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   04-NOV-2026, entry version 204.
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; DOI=10.4049/jimmunol.155.1.203;
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_002995.3.
DR   RefSeq; XP_054194116.1; XM_054338141.1.
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   PDB; 9AST; EM; 3.07 A; L=22-114.
DR   AlphaFoldDB; P47992; -.
DR   BMRB; P47992; -.
DR   EMDB; EMD-43825; -.
DR   MDposit; P47992; -.
DR   SMR; P47992; -.
DR   BioGRID; 112277; 26.
DR   DIP; DIP-29876N; -.
DR   FunCoup; P47992; 622.
DR   IntAct; P47992; 26.
DR   NDEx; IQUERY-CP-XCL1; 4 NDEx IQuery Curated Pathways.
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; 9606-ENSP00000356792; -.
DR   PeptideAtlas; P47992; -.
DR   Antibodypedia; 20539; 471 antibodies from 38 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   AGR; HGNC:10645; -.
DR   ClinPGx; PA35575; -.
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   OpenTargets; ENSG00000143184; -.
DR   VEuPathDB; HostDB:ENSG00000143184; -.
DR   eggNOG; ENOG502S6ZP; Eukaryota.
DR   GeneTree; ENSGT01130000278316; -.
DR   HOGENOM; CLU_141716_2_0_1; -.
DR   InParanoid; P47992; -.
DR   OMA; ADPEVNW; -.
DR   OrthoDB; 9906867at2759; -.
DR   PAN-GO; P47992; 8 GO annotations based on evolutionary models.
DR   PhylomeDB; P47992; -.
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   Agora; ENSG00000143184; -.
DR   BioGRID-ORCS; 6375; 75 hits in 1032 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 84 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; 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; IBA:GO_Central.
DR   GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; IDA:BHF-UCL.
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:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0035782; P:mature natural killer cell chemotaxis; IDA:BHF-UCL.
DR   GO; GO:2000562; P:negative regulation of CD4-positive, alpha-beta T cell proliferation; IDA:BHF-UCL.
DR   GO; GO:0045892; P:negative regulation of DNA-templated transcription; 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:0032689; P:negative regulation of type II interferon production; IDA:BHF-UCL.
DR   GO; GO:0030593; P:neutrophil chemotaxis; TAS:BHF-UCL.
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:0030335; P:positive regulation of cell migration; 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: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:0045944; P:positive regulation of transcription by RNA polymerase II; IDA: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   FunFam; 2.40.50.40:FF:000023; Lymphotactin isoform X1; 1.
DR   Gene3D; 2.40.50.40; -; 1.
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:SF101; CYTOKINE SCM-1 BETA-RELATED; 1.
DR   PANTHER; PTHR12015; SMALL INDUCIBLE CYTOKINE A; 1.
DR   Pfam; PF00048; IL8; 1.
DR   PRINTS; PR01731; LYMPHOTACTIN.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; Interleukin 8-like chemokines; 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   COMPBIAS        91..114
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        32..69
FT                   /evidence="ECO:0000269|PubMed:11601972"
FT   STRAND          29..31
FT                   /evidence="ECO:0007829|PDB:9AST"
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
//