCTURE BY NMR OF 22-114, AND DISULFIDE BOND.
RX PubMed=11601972; DOI=10.1021/bi011106p;
RA Kuloglu E.S., McCaslin D.R., Kitabwalla M., Pauza C.D., Markley J.L.,
RA Volkman B.F.;
RT "Monomeric solution structure of the prototypical 'C' chemokine
RT lymphotactin.";
RL Biochemistry 40:12486-12496(2001).
CC -!- FUNCTION: Chemotactic activity for lymphocytes but not for monocytes or
CC neutrophils. In thymus, mediates medullary accumulation of thymic
CC dendritic cells and contributes to regulatoy T cell development,
CC playing a role in self-tolerance establishment.
CC {ECO:0000250|UniProtKB:P47993}.
CC -!- INTERACTION:
CC P47992; Q99616: CCL13; NbExp=2; IntAct=EBI-10209901, EBI-725342;
CC P47992; Q9Y258: CCL26; NbExp=2; IntAct=EBI-10209901, EBI-7783416;
CC P47992; P13501: CCL5; NbExp=3; IntAct=EBI-10209901, EBI-2848366;
CC P47992; P48061: CXCL12; NbExp=2; IntAct=EBI-10209901, EBI-3913254;
CC P47992; P02776: PF4; NbExp=2; IntAct=EBI-10209901, EBI-2565740;
CC P47992; P10720: PF4V1; NbExp=2; IntAct=EBI-10209901, EBI-1223944;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Highest level in spleen, lower in peripheral
CC leukocytes and very low levels in lung, colon and small intestine.
CC -!- SIMILARITY: Belongs to the intercrine gamma family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=XCL1 entry;
CC URL="https://en.wikipedia.org/wiki/XCL1";
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DR EMBL; U23772; AAC50164.1; -; mRNA.
DR EMBL; D43768; BAA07825.1; -; mRNA.
DR EMBL; X86474; CAA60198.1; -; mRNA.
DR EMBL; D63790; BAA09859.1; -; Genomic_DNA.
DR EMBL; AL031736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069817; AAH69817.1; -; mRNA.
DR EMBL; BC070309; AAH70309.1; -; mRNA.
DR CCDS; CCDS1274.1; -.
DR PIR; S60650; ETHUL.
DR RefSeq; NP_002986.1; NM_002995.2.
DR RefSeq; XP_011508167.1; XM_011509865.2.
DR PDB; 1J8I; NMR; -; A=22-114.
DR PDB; 1J9O; NMR; -; A=22-114.
DR PDB; 2HDM; NMR; -; A=23-114.
DR PDB; 2JP1; NMR; -; A/B=22-114.
DR PDB; 2N54; NMR; -; A/B=22-114.
DR PDB; 2NYZ; X-ray; 2.60 A; D/E=22-114.
DR PDBsum; 1J8I; -.
DR PDBsum; 1J9O; -.
DR PDBsum; 2HDM; -.
DR PDBsum; 2JP1; -.
DR PDBsum; 2N54; -.
DR PDBsum; 2NYZ; -.
DR AlphaFoldDB; P47992; -.
DR BMRB; P47992; -.
DR SMR; P47992; -.
DR BioGRID; 112277; 25.
DR DIP; DIP-29876N; -.
DR IntAct; P47992; 25.
DR STRING; 9606.ENSP00000356792; -.
DR MoonDB; P47992; Curated.
DR MoonProt; P47992; -.
DR GlyGen; P47992; 1 site, 1 O-linked glycan (1 site).
DR PhosphoSitePlus; P47992; -.
DR BioMuta; XCL1; -.
DR DMDM; 1346471; -.
DR MassIVE; P47992; -.
DR PaxDb; P47992; -.
DR PeptideAtlas; P47992; -.
DR PRIDE; P47992; -.
DR Antibodypedia; 20539; 438 antibodies from 34 providers.
DR DNASU; 6375; -.
DR Ensembl; ENST00000367818.4; ENSP00000356792.3; ENSG00000143184.5.
DR GeneID; 6375; -.
DR KEGG; hsa:6375; -.
DR MANE-Select; ENST00000367818.4; ENSP00000356792.3; NM_002995.3; NP_002986.1.
DR UCSC; uc001gfo.2; human.
DR CTD; 6375; -.
DR DisGeNET; 6375; -.
DR GeneCards; XCL1; -.
DR HGNC; HGNC:10645; XCL1.
DR HPA; ENSG00000143184; Tissue enhanced (lymphoid).
DR MIM; 600250; gene.
DR neXtProt; NX_P47992; -.
DR OpenTargets; ENSG00000143184; -.
DR PharmGKB; PA35575; -.
DR VEuPathDB; HostDB:ENSG00000143184; -.
DR eggNOG; ENOG502S6ZP; Eukaryota.
DR GeneTree; ENSGT01050000244920; -.
DR HOGENOM; CLU_141716_2_0_1; -.
DR InParanoid; P47992; -.
DR OMA; GIKICAD; -.
DR OrthoDB; 1553663at2759; -.
DR PhylomeDB; P47992; -.
DR TreeFam; TF334888; -.
DR PathwayCommons; P47992; -.
DR Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR Reactome; R-HSA-416476; G alpha (q) signalling events.
DR SignaLink; P47992; -.
DR SIGNOR; P47992; -.
DR BioGRID-ORCS; 6375; 73 hits in 978 CRISPR screens.
DR EvolutionaryTrace; P47992; -.
DR GenomeRNAi; 6375; -.
DR Pharos; P47992; Tbio.
DR PRO; PR:P47992; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P47992; protein.
DR Bgee; ENSG00000143184; Expressed in granulocyte and 83 other tissues.
DR Genevisible; P47992; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; ISS:BHF-UCL.
DR GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR GO; GO:0008009; F:chemokine activity; IDA:BHF-UCL.
DR GO; GO:0042379; F:chemokine receptor binding; IDA:BHF-UCL.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:BHF-UCL.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0007267; P:cell-cell signaling; IDA: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:0071353; P:cellular response to interleukin-4; ISS:BHF-UCL.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; ISS:BHF-UCL.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
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:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0035782; P:mature natural killer cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:BHF-UCL.
DR GO; GO:0002725; P:negative regulation of T cell cytokine production; IDA:BHF-UCL.
DR GO; GO:2000518; P:negative regulation of T-helper 1 cell activation; IDA:BHF-UCL.
DR GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IC:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR GO; GO:2000538; P:positive regulation of B cell chemotaxis; ISS:BHF-UCL.
DR GO; GO:2000563; P:positive regulation of CD4-positive, alpha-beta T cell proliferation; ISS:BHF-UCL.
DR GO; GO:2000566; P:positive regulation of CD8-positive, alpha-beta T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR GO; GO:2000513; P:positive regulation of granzyme A production; IDA:BHF-UCL.
DR GO; GO:0071663; P:positive regulation of granzyme B production; IDA:BHF-UCL.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:2000558; P:positive regulation of immunoglobulin production in mucosal tissue; ISS:BHF-UCL.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
DR GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; ISS:BHF-UCL.
DR GO; GO:2000503; P:positive regulation of natural killer cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; ISS:BHF-UCL.
DR GO; GO:0051281; P:positive regulation of release of sequestered calcium ion into cytosol; IDA:BHF-UCL.
DR GO; GO:0010820; P:positive regulation of T cell chemotaxis; IDA:BHF-UCL.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; ISS:BHF-UCL.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; IDA:BHF-UCL.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:BHF-UCL.
DR GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; ISS:BHF-UCL.
DR GO; GO:2000412; P:positive regulation of thymocyte migration; ISS:BHF-UCL.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IDA:BHF-UCL.
DR GO; GO:0050727; P:regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:BHF-UCL.
DR GO; GO:0009615; P:response to virus; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; IC:BHF-UCL.
DR CDD; cd00271; Chemokine_C; 1.
DR DisProt; DP02957; -.
DR InterPro; IPR039809; Chemokine_b/g/d.
DR InterPro; IPR001811; Chemokine_IL8-like_dom.
DR InterPro; IPR008105; Chemokine_XCL1/XCL2.
DR InterPro; IPR036048; Interleukin_8-like_sf.
DR PANTHER; PTHR12015; PTHR12015; 1.
DR PANTHER; PTHR12015:SF101; PTHR12015:SF101; 1.
DR Pfam; PF00048; IL8; 1.
DR PRINTS; PR01731; LYMPHOTACTIN.
DR SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Cytokine; Disulfide bond; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..114
FT /note="Lymphotactin"
FT /id="PRO_0000005248"
FT REGION 91..114
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 32..69
FT /evidence="ECO:0000269|PubMed:11601972"
FT STRAND 33..35
FT /evidence="ECO:0007829|PDB:1J8I"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2NYZ"
FT STRAND 45..50
FT /evidence="ECO:0007829|PDB:1J8I"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:2NYZ"
FT STRAND 57..62
FT /evidence="ECO:0007829|PDB:2NYZ"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:2NYZ"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:2NYZ"
FT HELIX 75..82
FT /evidence="ECO:0007829|PDB:2NYZ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:2NYZ"
FT TURN 88..91
FT /evidence="ECO:0007829|PDB:1J8I"
SQ SEQUENCE 114 AA; 12517 MW; FABA16063C3FC165 CRC64;
MRLLILALLG ICSLTAYIVE GVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF
ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG
