IL20_HUMAN
ID IL20_HUMAN Reviewed; 176 AA.
AC Q9NYY1; Q17RB3; Q2THG6; Q96QZ6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Interleukin-20;
DE Short=IL-20;
DE AltName: Full=Cytokine Zcyto10;
DE Flags: Precursor;
GN Name=IL20; Synonyms=ZCYTO10; ORFNames=UNQ852/PRO1801;
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] (ISOFORM 1).
RX PubMed=11163236; DOI=10.1016/s0092-8674(01)00187-8;
RA Blumberg H., Conklin D., Xu W.F., Grossmann A., Brender T., Carollo S.,
RA Eagan M., Foster D., Haldeman B.A., Hammond A., Haugen H., Jelinek L.,
RA Kelly J.D., Madden K., Maurer M.F., Parrish-Novak J., Prunkard D.,
RA Sexson S., Sprecher C., Waggie K., West J., Whitmore T.E., Yao L.,
RA Kuechle M.K., Dale B.A., Chandrasekher Y.A.;
RT "Interleukin 20: discovery, receptor identification, and role in epidermal
RT function.";
RL Cell 104:9-19(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY (ISOFORM 2).
RX PubMed=16511554; DOI=10.1038/sj.gene.6364291;
RA Hsieh M.Y., Chen W.Y., Jiang M.J., Cheng B.C., Huang T.Y., Chang M.S.;
RT "Interleukin-20 promotes angiogenesis in a direct and indirect manner.";
RL Genes Immun. 7:234-242(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG SeattleSNPs variation discovery resource;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [7]
RP PROTEIN SEQUENCE OF 25-39.
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=16908179; DOI=10.1016/j.cyto.2006.07.006;
RA Hsing C.H., Ho C.L., Chang L.Y., Lee Y.L., Chuang S.S., Chang M.S.;
RT "Tissue microarray analysis of interleukin-20 expression.";
RL Cytokine 35:44-52(2006).
RN [9]
RP INDUCTION BY UV-B.
RX PubMed=16709143; DOI=10.1562/2005-08-31-ra-668;
RA Hunt D.W., Boivin W.A., Fairley L.A., Jovanovic M.M., King D.E.,
RA Salmon R.A., Utting O.B.;
RT "Ultraviolet B light stimulates interleukin-20 expression by human
RT epithelial keratinocytes.";
RL Photochem. Photobiol. 82:1292-1300(2006).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 25-176 IN COMPLEX WITH IL20RA AND
RP IL20RB, SUBUNIT, AND DISULFIDE BONDS.
RX PubMed=22802649; DOI=10.1073/pnas.1117551109;
RA Logsdon N.J., Deshpande A., Harris B.D., Rajashankar K.R., Walter M.R.;
RT "Structural basis for receptor sharing and activation by interleukin-20
RT receptor-2 (IL-20R2) binding cytokines.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12704-12709(2012).
CC -!- FUNCTION: Pro-inflammatory and angiogenic cytokine that may be involved
CC in epidermal function and psoriasis. Angiogenic and proliferative
CC activities are antagonized by IL10. May act through STAT3.
CC {ECO:0000269|PubMed:16511554}.
CC -!- SUBUNIT: Forms a 1:1:1 heterotrimeric complex with its primary high-
CC affinity heterodimeric receptor IL20RA/IL20RB.
CC {ECO:0000269|PubMed:22802649}.
CC -!- INTERACTION:
CC PRO_0000015381; Q9UHF4: IL20RA; NbExp=4; IntAct=EBI-14022785, EBI-2933034;
CC PRO_0000015381; Q6UXL0: IL20RB; NbExp=5; IntAct=EBI-14022785, EBI-14022792;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=IL-20W, Wild type;
CC IsoId=Q9NYY1-1; Sequence=Displayed;
CC Name=2; Synonyms=IL-20S, ex4-del, Short;
CC IsoId=Q9NYY1-2; Sequence=VSP_054904;
CC -!- TISSUE SPECIFICITY: Expressed in most tissues and five major cell
CC types: epithelial cells (primarily skin, buccal mucosa, tongue, nasal
CC mucosa, lung, ureter, breast, prostate, fallopian tube, and adrenal
CC gland), myoepithelial cells (mainly prostate), endothelial cells
CC (mainly in small vessels or capillaries), macrophages, and skeletal
CC muscle. Isoform 2 was detected in the lung tissue only.
CC {ECO:0000269|PubMed:16908179}.
CC -!- INDUCTION: Up-regulated by UV-B irradiation in epithelial
CC keratinocytes. {ECO:0000269|PubMed:16709143}.
CC -!- MISCELLANEOUS: [Isoform 2]: Lung-specific. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il20/";
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; AF224266; AAF36679.1; -; mRNA.
DR EMBL; AY876922; AAW78348.1; -; mRNA.
DR EMBL; AY358320; AAQ88686.1; -; mRNA.
DR EMBL; AF402002; AAK84423.1; -; Genomic_DNA.
DR EMBL; AC098935; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC069311; AAH69311.1; -; mRNA.
DR EMBL; BC069364; AAH69364.1; -; mRNA.
DR EMBL; BC069398; AAH69398.1; -; mRNA.
DR EMBL; BC069425; AAH69425.1; -; mRNA.
DR EMBL; BC069449; AAH69449.1; -; mRNA.
DR EMBL; BC069487; AAH69487.1; -; mRNA.
DR EMBL; BC069523; AAH69523.1; -; mRNA.
DR EMBL; BC069559; AAH69559.1; -; mRNA.
DR EMBL; BC074948; AAH74948.1; -; mRNA.
DR EMBL; BC074949; AAH74949.1; -; mRNA.
DR EMBL; BC117386; AAI17387.1; -; mRNA.
DR EMBL; BC117390; AAI17391.1; -; mRNA.
DR CCDS; CCDS1470.1; -. [Q9NYY1-1]
DR RefSeq; NP_061194.2; NM_018724.3. [Q9NYY1-1]
DR PDB; 4DOH; X-ray; 2.80 A; A/C=25-176.
DR PDBsum; 4DOH; -.
DR AlphaFoldDB; Q9NYY1; -.
DR SMR; Q9NYY1; -.
DR BioGRID; 119086; 12.
DR IntAct; Q9NYY1; 3.
DR STRING; 9606.ENSP00000356065; -.
DR ChEMBL; CHEMBL3713449; -.
DR iPTMnet; Q9NYY1; -.
DR PhosphoSitePlus; Q9NYY1; -.
DR BioMuta; IL20; -.
DR DMDM; 38258955; -.
DR MassIVE; Q9NYY1; -.
DR PaxDb; Q9NYY1; -.
DR PeptideAtlas; Q9NYY1; -.
DR PRIDE; Q9NYY1; -.
DR ProteomicsDB; 61496; -.
DR ProteomicsDB; 83298; -. [Q9NYY1-1]
DR ABCD; Q9NYY1; 2 sequenced antibodies.
DR Antibodypedia; 34589; 476 antibodies from 31 providers.
DR DNASU; 50604; -.
DR Ensembl; ENST00000367096.7; ENSP00000356063.3; ENSG00000162891.11. [Q9NYY1-1]
DR Ensembl; ENST00000367098.6; ENSP00000356065.1; ENSG00000162891.11. [Q9NYY1-1]
DR Ensembl; ENST00000391930.3; ENSP00000375796.2; ENSG00000162891.11. [Q9NYY1-2]
DR GeneID; 50604; -.
DR KEGG; hsa:50604; -.
DR MANE-Select; ENST00000367098.6; ENSP00000356065.1; NM_018724.4; NP_061194.2.
DR UCSC; uc001her.4; human. [Q9NYY1-1]
DR CTD; 50604; -.
DR DisGeNET; 50604; -.
DR GeneCards; IL20; -.
DR HGNC; HGNC:6002; IL20.
DR HPA; ENSG00000162891; Not detected.
DR MIM; 605619; gene.
DR neXtProt; NX_Q9NYY1; -.
DR OpenTargets; ENSG00000162891; -.
DR PharmGKB; PA29817; -.
DR VEuPathDB; HostDB:ENSG00000162891; -.
DR eggNOG; ENOG502S5RZ; Eukaryota.
DR GeneTree; ENSGT00950000183124; -.
DR HOGENOM; CLU_098690_0_0_1; -.
DR InParanoid; Q9NYY1; -.
DR OMA; TVHTHEL; -.
DR OrthoDB; 1189017at2759; -.
DR PhylomeDB; Q9NYY1; -.
DR TreeFam; TF333253; -.
DR PathwayCommons; Q9NYY1; -.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q9NYY1; -.
DR SIGNOR; Q9NYY1; -.
DR BioGRID-ORCS; 50604; 7 hits in 1062 CRISPR screens.
DR GenomeRNAi; 50604; -.
DR Pharos; Q9NYY1; Tbio.
DR PRO; PR:Q9NYY1; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NYY1; protein.
DR Bgee; ENSG00000162891; Expressed in pancreatic ductal cell and 69 other tissues.
DR Genevisible; Q9NYY1; HS.
DR GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0045517; F:interleukin-20 receptor binding; TAS:UniProtKB.
DR GO; GO:0045518; F:interleukin-22 receptor binding; IEA:Ensembl.
DR GO; GO:0030316; P:osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0045606; P:positive regulation of epidermal cell differentiation; TAS:UniProtKB.
DR GO; GO:0045618; P:positive regulation of keratinocyte differentiation; TAS:UniProtKB.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; TAS:UniProtKB.
DR GO; GO:0050727; P:regulation of inflammatory response; TAS:UniProtKB.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020443; IL-10/19/20/22/24/26_fam.
DR InterPro; IPR020423; IL-10_CS.
DR InterPro; IPR020442; IL-20.
DR Pfam; PF00726; IL10; 1.
DR PRINTS; PR01935; INTRLEUKIN20.
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; Alternative splicing; Cytokine; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..176
FT /note="Interleukin-20"
FT /id="PRO_0000015381"
FT DISULFID 33..126
FT /evidence="ECO:0000269|PubMed:22802649"
FT DISULFID 80..132
FT /evidence="ECO:0000269|PubMed:22802649"
FT DISULFID 81..134
FT /evidence="ECO:0000269|PubMed:22802649"
FT VAR_SEQ 127..151
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16511554"
FT /id="VSP_054904"
FT VARIANT 107
FT /note="R -> Q (in dbSNP:rs35856950)"
FT /id="VAR_049577"
FT CONFLICT 48
FT /note="E -> D (in Ref. 1; AAF36679)"
FT /evidence="ECO:0000305"
FT CONFLICT 126
FT /note="C -> S (in Ref. 3; AAQ88686)"
FT /evidence="ECO:0000305"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:4DOH"
FT STRAND 33..37
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 39..47
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 50..55
FT /evidence="ECO:0007829|PDB:4DOH"
FT STRAND 67..69
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 76..93
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 95..97
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 103..128
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 136..151
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 154..162
FT /evidence="ECO:0007829|PDB:4DOH"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:4DOH"
SQ SEQUENCE 176 AA; 20072 MW; 8385992500B6C447 CRC64;
MKASSLAFSL LSAAFYLLWT PSTGLKTLNL GSCVIATNLQ EIRNGFSEIR GSVQAKDGNI
DIRILRRTES LQDTKPANRC CLLRHLLRLY LDRVFKNYQT PDHYTLRKIS SLANSFLTIK
KDLRLCHAHM TCHCGEEAMK KYSQILSHFE KLEPQAAVVK ALGELDILLQ WMEETE
