Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P47992 (XCL1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 127. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lymphotactin
Alternative name(s):
ATAC
C motif chemokine 1
Cytokine SCM-1
Lymphotaxin
SCM-1-alpha
Small-inducible cytokine C1
XC chemokine ligand 1
Gene names
Name:XCL1
Synonyms:LTN, SCYC1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length114 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chemotactic activity for lymphocytes but not for monocytes or neutrophils.

Subcellular location

Secreted.

Tissue specificity

Highest level in spleen, lower in peripheral leukocytes and very low levels in lung, colon and small intestine.

Sequence similarities

Belongs to the intercrine gamma family.

Ontologies

Keywords
   Biological processChemotaxis
   Cellular componentSecreted
   DomainSignal
   Molecular functionCytokine
   PTMDisulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell-cell signaling

Inferred from direct assay Ref.1. Source: BHF-UCL

cellular response to interleukin-4

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular response to transforming growth factor beta stimulus

Inferred from sequence or structural similarity. Source: BHF-UCL

immune response

Inferred from electronic annotation. Source: InterPro

mature natural killer cell chemotaxis

Inferred from direct assay PubMed 9029087. Source: BHF-UCL

negative regulation of CD4-positive, alpha-beta T cell proliferation

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of T cell cytokine production

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of T-helper 1 cell activation

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of T-helper 1 type immune response

Inferred by curator PubMed 10887101. Source: BHF-UCL

negative regulation of interferon-gamma production

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of interleukin-2 production

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

neutrophil chemotaxis

Traceable author statement PubMed 11889129. Source: BHF-UCL

positive regulation of B cell chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of CD4-positive, alpha-beta T cell proliferation

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of CD8-positive, alpha-beta T cell proliferation

Inferred from direct assay PubMed 10887101. Source: BHF-UCL

positive regulation of T cell chemotaxis

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of T cell cytokine production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T cell mediated cytotoxicity

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

positive regulation of T-helper 1 cell cytokine production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of T-helper 2 cell cytokine production

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of granzyme A production

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

positive regulation of granzyme B production

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

positive regulation of immunoglobulin production in mucosal tissue

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of interleukin-10 production

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

positive regulation of leukocyte chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of natural killer cell chemotaxis

Inferred from direct assay PubMed 9029087. Source: BHF-UCL

positive regulation of neutrophil chemotaxis

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of release of sequestered calcium ion into cytosol

Inferred from direct assay Ref.1. Source: BHF-UCL

positive regulation of thymocyte migration

Inferred from sequence or structural similarity. Source: BHF-UCL

positive regulation of transforming growth factor beta production

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

regulation of inflammatory response

Inferred from direct assay PubMed 18832695. Source: BHF-UCL

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: BHF-UCL

response to virus

Inferred from direct assay PubMed 14734774. Source: BHF-UCL

signal transduction

Inferred by curator PubMed 9632725. Source: BHF-UCL

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionchemokine activity

Inferred from direct assay Ref.1. Source: BHF-UCL

chemokine receptor binding

Inferred from direct assay PubMed 9632725. Source: BHF-UCL

protein homodimerization activity

Inferred from direct assay PubMed 11889129. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 11493Lymphotactin
PRO_0000005248

Amino acid modifications

Disulfide bond32 ↔ 69 Ref.7

Secondary structure

.................. 114
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P47992 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: FABA16063C3FC165

FASTA11412,517
        10         20         30         40         50         60 
MRLLILALLG ICSLTAYIVE GVGSEVSDKR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF 

        70         80         90        100        110 
ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning and functional characterization of human lymphotactin."
Kennedy J., Kelner G.S., Kleyensteuber S., Schall T.J., Weiss M.C., Yssel H., Schneider P.V., Cocks B.G., Bacon K.B., Zlotnik A.
J. Immunol. 155:203-209(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of a novel C or gamma type chemokine, SCM-1."
Yoshida T., Imai T., Kakizaki M., Nishimura M., Yoshie O.
FEBS Lett. 360:155-159(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[3]"Cloning of ATAC, an activation-induced, chemokine-related molecule exclusively expressed in CD8+ T lymphocytes."
Mueller S., Dorner B., Korthauer U., Mages H.W., D'Apuzzo M., Senger G., Kroczek R.A.
Eur. J. Immunol. 25:1744-1748(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Peripheral blood.
[4]"Structure and expression of two highly related genes encoding SCM-1/human lymphotactin."
Yoshida T., Imai T., Takagi S., Nishimura M., Ishikawa I., Yaoi T., Yoshie O.
FEBS Lett. 395:82-88(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Blood.
[7]"Monomeric solution structure of the prototypical 'C' chemokine lymphotactin."
Kuloglu E.S., McCaslin D.R., Kitabwalla M., Pauza C.D., Markley J.L., Volkman B.F.
Biochemistry 40:12486-12496(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 22-114, DISULFIDE BOND.
+Additional computationally mapped references.

Web resources

Wikipedia

XCL1 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23772 mRNA. Translation: AAC50164.1.
D43768 mRNA. Translation: BAA07825.1.
X86474 mRNA. Translation: CAA60198.1.
D63790 Genomic DNA. Translation: BAA09859.1.
AL031736 Genomic DNA. Translation: CAB46691.1.
BC069817 mRNA. Translation: AAH69817.1.
BC070309 mRNA. Translation: AAH70309.1.
PIRETHUL. S60650.
RefSeqNP_002986.1. NM_002995.2.
UniGeneHs.458346.
Hs.546295.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1J8INMR-A22-114[»]
1J9ONMR-A22-114[»]
2HDMNMR-A23-114[»]
2JP1NMR-A/B22-114[»]
2NYZX-ray2.60D/E22-114[»]
ProteinModelPortalP47992.
SMRP47992. Positions 22-114.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-29876N.
MINTMINT-1535585.
STRING9606.ENSP00000356792.

Polymorphism databases

DMDM1346471.

Proteomic databases

PaxDbP47992.
PRIDEP47992.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000367818; ENSP00000356792; ENSG00000143184.
GeneID6375.
KEGGhsa:6375.
UCSCuc001gfo.2. human.

Organism-specific databases

CTD6375.
GeneCardsGC01P168545.
HGNCHGNC:10645. XCL1.
HPAHPA057725.
MIM600250. gene.
neXtProtNX_P47992.
PharmGKBPA35575.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG47852.
HOGENOMHOG000036685.
HOVERGENHBG102118.
InParanoidP47992.
KOK05507.
OMACADPQAK.
OrthoDBEOG7RBZBM.
PhylomeDBP47992.
TreeFamTF334888.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

BgeeP47992.
CleanExHS_XCL1.
GenevestigatorP47992.

Family and domain databases

InterProIPR001811. Chemokine_IL8-like_dom.
IPR008105. Chemokine_XCL1.
[Graphical view]
PfamPF00048. IL8. 1 hit.
[Graphical view]
PRINTSPR01731. LYMPHOTACTIN.
SMARTSM00199. SCY. 1 hit.
[Graphical view]
SUPFAMSSF54117. SSF54117. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP47992.
GenomeRNAi6375.
NextBio24768.
PMAP-CutDBP47992.
PROP47992.
SOURCESearch...

Entry information

Entry nameXCL1_HUMAN
AccessionPrimary (citable) accession number: P47992
Secondary accession number(s): Q52MA8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: April 16, 2014
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM