IL22_HUMAN
ID IL22_HUMAN Reviewed; 179 AA.
AC Q9GZX6;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Interleukin-22;
DE Short=IL-22;
DE AltName: Full=Cytokine Zcyto18;
DE AltName: Full=IL-10-related T-cell-derived-inducible factor;
DE Short=IL-TIF;
DE Flags: Precursor;
GN Name=IL22; Synonyms=ILTIF, ZCYTO18; ORFNames=UNQ3099/PRO10096;
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].
RX PubMed=10954742; DOI=10.1073/pnas.170291697;
RA Dumoutier L., Van Roost E., Colau D., Renauld J.-C.;
RT "Human interleukin-10-related T cell-derived inducible factor: molecular
RT cloning and functional characterization as an hepatocyte-stimulating
RT factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:10144-10149(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11197690; DOI=10.1038/sj.gene.6363716;
RA Dumoutier L., Van Roost E., Colau D., Ameye G., Michaux L., Renauld J.-C.;
RT "IL-TIF/IL-22: genomic organization and mapping of the human and mouse
RT genes.";
RL Genes Immun. 1:488-494(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10875937; DOI=10.1074/jbc.m005304200;
RA Xie M.-H., Aggarwal S., Ho W.-H., Foster J., Zhang Z., Stinson J.,
RA Wood W.I., Goddard A.D., Gurney A.L.;
RT "Interleukin (IL)-22, a novel human cytokine that signals through the
RT interferon receptor-related proteins CRF2-4 and IL-22R.";
RL J. Biol. Chem. 275:31335-31339(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLY-158.
RG SeattleSNPs variation discovery resource;
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [6]
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 [7]
RP PROTEIN SEQUENCE OF 34-48.
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 X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 29-179.
RX PubMed=11856845; DOI=10.1107/s0907444902001063;
RA Nagem R.A., Lucchesi K.W., Colau D., Dumoutier L., Renauld J.-C.,
RA Polikarpov I.;
RT "Crystallization and synchrotron X-ray diffraction studies of human
RT interleukin-22.";
RL Acta Crystallogr. D 58:529-530(2002).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 38-179, AND GLYCOSYLATION AT
RP ASN-54 AND ASN-97.
RX PubMed=15983417; DOI=10.1107/s0907444905009601;
RA Xu T., Logsdon N.J., Walter M.R.;
RT "Structure of insect-cell-derived IL-22.";
RL Acta Crystallogr. D 61:942-950(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 39-179 IN COMPLEX WITH IL22RA1,
RP AND DISULFIDE BONDS.
RX PubMed=18599299; DOI=10.1016/j.str.2008.06.005;
RA Jones B.C., Logsdon N.J., Walter M.R.;
RT "Structure of IL-22 bound to its high-affinity IL-22R1 chain.";
RL Structure 16:1333-1344(2008).
CC -!- FUNCTION: Cytokine that contributes to the inflammatory response in
CC vivo.
CC -!- INTERACTION:
CC Q9GZX6; Q08334: IL10RB; NbExp=2; IntAct=EBI-8040250, EBI-11175900;
CC Q9GZX6; Q8N6P7: IL22RA1; NbExp=9; IntAct=EBI-8040250, EBI-3940749;
CC PRO_0000015383; Q8N6P7: IL22RA1; NbExp=5; IntAct=EBI-11315863, EBI-3940749;
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il22/";
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL22ID44519ch12q15.html";
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DR EMBL; AJ277247; CAC06085.1; -; mRNA.
DR EMBL; AJ277248; CAC19409.1; -; Genomic_DNA.
DR EMBL; AF279437; AAG22064.1; -; mRNA.
DR EMBL; AY358890; AAQ89249.1; -; mRNA.
DR EMBL; AF387519; AAK62468.1; -; Genomic_DNA.
DR EMBL; BC066263; AAH66263.1; -; mRNA.
DR EMBL; BC067510; AAH67510.1; -; mRNA.
DR EMBL; BC069112; AAH69112.1; -; mRNA.
DR EMBL; BC069308; AAH69308.1; -; mRNA.
DR EMBL; BC070261; AAH70261.1; -; mRNA.
DR CCDS; CCDS8982.1; -.
DR RefSeq; NP_065386.1; NM_020525.4.
DR PDB; 1M4R; X-ray; 2.00 A; A/B=29-179.
DR PDB; 1YKB; X-ray; 2.60 A; A/B/C/D/E/F=38-179.
DR PDB; 3DGC; X-ray; 2.50 A; L/M=39-179.
DR PDB; 3DLQ; X-ray; 1.90 A; I=29-179.
DR PDB; 3G9V; X-ray; 2.76 A; B/D=29-179.
DR PDB; 3Q1S; X-ray; 2.15 A; I=29-179.
DR PDBsum; 1M4R; -.
DR PDBsum; 1YKB; -.
DR PDBsum; 3DGC; -.
DR PDBsum; 3DLQ; -.
DR PDBsum; 3G9V; -.
DR PDBsum; 3Q1S; -.
DR AlphaFoldDB; Q9GZX6; -.
DR SMR; Q9GZX6; -.
DR BioGRID; 119096; 6.
DR DIP; DIP-46035N; -.
DR IntAct; Q9GZX6; 3.
DR MINT; Q9GZX6; -.
DR STRING; 9606.ENSP00000442424; -.
DR BindingDB; Q9GZX6; -.
DR ChEMBL; CHEMBL3712915; -.
DR GlyGen; Q9GZX6; 3 sites.
DR iPTMnet; Q9GZX6; -.
DR PhosphoSitePlus; Q9GZX6; -.
DR BioMuta; IL22; -.
DR DMDM; 17366814; -.
DR jPOST; Q9GZX6; -.
DR MassIVE; Q9GZX6; -.
DR PaxDb; Q9GZX6; -.
DR PeptideAtlas; Q9GZX6; -.
DR PRIDE; Q9GZX6; -.
DR ProteomicsDB; 80167; -.
DR ABCD; Q9GZX6; 35 sequenced antibodies.
DR Antibodypedia; 16687; 927 antibodies from 42 providers.
DR DNASU; 50616; -.
DR Ensembl; ENST00000328087.6; ENSP00000329384.4; ENSG00000127318.11.
DR Ensembl; ENST00000538666.6; ENSP00000442424.1; ENSG00000127318.11.
DR GeneID; 50616; -.
DR KEGG; hsa:50616; -.
DR MANE-Select; ENST00000538666.6; ENSP00000442424.1; NM_020525.5; NP_065386.1.
DR UCSC; uc001sty.2; human.
DR CTD; 50616; -.
DR DisGeNET; 50616; -.
DR GeneCards; IL22; -.
DR HGNC; HGNC:14900; IL22.
DR HPA; ENSG00000127318; Tissue enhanced (urinary).
DR MIM; 605330; gene.
DR neXtProt; NX_Q9GZX6; -.
DR OpenTargets; ENSG00000127318; -.
DR PharmGKB; PA29822; -.
DR VEuPathDB; HostDB:ENSG00000127318; -.
DR eggNOG; ENOG502S5PC; Eukaryota.
DR GeneTree; ENSGT00510000048550; -.
DR HOGENOM; CLU_127397_0_0_1; -.
DR InParanoid; Q9GZX6; -.
DR OMA; YMQEVVS; -.
DR OrthoDB; 1406348at2759; -.
DR PhylomeDB; Q9GZX6; -.
DR TreeFam; TF333253; -.
DR PathwayCommons; Q9GZX6; -.
DR Reactome; R-HSA-8854691; Interleukin-20 family signaling.
DR SignaLink; Q9GZX6; -.
DR SIGNOR; Q9GZX6; -.
DR BioGRID-ORCS; 50616; 10 hits in 1058 CRISPR screens.
DR ChiTaRS; IL22; human.
DR EvolutionaryTrace; Q9GZX6; -.
DR GeneWiki; Interleukin_22; -.
DR GenomeRNAi; 50616; -.
DR Pharos; Q9GZX6; Tbio.
DR PRO; PR:Q9GZX6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9GZX6; protein.
DR Bgee; ENSG00000127318; Expressed in vermiform appendix and 57 other tissues.
DR Genevisible; Q9GZX6; HS.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0045518; F:interleukin-22 receptor binding; NAS:UniProtKB.
DR GO; GO:0006953; P:acute-phase response; NAS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; NAS:UniProtKB.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR020423; IL-10_CS.
DR InterPro; IPR020453; IL-22.
DR Pfam; PF14565; IL22; 1.
DR PIRSF; PIRSF037726; Interleukin-22; 1.
DR PRINTS; PR01936; INTRLEUKIN22.
DR SUPFAM; SSF47266; SSF47266; 1.
DR PROSITE; PS00520; INTERLEUKIN_10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
KW Glycoprotein; Reference proteome; Secreted; Signal.
FT SIGNAL 1..33
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 34..179
FT /note="Interleukin-22"
FT /id="PRO_0000015383"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15983417"
FT CARBOHYD 68
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 97
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:15983417"
FT DISULFID 40..132
FT /evidence="ECO:0000269|PubMed:18599299"
FT DISULFID 89..178
FT /evidence="ECO:0000269|PubMed:18599299"
FT VARIANT 158
FT /note="S -> G (in dbSNP:rs2227507)"
FT /evidence="ECO:0000269|Ref.5"
FT /id="VAR_013078"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 50..65
FT /evidence="ECO:0007829|PDB:3DLQ"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:1M4R"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 88..102
FT /evidence="ECO:0007829|PDB:3DLQ"
FT TURN 103..109
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 114..129
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 141..155
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:3DLQ"
FT HELIX 167..178
FT /evidence="ECO:0007829|PDB:3DLQ"
SQ SEQUENCE 179 AA; 20011 MW; 3C35E64D60CF8767 CRC64;
MAALQKSVSS FLMGTLATSC LLLLALLVQG GAAAPISSHC RLDKSNFQQP YITNRTFMLA
KEASLADNNT DVRLIGEKLF HGVSMSERCY LMKQVLNFTL EEVLFPQSDR FQPYMQEVVP
FLARLSNRLS TCHIEGDDLH IQRNVQKLKD TVKKLGESGE IKAIGELDLL FMSLRNACI
