GenomeNet

Database: UniProt
Entry: XCL2_HUMAN
LinkDB: XCL2_HUMAN
Original site: XCL2_HUMAN 
ID   XCL2_HUMAN              Reviewed;         114 AA.
AC   Q9UBD3;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   11-DEC-2019, entry version 155.
DE   RecName: Full=Cytokine SCM-1 beta;
DE   AltName: Full=C motif chemokine 2;
DE   AltName: Full=XC chemokine ligand 2;
DE   Flags: Precursor;
GN   Name=XCL2; Synonyms=SCYC2;
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 [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   [2]
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   [3]
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   [4]
RP   PROTEIN SEQUENCE OF 22-36.
RX   PubMed=15340161; DOI=10.1110/ps.04682504;
RA   Zhang Z., Henzel W.J.;
RT   "Signal peptide prediction based on analysis of experimentally verified
RT   cleavage sites.";
RL   Protein Sci. 13:2819-2824(2004).
CC   -!- FUNCTION: Chemotactic activity for lymphocytes but not for monocytes or
CC       neutrophils. {ECO:0000250}.
CC   -!- INTERACTION:
CC       P13501:CCL5; NbExp=2; IntAct=EBI-10319095, EBI-2848366;
CC       P48061:CXCL12; NbExp=2; IntAct=EBI-10319095, EBI-3913254;
CC       P60411:KRTAP10-9; NbExp=3; IntAct=EBI-10319095, EBI-10172052;
CC       Q7Z3S9:NOTCH2NLA; NbExp=3; IntAct=EBI-10319095, EBI-945833;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the intercrine gamma family. {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=XCL2 entry;
CC       URL="https://en.wikipedia.org/wiki/XCL2";
DR   EMBL; D63789; BAA09858.1; -; Genomic_DNA.
DR   EMBL; AL031736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC069360; AAH69360.1; -; mRNA.
DR   EMBL; BC070308; AAH70308.1; -; mRNA.
DR   CCDS; CCDS1273.1; -.
DR   RefSeq; NP_003166.1; NM_003175.3.
DR   SMR; Q9UBD3; -.
DR   BioGrid; 112713; 2.
DR   IntAct; Q9UBD3; 16.
DR   STRING; 9606.ENSP00000356793; -.
DR   iPTMnet; Q9UBD3; -.
DR   PhosphoSitePlus; Q9UBD3; -.
DR   BioMuta; XCL2; -.
DR   DMDM; 11387207; -.
DR   MassIVE; Q9UBD3; -.
DR   PaxDb; Q9UBD3; -.
DR   PeptideAtlas; Q9UBD3; -.
DR   PRIDE; Q9UBD3; -.
DR   ProteomicsDB; 83946; -.
DR   DNASU; 6846; -.
DR   Ensembl; ENST00000367819; ENSP00000356793; ENSG00000143185.
DR   GeneID; 6846; -.
DR   KEGG; hsa:6846; -.
DR   UCSC; uc001gfn.4; human.
DR   CTD; 6846; -.
DR   DisGeNET; 6846; -.
DR   EuPathDB; HostDB:ENSG00000143185.3; -.
DR   GeneCards; XCL2; -.
DR   HGNC; HGNC:10646; XCL2.
DR   HPA; HPA057725; -.
DR   MIM; 604828; gene.
DR   neXtProt; NX_Q9UBD3; -.
DR   OpenTargets; ENSG00000143185; -.
DR   PharmGKB; PA35576; -.
DR   eggNOG; ENOG410IZ5E; Eukaryota.
DR   eggNOG; ENOG4111C3M; LUCA.
DR   GeneTree; ENSGT00970000193327; -.
DR   HOGENOM; HOG000036685; -.
DR   InParanoid; Q9UBD3; -.
DR   KO; K22675; -.
DR   OMA; CANPEAN; -.
DR   OrthoDB; 1553663at2759; -.
DR   PhylomeDB; Q9UBD3; -.
DR   TreeFam; TF334888; -.
DR   Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-HSA-416476; G alpha (q) signalling events.
DR   GenomeRNAi; 6846; -.
DR   Pharos; Q9UBD3; Tbio.
DR   PRO; PR:Q9UBD3; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q9UBD3; protein.
DR   Bgee; ENSG00000143185; Expressed in 78 organ(s), highest expression level in blood.
DR   Genevisible; Q9UBD3; HS.
DR   GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR   GO; GO:0008015; P:blood circulation; TAS:ProtInc.
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: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:0048245; P:eosinophil chemotaxis; 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:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR   GO; GO:0010820; P:positive regulation of T cell chemotaxis; IBA:GO_Central.
DR   GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR   CDD; cd00271; Chemokine_C; 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; 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   Chemotaxis; Cytokine; Direct protein sequencing; Disulfide bond;
KW   Polymorphism; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000269|PubMed:15340161"
FT   CHAIN           22..114
FT                   /note="Cytokine SCM-1 beta"
FT                   /id="PRO_0000005251"
FT   DISULFID        32..69
FT                   /evidence="ECO:0000255"
FT   VARIANT         28
FT                   /note="H -> D (in dbSNP:rs4301615)"
FT                   /id="VAR_048713"
FT   VARIANT         29
FT                   /note="R -> K (in dbSNP:rs4501820)"
FT                   /id="VAR_059212"
SQ   SEQUENCE   114 AA;  12567 MW;  E7F3C283F02D6D9D CRC64;
     MRLLILALLG ICSLTAYIVE GVGSEVSHRR TCVSLTTQRL PVSRIKTYTI TEGSLRAVIF
     ITKRGLKVCA DPQATWVRDV VRSMDRKSNT RNNMIQTKPT GTQQSTNTAV TLTG
//
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