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Interleukin-10 (IL-10) (Cytokine synthesis inhibitory factor) (CSIF)

 IL10_HUMAN              Reviewed;         178 AA.
P22301;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
30-AUG-2017, entry version 180.
RecName: Full=Interleukin-10;
Short=IL-10;
AltName: Full=Cytokine synthesis inhibitory factor;
Short=CSIF;
Flags: Precursor;
Name=IL10;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=T-cell;
PubMed=1847510; DOI=10.1073/pnas.88.4.1172;
Vieira P., de Waal-Malefyt R., Dang M.-N., Johnson K.E., Kastelein R.,
Fiorentino D.F., Devries J.E., Roncarolo M.-G., Mosmann T.R.,
Moore K.W.;
"Isolation and expression of human cytokine synthesis inhibitory
factor cDNA clones: homology to Epstein-Barr virus open reading frame
BCRFI.";
Proc. Natl. Acad. Sci. U.S.A. 88:1172-1176(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Sanjanwala B., de Waal-Malefyt R.;
"The structure of the human IL-10 gene.";
Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA].
Dai W.-J., Jiang H.-C., Pan S.-H.;
"Cloning, sequencing of human interleukin-10 cDNA and construction of
its eukaryotic expression vector.";
Haerbin Yi Ke Da Xue Xue Bao 35:4-6(2001).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[5]
PROTEIN SEQUENCE OF 26-34 AND 170-178.
PubMed=9405662; DOI=10.1073/pnas.94.26.14620;
Gesser B., Leffers H., Jinquan T., Vestergaard C., Kirstein N.,
Sindet-Pedersen S., Jensen S.L., Thestrup-Pedersen K., Larsen C.G.;
"Identification of functional domains on human interleukin 10.";
Proc. Natl. Acad. Sci. U.S.A. 94:14620-14625(1997).
[6]
PROTEIN SEQUENCE OF 19-33.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[7]
DISULFIDE BONDS.
PubMed=8364028; DOI=10.1021/bi00085a011;
Windsor W.T., Syto R., Tsarbopoulos A., Zhang R., Durkin J.,
Baldwin S., Paliwal S., Mui P.W., Pramanik B., Trotta P.P.;
"Disulfide bond assignments and secondary structure analysis of human
and murine interleukin 10.";
Biochemistry 32:8807-8815(1993).
[8]
INVOLVEMENT IN RESISTANCE TO GVHDS.
PubMed=14657427; DOI=10.1056/NEJMoa022060;
Lin M.T., Storer B., Martin P.J., Tseng L.H., Gooley T., Chen P.J.,
Hansen J.A.;
"Relation of an interleukin-10 promoter polymorphism to graft-versus-
host disease and survival after hematopoietic-cell transplantation.";
N. Engl. J. Med. 349:2201-2210(2003).
[9]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=7547951; DOI=10.1021/bi00038a004;
Walter M.R., Nagabhushan T.L.;
"Crystal structure of interleukin 10 reveals an interferon gamma-like
fold.";
Biochemistry 34:12118-12125(1995).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
PubMed=8590020; DOI=10.1016/S0969-2126(01)00193-9;
Zdanov A., Schalk-Hihi C., Gustchina A., Tsang M., Wheatherbee J.,
Wlodawer A.;
"Crystal structure of interleukin-10 reveals the functional dimer with
an unexpected topological similarity to interferon gamma.";
Structure 3:591-601(1995).
[11]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
PubMed=8897595; DOI=10.1002/pro.5560051001;
Zdanov A., Schalk-Hihi C., Wlodawer A.;
"Crystal structure of human interleukin-10 at 1.6-A resolution and a
model of a complex with its soluble receptor.";
Protein Sci. 5:1955-1962(1996).
[12]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 19-178 IN COMPLEX WITH
IL10R1.
PubMed=11485736; DOI=10.1016/S1074-7613(01)00169-8;
Josephson K., Logsdon N.J., Walter M.R.;
"Crystal structure of the IL-10/IL-10R1 complex reveals a shared
receptor binding site.";
Immunity 15:35-46(2001).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-178 IN COMPLEX WITH
IL10R1.
PubMed=15837194; DOI=10.1016/j.str.2005.01.016;
Yoon S.I., Jones B.C., Logsdon N.J., Walter M.R.;
"Same structure, different function crystal structure of the Epstein-
Barr virus IL-10 bound to the soluble IL-10R1 chain.";
Structure 13:551-564(2005).
[14]
VARIANT ARG-15.
PubMed=12825869; DOI=10.1080/00365520310003011;
van der Linde K., Boor P.P., Sandkuijl L.A., Meijssen M.A.,
Savelkoul H.F., Wilson J.H., de Rooij F.W.;
"A Gly15Arg mutation in the interleukin-10 gene reduces secretion of
interleukin-10 in Crohn disease.";
Scand. J. Gastroenterol. 38:611-617(2003).
-!- FUNCTION: Inhibits the synthesis of a number of cytokines,
including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by
activated macrophages and by helper T-cells.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11485736,
ECO:0000269|PubMed:15837194}.
-!- INTERACTION:
Q13651:IL10RA; NbExp=6; IntAct=EBI-1031632, EBI-1031656;
P60410:KRTAP10-8; NbExp=4; IntAct=EBI-1031632, EBI-10171774;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Produced by a variety of cell lines, including
T-cells, macrophages, mast cells and other cell types.
-!- POLYMORPHISM: A polymorphism in IL10 promoter region is associated
with resistance to graft-versus-host disease (GVHDS) [MIM:614395].
GVHDS is a major complication of allogeneic bone marrow
transplantation, in which mature donor T-cells that contaminate
the allogeneic bone marrow recognize the tissues of the recipient
as foreign, causing a severe inflammatory disease.
{ECO:0000269|PubMed:14657427}.
-!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-10 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_10";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il10/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL10";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; M57627; AAA63207.1; -; mRNA.
EMBL; U16720; AAA80104.1; -; Genomic_DNA.
EMBL; AY029171; AAK38162.1; -; mRNA.
EMBL; AF418271; AAL06594.1; -; Genomic_DNA.
CCDS; CCDS1467.1; -.
PIR; A38580; A38580.
RefSeq; NP_000563.1; NM_000572.2.
UniGene; Hs.193717; -.
PDB; 1ILK; X-ray; 1.80 A; A=28-178.
PDB; 1INR; X-ray; 2.00 A; A=19-178.
PDB; 1J7V; X-ray; 2.90 A; L=19-178.
PDB; 1LK3; X-ray; 1.91 A; A/B=26-178.
PDB; 1Y6K; X-ray; 2.52 A; L=19-178.
PDB; 2H24; X-ray; 2.00 A; A=19-178.
PDB; 2ILK; X-ray; 1.60 A; A=19-178.
PDBsum; 1ILK; -.
PDBsum; 1INR; -.
PDBsum; 1J7V; -.
PDBsum; 1LK3; -.
PDBsum; 1Y6K; -.
PDBsum; 2H24; -.
PDBsum; 2ILK; -.
ProteinModelPortal; P22301; -.
SMR; P22301; -.
BioGrid; 109800; 7.
DIP; DIP-3511N; -.
IntAct; P22301; 8.
MINT; MINT-206740; -.
STRING; 9606.ENSP00000412237; -.
BindingDB; P22301; -.
ChEMBL; CHEMBL3712920; -.
DrugBank; DB05066; AV411.
DrugBank; DB05744; CRx-139.
DrugBank; DB05771; LLL-3348.
BioMuta; IL10; -.
DMDM; 124292; -.
PaxDb; P22301; -.
PeptideAtlas; P22301; -.
PRIDE; P22301; -.
DNASU; 3586; -.
Ensembl; ENST00000423557; ENSP00000412237; ENSG00000136634.
GeneID; 3586; -.
KEGG; hsa:3586; -.
CTD; 3586; -.
DisGeNET; 3586; -.
GeneCards; IL10; -.
HGNC; HGNC:5962; IL10.
HPA; CAB013120; -.
MalaCards; IL10; -.
MIM; 124092; gene.
MIM; 614395; phenotype.
neXtProt; NX_P22301; -.
OpenTargets; ENSG00000136634; -.
Orphanet; 238569; Autosomal recessive early-onset inflammatory bowel disease.
Orphanet; 117; Behcet disease.
Orphanet; 536; Systemic lupus erythematosus.
PharmGKB; PA29778; -.
eggNOG; ENOG410IYFW; Eukaryota.
eggNOG; ENOG4111PXC; LUCA.
GeneTree; ENSGT00510000048535; -.
HOGENOM; HOG000072692; -.
HOVERGEN; HBG004110; -.
InParanoid; P22301; -.
KO; K05443; -.
OMA; PHMLREL; -.
OrthoDB; EOG091G0Y3M; -.
PhylomeDB; P22301; -.
TreeFam; TF333253; -.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; P22301; -.
SIGNOR; P22301; -.
EvolutionaryTrace; P22301; -.
GeneWiki; Interleukin_10; -.
GenomeRNAi; 3586; -.
PRO; PR:P22301; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000136634; -.
CleanEx; HS_IL10; -.
ExpressionAtlas; P22301; baseline and differential.
Genevisible; P22301; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; NAS:BHF-UCL.
GO; GO:0008083; F:growth factor activity; NAS:UniProtKB.
GO; GO:0005141; F:interleukin-10 receptor binding; NAS:UniProtKB.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
GO; GO:0042100; P:B cell proliferation; NAS:UniProtKB.
GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
GO; GO:0007267; P:cell-cell signaling; IC:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; NAS:BHF-UCL.
GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
GO; GO:0072577; P:endothelial cell apoptotic process; ISS:BHF-UCL.
GO; GO:0030097; P:hemopoiesis; TAS:UniProtKB.
GO; GO:0006954; P:inflammatory response; IDA:BHF-UCL.
GO; GO:0030595; P:leukocyte chemotaxis; TAS:ProtInc.
GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
GO; GO:0030889; P:negative regulation of B cell proliferation; IDA:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; ISS:BHF-UCL.
GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; TAS:AgBase.
GO; GO:0002875; P:negative regulation of chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
GO; GO:0060302; P:negative regulation of cytokine activity; IMP:CACAO.
GO; GO:0002740; P:negative regulation of cytokine secretion involved in immune response; IDA:BHF-UCL.
GO; GO:0044130; P:negative regulation of growth of symbiont in host; IEA:Ensembl.
GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0045355; P:negative regulation of interferon-alpha biosynthetic process; NAS:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032692; P:negative regulation of interleukin-1 production; TAS:AgBase.
GO; GO:0032695; P:negative regulation of interleukin-12 production; TAS:AgBase.
GO; GO:0032701; P:negative regulation of interleukin-18 production; TAS:AgBase.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
GO; GO:0032717; P:negative regulation of interleukin-8 production; TAS:AgBase.
GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; TAS:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:BHF-UCL.
GO; GO:0030886; P:negative regulation of myeloid dendritic cell activation; IEA:Ensembl.
GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:1904057; P:negative regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0042130; P:negative regulation of T cell proliferation; NAS:UniProtKB.
GO; GO:0042536; P:negative regulation of tumor necrosis factor biosynthetic process; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; TAS:AgBase.
GO; GO:1904706; P:negative regulation of vascular smooth muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0002904; P:positive regulation of B cell apoptotic process; IDA:MGI.
GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IDA:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISS:BHF-UCL.
GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; IDA:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:1904707; P:positive regulation of vascular smooth muscle cell proliferation; ISS:BHF-UCL.
GO; GO:0032800; P:receptor biosynthetic process; IDA:BHF-UCL.
GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
GO; GO:0045191; P:regulation of isotype switching; NAS:UniProtKB.
GO; GO:1903034; P:regulation of response to wounding; ISS:BHF-UCL.
GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
GO; GO:0014823; P:response to activity; IEA:Ensembl.
GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
GO; GO:0014854; P:response to inactivity; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
GO; GO:0042092; P:type 2 immune response; TAS:UniProtKB.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000098; IL-10.
InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
InterPro; IPR020423; IL-10_CS.
Pfam; PF00726; IL10; 1.
PRINTS; PR01294; INTRLEUKIN10.
SMART; SM00188; IL10; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00520; INTERLEUKIN_10; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytokine; Direct protein sequencing;
Disease mutation; Disulfide bond; Glycoprotein; Reference proteome;
Secreted; Signal.
SIGNAL 1 18 {ECO:0000269|PubMed:15340161}.
CHAIN 19 178 Interleukin-10.
/FTId=PRO_0000015360.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 30 126 {ECO:0000269|PubMed:8364028}.
DISULFID 80 132 {ECO:0000269|PubMed:8364028}.
VARIANT 15 15 G -> R (in a family affected by Crohn
disease; decreases secretion thereby
reducing the anti-inflammatory effect;
dbSNP:rs145922845).
{ECO:0000269|PubMed:12825869}.
/FTId=VAR_015883.
TURN 33 36 {ECO:0000244|PDB:2ILK}.
HELIX 37 49 {ECO:0000244|PDB:2ILK}.
HELIX 52 58 {ECO:0000244|PDB:2ILK}.
HELIX 68 75 {ECO:0000244|PDB:2ILK}.
TURN 76 78 {ECO:0000244|PDB:1Y6K}.
HELIX 79 93 {ECO:0000244|PDB:2ILK}.
HELIX 95 99 {ECO:0000244|PDB:2ILK}.
TURN 103 105 {ECO:0000244|PDB:2ILK}.
HELIX 106 125 {ECO:0000244|PDB:2ILK}.
TURN 127 129 {ECO:0000244|PDB:2H24}.
HELIX 131 133 {ECO:0000244|PDB:2ILK}.
HELIX 137 148 {ECO:0000244|PDB:2ILK}.
HELIX 151 159 {ECO:0000244|PDB:2ILK}.
HELIX 161 176 {ECO:0000244|PDB:2ILK}.
SEQUENCE 178 AA; 20517 MW; 6825E9FA4337CDE4 CRC64;
MHSSALLCCL VLLTGVRASP GQGTQSENSC THFPGNLPNM LRDLRDAFSR VKTFFQMKDQ
LDNLLLKESL LEDFKGYLGC QALSEMIQFY LEEVMPQAEN QDPDIKAHVN SLGENLKTLR
LRLRRCHRFL PCENKSKAVE QVKNAFNKLQ EKGIYKAMSE FDIFINYIEA YMTMKIRN


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