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 27-MAR-2024, entry version 222. 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; Q9BYQ7: KRTAP4-1; NbExp=3; IntAct=EBI-1031632, EBI-34579671; 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 EMDB; EMD-22098; -. DR SMR; P22301; -. DR BioGRID; 109800; 22. 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 GlyCosmos; P22301; 1 site, No reported glycans. DR GlyGen; P22301; 1 site. DR BioMuta; IL10; -. DR DMDM; 124292; -. DR MassIVE; P22301; -. DR PaxDb; 9606-ENSP00000412237; -. DR PeptideAtlas; P22301; -. DR ProteomicsDB; 53970; -. DR ABCD; P22301; 1 sequenced antibody. DR Antibodypedia; 3407; 1872 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 AGR; HGNC:5962; -. 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; VMPKAEN; -. DR OrthoDB; 4203939at2759; -. 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 1150 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 103 other cell types or tissues. DR ExpressionAtlas; P22301; baseline and differential. 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: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: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: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:0045019; P:negative regulation of nitric oxide biosynthetic process; IEA:Ensembl. DR GO; GO:1903377; P:negative regulation of oxidative stress-induced neuron intrinsic apoptotic signaling pathway; 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:0032689; P:negative regulation of type II interferon production; IEA:Ensembl. 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:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB. 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: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 PANTHER; PTHR48394:SF1; INTERLEUKIN-10; 1. DR PANTHER; PTHR48394; INTERLEUKIN-19-RELATED; 1. DR Pfam; PF00726; IL10; 1. DR PRINTS; PR01294; INTRLEUKIN10. DR SMART; SM00188; IL10; 1. DR SUPFAM; SSF47266; 4-helical cytokines; 1. DR PROSITE; PS00520; INTERLEUKIN_10; 1. DR Genevisible; P22301; HS. 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 //