IL10_HUMAN
ID IL10_HUMAN Reviewed; 178 AA.
AC P22301;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 213.
DE RecName: Full=Interleukin-10;
DE Short=IL-10;
DE AltName: Full=Cytokine synthesis inhibitory factor;
DE Short=CSIF;
DE Flags: Precursor;
GN Name=IL10;
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].
RC TISSUE=T-cell;
RX PubMed=1847510; DOI=10.1073/pnas.88.4.1172;
RA Vieira P., de Waal-Malefyt R., Dang M.-N., Johnson K.E., Kastelein R.,
RA Fiorentino D.F., Devries J.E., Roncarolo M.-G., Mosmann T.R., Moore K.W.;
RT "Isolation and expression of human cytokine synthesis inhibitory factor
RT cDNA clones: homology to Epstein-Barr virus open reading frame BCRFI.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:1172-1176(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Sanjanwala B., de Waal-Malefyt R.;
RT "The structure of the human IL-10 gene.";
RL Submitted (OCT-1994) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dai W.-J., Jiang H.-C., Pan S.-H.;
RT "Cloning, sequencing of human interleukin-10 cDNA and construction of its
RT eukaryotic expression vector.";
RL Haerbin Yi Ke Da Xue Xue Bao 35:4-6(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PROTEIN SEQUENCE OF 26-34 AND 170-178.
RX PubMed=9405662; DOI=10.1073/pnas.94.26.14620;
RA Gesser B., Leffers H., Jinquan T., Vestergaard C., Kirstein N.,
RA Sindet-Pedersen S., Jensen S.L., Thestrup-Pedersen K., Larsen C.G.;
RT "Identification of functional domains on human interleukin 10.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:14620-14625(1997).
RN [6]
RP PROTEIN SEQUENCE OF 19-33.
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).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=1940799; DOI=10.1084/jem.174.5.1209;
RA de Waal Malefyt R., Abrams J., Bennett B., Figdor C.G., de Vries J.E.;
RT "Interleukin 10(IL-10) inhibits cytokine synthesis by human monocytes: an
RT autoregulatory role of IL-10 produced by monocytes.";
RL J. Exp. Med. 174:1209-1220(1991).
RN [8]
RP DISULFIDE BONDS.
RX PubMed=8364028; DOI=10.1021/bi00085a011;
RA Windsor W.T., Syto R., Tsarbopoulos A., Zhang R., Durkin J., Baldwin S.,
RA Paliwal S., Mui P.W., Pramanik B., Trotta P.P.;
RT "Disulfide bond assignments and secondary structure analysis of human and
RT murine interleukin 10.";
RL Biochemistry 32:8807-8815(1993).
RN [9]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=7512027; DOI=10.1002/eji.1830240435;
RA Willems F., Marchant A., Delville J.P., Gerard C., Delvaux A., Velu T.,
RA de Boer M., Goldman M.;
RT "Interleukin-10 inhibits B7 and intercellular adhesion molecule-1
RT expression on human monocytes.";
RL Eur. J. Immunol. 24:1007-1009(1994).
RN [10]
RP FUNCTION.
RX PubMed=8144879;
RA Frei K., Lins H., Schwerdel C., Fontana A.;
RT "Antigen presentation in the central nervous system. The inhibitory effect
RT of IL-10 on MHC class II expression and production of cytokines depends on
RT the inducing signals and the type of cell analyzed.";
RL J. Immunol. 152:2720-2728(1994).
RN [11]
RP FUNCTION.
RX PubMed=11564774; DOI=10.4049/jimmunol.167.7.3619;
RA Hashimoto S.I., Komuro I., Yamada M., Akagawa K.S.;
RT "IL-10 inhibits granulocyte-macrophage colony-stimulating factor-dependent
RT human monocyte survival at the early stage of the culture and inhibits the
RT generation of macrophages.";
RL J. Immunol. 167:3619-3625(2001).
RN [12]
RP INVOLVEMENT IN RESISTANCE TO GVHDS.
RX PubMed=14657427; DOI=10.1056/nejmoa022060;
RA Lin M.T., Storer B., Martin P.J., Tseng L.H., Gooley T., Chen P.J.,
RA Hansen J.A.;
RT "Relation of an interleukin-10 promoter polymorphism to graft-versus-host
RT disease and survival after hematopoietic-cell transplantation.";
RL N. Engl. J. Med. 349:2201-2210(2003).
RN [13]
RP FUNCTION, MUTAGENESIS OF ARG-42, AND INTERACTION WITH IL10RA AND IL10RB.
RX PubMed=16982608; DOI=10.1074/jbc.m606791200;
RA Yoon S.I., Logsdon N.J., Sheikh F., Donnelly R.P., Walter M.R.;
RT "Conformational changes mediate interleukin-10 receptor 2 (IL-10R2) binding
RT to IL-10 and assembly of the signaling complex.";
RL J. Biol. Chem. 281:35088-35096(2006).
RN [14]
RP FUNCTION.
RX PubMed=18025162; DOI=10.4049/jimmunol.179.11.7215;
RA El Kasmi K.C., Smith A.M., Williams L., Neale G., Panopolous A.,
RA Watowich S.S., Hacker H., Foxwell B.M., Murray P.J.;
RT "A transcriptional repressor and corepressor induced by the STAT3-regulated
RT anti-inflammatory signaling pathway.";
RL J. Immunol. 179:7215-7219(2007).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=7547951; DOI=10.1021/bi00038a004;
RA Walter M.R., Nagabhushan T.L.;
RT "Crystal structure of interleukin 10 reveals an interferon gamma-like
RT fold.";
RL Biochemistry 34:12118-12125(1995).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
RX PubMed=8590020; DOI=10.1016/s0969-2126(01)00193-9;
RA Zdanov A., Schalk-Hihi C., Gustchina A., Tsang M., Wheatherbee J.,
RA Wlodawer A.;
RT "Crystal structure of interleukin-10 reveals the functional dimer with an
RT unexpected topological similarity to interferon gamma.";
RL Structure 3:591-601(1995).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
RX PubMed=8897595; DOI=10.1002/pro.5560051001;
RA Zdanov A., Schalk-Hihi C., Wlodawer A.;
RT "Crystal structure of human interleukin-10 at 1.6-A resolution and a model
RT of a complex with its soluble receptor.";
RL Protein Sci. 5:1955-1962(1996).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 19-178 IN COMPLEX WITH IL10R1.
RX PubMed=11485736; DOI=10.1016/s1074-7613(01)00169-8;
RA Josephson K., Logsdon N.J., Walter M.R.;
RT "Crystal structure of the IL-10/IL-10R1 complex reveals a shared receptor
RT binding site.";
RL Immunity 15:35-46(2001).
RN [19]
RP X-RAY CRYSTALLOGRAPHY (1.91 ANGSTROMS) OF 26-178.
RX PubMed=12121653; DOI=10.1016/s0969-2126(02)00791-8;
RA Josephson K., Jones B.C., Walter L.J., DiGiacomo R., Indelicato S.R.,
RA Walter M.R.;
RT "Noncompetitive antibody neutralization of IL-10 revealed by protein
RT engineering and x-ray crystallography.";
RL Structure 10:981-987(2002).
RN [20]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 19-178 IN COMPLEX WITH IL10R1.
RX PubMed=15837194; DOI=10.1016/j.str.2005.01.016;
RA Yoon S.I., Jones B.C., Logsdon N.J., Walter M.R.;
RT "Same structure, different function crystal structure of the Epstein-Barr
RT virus IL-10 bound to the soluble IL-10R1 chain.";
RL Structure 13:551-564(2005).
RN [21]
RP VARIANT ARG-15.
RX PubMed=12825869; DOI=10.1080/00365520310003011;
RA van der Linde K., Boor P.P., Sandkuijl L.A., Meijssen M.A., Savelkoul H.F.,
RA Wilson J.H., de Rooij F.W.;
RT "A Gly15Arg mutation in the interleukin-10 gene reduces secretion of
RT interleukin-10 in Crohn disease.";
RL Scand. J. Gastroenterol. 38:611-617(2003).
CC -!- FUNCTION: Major immune regulatory cytokine that acts on many cells of
CC the immune system where it has profound anti-inflammatory functions,
CC limiting excessive tissue disruption caused by inflammation.
CC Mechanistically, IL10 binds to its heterotetrameric receptor comprising
CC IL10RA and IL10RB leading to JAK1 and STAT2-mediated phosphorylation of
CC STAT3 (PubMed:16982608). In turn, STAT3 translocates to the nucleus
CC where it drives expression of anti-inflammatory mediators
CC (PubMed:18025162). Targets antigen-presenting cells (APCs) such as
CC macrophages and monocytes and inhibits their release of pro-
CC inflammatory cytokines including granulocyte-macrophage colony-
CC stimulating factor /GM-CSF, granulocyte colony-stimulating factor/G-
CC CSF, IL-1 alpha, IL-1 beta, IL-6, IL-8 and TNF-alpha (PubMed:1940799,
CC PubMed:7512027, PubMed:11564774). Interferes also with antigen
CC presentation by reducing the expression of MHC-class II and co-
CC stimulatory molecules, thereby inhibiting their ability to induce T
CC cell activation (PubMed:8144879). In addition, controls the
CC inflammatory response of macrophages by reprogramming essential
CC metabolic pathways including mTOR signaling (By similarity).
CC {ECO:0000250|UniProtKB:P18893, ECO:0000269|PubMed:11564774,
CC ECO:0000269|PubMed:16982608, ECO:0000269|PubMed:18025162,
CC ECO:0000269|PubMed:1940799, ECO:0000269|PubMed:7512027,
CC ECO:0000269|PubMed:8144879}.
CC -!- SUBUNIT: Homodimer (PubMed:11485736, PubMed:15837194). Interacts with
CC IL10RA and IL10RB (PubMed:16982608). {ECO:0000269|PubMed:11485736,
CC ECO:0000269|PubMed:15837194, ECO:0000269|PubMed:16982608}.
CC -!- INTERACTION:
CC P22301; O76003: GLRX3; NbExp=3; IntAct=EBI-1031632, EBI-374781;
CC P22301; Q13651: IL10RA; NbExp=9; IntAct=EBI-1031632, EBI-1031656;
CC P22301; Q08334: IL10RB; NbExp=2; IntAct=EBI-1031632, EBI-11175900;
CC P22301; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-1031632, EBI-11749135;
CC P22301; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-1031632, EBI-10171774;
CC P22301; A0A087WY89: KRTAP4-1; NbExp=3; IntAct=EBI-1031632, EBI-11957260;
CC P22301; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-1031632, EBI-22310682;
CC P22301; P25490: YY1; NbExp=3; IntAct=EBI-1031632, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Produced by a variety of cell lines, including T-
CC cells, macrophages, mast cells and other cell types.
CC {ECO:0000269|PubMed:1940799, ECO:0000269|PubMed:7512027}.
CC -!- POLYMORPHISM: A polymorphism in IL10 promoter region is associated with
CC resistance to graft-versus-host disease (GVHDS) [MIM:614395]. GVHDS is
CC a major complication of allogeneic bone marrow transplantation, in
CC which mature donor T-cells that contaminate the allogeneic bone marrow
CC recognize the tissues of the recipient as foreign, causing a severe
CC inflammatory disease. {ECO:0000269|PubMed:14657427}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-10 entry;
CC URL="https://en.wikipedia.org/wiki/Interleukin_10";
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il10/";
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M57627; AAA63207.1; -; mRNA.
DR EMBL; U16720; AAA80104.1; -; Genomic_DNA.
DR EMBL; AY029171; AAK38162.1; -; mRNA.
DR EMBL; AF418271; AAL06594.1; -; Genomic_DNA.
DR CCDS; CCDS1467.1; -.
DR PIR; A38580; A38580.
DR RefSeq; NP_000563.1; NM_000572.2.
DR PDB; 1ILK; X-ray; 1.80 A; A=28-178.
DR PDB; 1INR; X-ray; 2.00 A; A=19-178.
DR PDB; 1J7V; X-ray; 2.90 A; L=19-178.
DR PDB; 1LK3; X-ray; 1.91 A; A/B=26-178.
DR PDB; 1Y6K; X-ray; 2.52 A; L=19-178.
DR PDB; 2H24; X-ray; 2.00 A; A=19-178.
DR PDB; 2ILK; X-ray; 1.60 A; A=19-178.
DR PDB; 6X93; EM; 3.50 A; A/D=19-178.
DR PDBsum; 1ILK; -.
DR PDBsum; 1INR; -.
DR PDBsum; 1J7V; -.
DR PDBsum; 1LK3; -.
DR PDBsum; 1Y6K; -.
DR PDBsum; 2H24; -.
DR PDBsum; 2ILK; -.
DR PDBsum; 6X93; -.
DR AlphaFoldDB; P22301; -.
DR SMR; P22301; -.
DR BioGRID; 109800; 20.
DR CORUM; P22301; -.
DR DIP; DIP-3511N; -.
DR IntAct; P22301; 9.
DR MINT; P22301; -.
DR STRING; 9606.ENSP00000412237; -.
DR BindingDB; P22301; -.
DR ChEMBL; CHEMBL3712920; -.
DR DrugBank; DB05744; CRx-139.
DR DrugBank; DB05771; LLL-3348.
DR GlyGen; P22301; 1 site.
DR BioMuta; IL10; -.
DR DMDM; 124292; -.
DR MassIVE; P22301; -.
DR PaxDb; P22301; -.
DR PeptideAtlas; P22301; -.
DR PRIDE; P22301; -.
DR ProteomicsDB; 53970; -.
DR ABCD; P22301; 1 sequenced antibody.
DR Antibodypedia; 3407; 1676 antibodies from 46 providers.
DR DNASU; 3586; -.
DR Ensembl; ENST00000423557.1; ENSP00000412237.1; ENSG00000136634.7.
DR GeneID; 3586; -.
DR KEGG; hsa:3586; -.
DR MANE-Select; ENST00000423557.1; ENSP00000412237.1; NM_000572.3; NP_000563.1.
DR CTD; 3586; -.
DR DisGeNET; 3586; -.
DR GeneCards; IL10; -.
DR HGNC; HGNC:5962; IL10.
DR HPA; ENSG00000136634; Tissue enhanced (adipose tissue, lymphoid tissue).
DR MalaCards; IL10; -.
DR MIM; 124092; gene.
DR MIM; 614395; phenotype.
DR neXtProt; NX_P22301; -.
DR OpenTargets; ENSG00000136634; -.
DR Orphanet; 117; Behcet disease.
DR Orphanet; 238569; Immune dysregulation-inflammatory bowel disease-arthritis-recurrent infections syndrome.
DR Orphanet; 536; Systemic lupus erythematosus.
DR PharmGKB; PA29778; -.
DR VEuPathDB; HostDB:ENSG00000136634; -.
DR eggNOG; ENOG502S22U; Eukaryota.
DR GeneTree; ENSGT00950000183124; -.
DR HOGENOM; CLU_127747_0_0_1; -.
DR InParanoid; P22301; -.
DR OMA; MIQFYLV; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P22301; -.
DR TreeFam; TF333253; -.
DR PathwayCommons; P22301; -.
DR Reactome; R-HSA-6783783; Interleukin-10 signaling.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
DR Reactome; R-HSA-9662834; CD163 mediating an anti-inflammatory response.
DR Reactome; R-HSA-9664323; FCGR3A-mediated IL10 synthesis.
DR SignaLink; P22301; -.
DR SIGNOR; P22301; -.
DR BioGRID-ORCS; 3586; 8 hits in 1066 CRISPR screens.
DR ChiTaRS; IL10; human.
DR EvolutionaryTrace; P22301; -.
DR GeneWiki; Interleukin_10; -.
DR GenomeRNAi; 3586; -.
DR Pharos; P22301; Tbio.
DR PRO; PR:P22301; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; P22301; protein.
DR Bgee; ENSG00000136634; Expressed in vermiform appendix and 102 other tissues.
DR ExpressionAtlas; P22301; baseline and differential.
DR Genevisible; P22301; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
DR GO; GO:0005125; F:cytokine activity; NAS:BHF-UCL.
DR GO; GO:0008083; F:growth factor activity; NAS:UniProtKB.
DR GO; GO:0005141; F:interleukin-10 receptor binding; NAS:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0030183; P:B cell differentiation; NAS:UniProtKB.
DR GO; GO:0042100; P:B cell proliferation; NAS:UniProtKB.
DR GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; IEA:Ensembl.
DR GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
DR GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IEA:Ensembl.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:ARUK-UCL.
DR GO; GO:0002439; P:chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0007253; P:cytoplasmic sequestering of NF-kappaB; NAS:UniProtKB.
DR GO; GO:0042742; P:defense response to bacterium; IEA:Ensembl.
DR GO; GO:0042832; P:defense response to protozoan; IEA:Ensembl.
DR GO; GO:0072577; P:endothelial cell apoptotic process; ISS:BHF-UCL.
DR GO; GO:0030097; P:hemopoiesis; TAS:UniProtKB.
DR GO; GO:0030595; P:leukocyte chemotaxis; TAS:ProtInc.
DR GO; GO:0097421; P:liver regeneration; IEA:Ensembl.
DR GO; GO:0043066; P:negative regulation of apoptotic process; NAS:UniProtKB.
DR GO; GO:0010507; P:negative regulation of autophagy; IDA:UniProtKB.
DR GO; GO:0030889; P:negative regulation of B cell proliferation; IDA:MGI.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:BHF-UCL.
DR GO; GO:0071650; P:negative regulation of chemokine (C-C motif) ligand 5 production; TAS:AgBase.
DR GO; GO:0002875; P:negative regulation of chronic inflammatory response to antigenic stimulus; IEA:Ensembl.
DR GO; GO:0060302; P:negative regulation of cytokine activity; IMP:CACAO.
DR GO; GO:0001818; P:negative regulation of cytokine production; IDA:UniProtKB.
DR GO; GO:0002719; P:negative regulation of cytokine production involved in immune response; IDA:BHF-UCL.
DR GO; GO:0034115; P:negative regulation of heterotypic cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:1903208; P:negative regulation of hydrogen peroxide-induced neuron death; ISS:ARUK-UCL.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IDA:BHF-UCL.
DR GO; GO:0032687; P:negative regulation of interferon-alpha production; NAS:UniProtKB.
DR GO; GO:0032689; P:negative regulation of interferon-gamma production; IEA:Ensembl.
DR GO; GO:0032692; P:negative regulation of interleukin-1 production; TAS:AgBase.
DR GO; GO:0032695; P:negative regulation of interleukin-12 production; TAS:AgBase.
DR GO; GO:0032701; P:negative regulation of interleukin-18 production; TAS:AgBase.
DR GO; GO:0032715; P:negative regulation of interleukin-6 production; IDA:BHF-UCL.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; TAS:AgBase.
DR GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:BHF-UCL.
DR GO; GO:0030886; P:negative regulation of myeloid dendritic cell activation; IEA:Ensembl.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:1904057; P:negative regulation of sensory perception of pain; IEA:Ensembl.
DR GO; GO:0042130; P:negative regulation of T cell proliferation; NAS:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; TAS:AgBase.
DR GO; GO:1904706; P:negative regulation of vascular associated smooth muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0002904; P:positive regulation of B cell apoptotic process; IDA:MGI.
DR GO; GO:0045787; P:positive regulation of cell cycle; IEA:Ensembl.
DR GO; GO:0001819; P:positive regulation of cytokine production; IDA:BHF-UCL.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; ISS:BHF-UCL.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IGI:ARUK-UCL.
DR GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
DR GO; GO:0045348; P:positive regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IDA:ARUK-UCL.
DR GO; GO:1900100; P:positive regulation of plasma cell differentiation; IGI:ARUK-UCL.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:UniProtKB.
DR GO; GO:2000273; P:positive regulation of signaling receptor activity; IDA:BHF-UCL.
DR GO; GO:1903672; P:positive regulation of sprouting angiogenesis; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:1904707; P:positive regulation of vascular associated smooth muscle cell proliferation; ISS:BHF-UCL.
DR GO; GO:0010468; P:regulation of gene expression; IDA:MGI.
DR GO; GO:0045191; P:regulation of isotype switching; NAS:UniProtKB.
DR GO; GO:1903034; P:regulation of response to wounding; ISS:BHF-UCL.
DR GO; GO:0050807; P:regulation of synapse organization; IEA:Ensembl.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0034465; P:response to carbon monoxide; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:BHF-UCL.
DR GO; GO:0014854; P:response to inactivity; IEA:Ensembl.
DR GO; GO:0032868; P:response to insulin; IEA:Ensembl.
DR GO; GO:0002237; P:response to molecule of bacterial origin; IDA:UniProtKB.
DR GO; GO:0009410; P:response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0042092; P:type 2 immune response; TAS:UniProtKB.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR000098; IL-10.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR020423; IL-10_CS.
DR Pfam; PF00726; IL10; 1.
DR PRINTS; PR01294; INTRLEUKIN10.
DR SMART; SM00188; IL10; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Direct protein sequencing; Disease variant;
KW Disulfide bond; Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 19..178
FT /note="Interleukin-10"
FT /id="PRO_0000015360"
FT CARBOHYD 134
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..126
FT /evidence="ECO:0000269|PubMed:8364028"
FT DISULFID 80..132
FT /evidence="ECO:0000269|PubMed:8364028"
FT VARIANT 15
FT /note="G -> R (in a family affected by Crohn disease;
FT decreases secretion thereby reducing the anti-inflammatory
FT effect; dbSNP:rs145922845)"
FT /evidence="ECO:0000269|PubMed:12825869"
FT /id="VAR_015883"
FT MUTAGEN 42
FT /note="R->A: About 80% loss of IL10RA binding."
FT /evidence="ECO:0000269|PubMed:16982608"
FT TURN 33..36
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 37..49
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 68..75
FT /evidence="ECO:0007829|PDB:2ILK"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:1Y6K"
FT HELIX 79..93
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:2ILK"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 106..125
FT /evidence="ECO:0007829|PDB:2ILK"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:2H24"
FT HELIX 131..133
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 137..148
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 151..159
FT /evidence="ECO:0007829|PDB:2ILK"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:2ILK"
SQ 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
