IL23A_HUMAN
ID IL23A_HUMAN Reviewed; 189 AA.
AC Q9NPF7; Q6NZ80; Q6NZ82; Q9H2A5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Interleukin-23 subunit alpha;
DE Short=IL-23 subunit alpha;
DE Short=IL-23-A;
DE AltName: Full=Interleukin-23 subunit p19;
DE Short=IL-23p19;
DE Flags: Precursor;
GN Name=IL23A; Synonyms=SGRF; ORFNames=UNQ2498/PRO5798;
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], FUNCTION, INTERACTION WITH IL12B, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=11114383; DOI=10.1016/s1074-7613(00)00070-4;
RA Oppmann B., Lesley R., Blom B., Timans J.C., Xu Y., Hunte B., Vega F.,
RA Yu N., Wang J., Singh K.P., Zonin F., Vaisberg E., Churakova T., Liu M.-R.,
RA Gorman D., Wagner J., Zurawski S., Liu Y.-J., Abrams J.S., Moore K.W.,
RA Rennick D.M., de Waal-Malefyt R., Hannum C., Bazan J.F., Kastelein R.A.;
RT "Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with
RT biological activities similar as well as distinct from IL-12.";
RL Immunity 13:715-725(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RC TISSUE=Spleen;
RA Hirata Y., Kosuge Y.;
RT "SGRF; a novel member of the IL-6/G-CSF family.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [5]
RP FUNCTION, AND INTERACTION WITH IL12RB1 AND IL23R.
RX PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699;
RA Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J.,
RA Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J.,
RA O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D.,
RA Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.;
RT "A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1
RT and a novel cytokine receptor subunit, IL-23R.";
RL J. Immunol. 168:5699-5708(2002).
RN [6]
RP INDUCTION.
RX PubMed=12421946; DOI=10.4049/jimmunol.169.10.5673;
RA Pirhonen J., Matikainen S., Julkunen I.;
RT "Regulation of virus-induced IL-12 and IL-23 expression in human
RT macrophages.";
RL J. Immunol. 169:5673-5678(2002).
RN [7]
RP INDUCTION.
RX PubMed=15114670; DOI=10.1002/eji.200324815;
RA Smits H.H., van Beelen A.J., Hessle C., Westland R., de Jong E.,
RA Soeteman E., Wold A., Wierenga E.A., Kapsenberg M.L.;
RT "Commensal Gram-negative bacteria prime human dendritic cells for enhanced
RT IL-23 and IL-27 expression and enhanced Th1 development.";
RL Eur. J. Immunol. 34:1371-1380(2004).
RN [8]
RP INDUCTION.
RX PubMed=15486065; DOI=10.1182/blood-2004-05-1718;
RA Schnurr M., Toy T., Shin A., Wagner M., Cebon J., Maraskovsky E.;
RT "Extracellular nucleotide signaling by P2 receptors inhibits IL-12 and
RT enhances IL-23 expression in human dendritic cells: a novel role for the
RT cAMP pathway.";
RL Blood 105:1582-1589(2005).
RN [9]
RP INDUCTION.
RX PubMed=15731058; DOI=10.1128/iai.73.3.1590-1597.2005;
RA Fedele G., Stefanelli P., Spensieri F., Fazio C., Mastrantonio P.,
RA Ausiello C.M.;
RT "Bordetella pertussis-infected human monocyte-derived dendritic cells
RT undergo maturation and induce Th1 polarization and interleukin-23
RT expression.";
RL Infect. Immun. 73:1590-1597(2005).
RN [10]
RP DEVELOPMENTAL STAGE.
RX PubMed=16342235; DOI=10.1002/eji.200535467;
RA Vanden Eijnden S., Goriely S., De Wit D., Goldman M., Willems F.;
RT "Preferential production of the IL-12(p40)/IL-23(p19) heterodimer by
RT dendritic cells from human newborns.";
RL Eur. J. Immunol. 36:21-26(2006).
RN [11]
RP FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
RX PubMed=16424222; DOI=10.4049/jimmunol.176.3.1908;
RA Piskin G., Sylva-Steenland R.M.R., Bos J.D., Teunissen M.B.M.;
RT "In vitro and in situ expression of IL-23 by keratinocytes in healthy skin
RT and psoriasis lesions: enhanced expression in psoriatic skin.";
RL J. Immunol. 176:1908-1915(2006).
RN [12]
RP INDUCTION.
RX PubMed=16751425; DOI=10.4049/jimmunol.176.12.7768;
RA Vaknin-Dembinsky A., Balashov K., Weiner H.L.;
RT "IL-23 is increased in dendritic cells in multiple sclerosis and down-
RT regulation of IL-23 by antisense oligos increases dendritic cell IL-10
RT production.";
RL J. Immunol. 176:7768-7774(2006).
RN [13]
RP INDUCTION.
RX PubMed=16688182; DOI=10.1038/nature04808;
RA Langowski J.L., Zhang X., Wu L., Mattson J.D., Chen T., Smith K.,
RA Basham B., McClanahan T.K., Kastelein R.A., Oft M.;
RT "IL-23 promotes tumour incidence and growth.";
RL Nature 442:461-465(2006).
RN [14]
RP FUNCTION.
RX PubMed=17676044; DOI=10.1038/ni1497;
RA Wilson N.J., Boniface K., Chan J.R., McKenzie B.S., Blumenschein W.M.,
RA Mattson J.D., Basham B., Smith K., Chen T., Morel F., Lecron J.C.,
RA Kastelein R.A., Cua D.J., McClanahan T.K., Bowman E.P., de Waal Malefyt R.;
RT "Development, cytokine profile and function of human interleukin 17-
RT producing helper T cells.";
RL Nat. Immunol. 8:950-957(2007).
RN [15]
RP FUNCTION IN BACTERIAL CLEARANCE.
RX PubMed=32474165; DOI=10.1016/j.jcmgh.2020.05.007;
RA Sun R., Abraham C.;
RT "IL23 Promotes Antimicrobial Pathways in Human Macrophages, Which Are
RT Reduced With the IBD-Protective IL23R R381Q Variant.";
RL Cell. Mol. Gastroenterol. Hepatol. 10:673-697(2020).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-189 IN COMPLEX WITH IL12B, AND
RP SUBUNIT.
RX PubMed=18680750; DOI=10.1016/j.jmb.2008.07.051;
RA Lupardus P.J., Garcia K.C.;
RT "The structure of interleukin-23 reveals the molecular basis of p40 subunit
RT sharing with interleukin-12.";
RL J. Mol. Biol. 382:931-941(2008).
RN [17] {ECO:0007744|PDB:5MXA, ECO:0007744|PDB:5MZV, ECO:0007744|PDB:5NJD}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH IL23R, DISULFIDE
RP BOND, AND FUNCTION.
RX PubMed=29287995; DOI=10.1016/j.immuni.2017.12.008;
RA Bloch Y., Bouchareychas L., Merceron R., Skladanowska K.,
RA Van den Bossche L., Detry S., Govindarajan S., Elewaut D., Haerynck F.,
RA Dullaers M., Adamopoulos I.E., Savvides S.N.;
RT "Structural Activation of Pro-inflammatory Human Cytokine IL-23 by Cognate
RT IL-23 Receptor Enables Recruitment of the Shared Receptor IL-12Rbeta1.";
RL Immunity 48:45-58.e6(2018).
RN [18] {ECO:0007744|PDB:6UIB}
RP X-RAY CRYSTALLOGRAPHY (2.74 ANGSTROMS) OF 20-189, AND DISULFIDE BOND.
RX PubMed=32479512; DOI=10.1371/journal.pone.0233961;
RA Pandya P., Sayers R.O., Ting J.P., Morshedian S., Torres C., Cudal J.S.,
RA Zhang K., Fitchett J.R., Zhang Q., Zhang F.F., Wang J., Durbin J.D.,
RA Carrillo J.J., Espada A., Broughton H., Qian Y., Afshar S.;
RT "Integration of phage and yeast display platforms: A reliable and cost
RT effective approach for binning of peptides as displayed on-phage.";
RL PLoS ONE 15:0-0(2020).
RN [19] {ECO:0007744|PDB:6WDQ}
RP X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 28-189 IN COMPLEX WITH IL23R AND
RP IL12RB1, DISULFIDE BOND, AND FUNCTION.
RX PubMed=33606986; DOI=10.1016/j.cell.2021.01.018;
RA Glassman C.R., Mathiharan Y.K., Jude K.M., Su L., Panova O., Lupardus P.J.,
RA Spangler J.B., Ely L.K., Thomas C., Skiniotis G., Garcia K.C.;
RT "Structural basis for IL-12 and IL-23 receptor sharing reveals a gateway
RT for shaping actions on T versus NK cells.";
RL Cell 184:983-999.e24(2021).
CC -!- FUNCTION: Associates with IL12B to form the pro-inflammatory cytokine
CC IL-23 that plays different roles in innate and adaptive immunity
CC (PubMed:11114383). Released by antigen-presenting cells such as
CC dendritic cells or macrophages, binds to a heterodimeric receptor
CC complex composed of IL12RB1 and IL23R to activate JAK2 and TYK2 which
CC then phosphorylate the receptor to form a docking site leading to the
CC phosphorylation of STAT3 and STAT4 (PubMed:32474165, PubMed:29287995,
CC PubMed:33606986). This process leads to activation of several pathways
CC including p38 MAPK or NF-kappa-B and promotes the production of pro-
CC inflammatory cytokines such as interleukin-17A/IL17A (PubMed:12023369).
CC In turn, participates in the early and effective intracellular
CC bacterial clearance (PubMed:32474165). Promotes the expansion and
CC survival of T-helper 17 cells, a CD4-positive helper T-cell subset that
CC produces IL-17, as well as other IL-17-producing cells
CC (PubMed:17676044). {ECO:0000269|PubMed:11114383,
CC ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:16424222,
CC ECO:0000269|PubMed:17676044, ECO:0000269|PubMed:29287995,
CC ECO:0000269|PubMed:32474165, ECO:0000269|PubMed:33606986}.
CC -!- SUBUNIT: Heterodimer with IL12B; disulfide-linked (PubMed:11114383,
CC PubMed:18680750). The heterodimer is known as interleukin IL-23
CC (PubMed:11114383, PubMed:18680750). Interacts with IL23R; this
CC interaction enables recruitment of IL12RB1 (PubMed:29287995,
CC PubMed:33606986). {ECO:0000269|PubMed:11114383,
CC ECO:0000269|PubMed:18680750, ECO:0000269|PubMed:29287995,
CC ECO:0000269|PubMed:33606986}.
CC -!- INTERACTION:
CC Q9NPF7; P29460: IL12B; NbExp=6; IntAct=EBI-2481154, EBI-1029614;
CC Q9NPF7; P40855: PEX19; NbExp=6; IntAct=EBI-2481154, EBI-594747;
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11114383}.
CC Note=Secreted upon association with IL12B.
CC -!- TISSUE SPECIFICITY: Secreted by activated dendritic and phagocytic
CC cells and keratinocytes. Also expressed by dermal Langerhans cells (at
CC protein level). {ECO:0000269|PubMed:11114383,
CC ECO:0000269|PubMed:16424222}.
CC -!- DEVELOPMENTAL STAGE: Expressed by newborns dendritic cells.
CC {ECO:0000269|PubMed:16342235}.
CC -!- INDUCTION: Up-regulated by a wide array of pathogens and pathogen-
CC products together with self-signals for danger or injury. Up-regulated
CC in psoriatic dermal tissues, in dendritic cells of multiple sclerosis
CC patients and in tumors. {ECO:0000269|PubMed:12421946,
CC ECO:0000269|PubMed:15114670, ECO:0000269|PubMed:15486065,
CC ECO:0000269|PubMed:15731058, ECO:0000269|PubMed:16424222,
CC ECO:0000269|PubMed:16688182, ECO:0000269|PubMed:16751425}.
CC -!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/IL23AID44517ch12q13.html";
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DR EMBL; AF301620; AAG37232.1; -; mRNA.
DR EMBL; AB030000; BAA93686.1; -; mRNA.
DR EMBL; AB030001; BAA93687.1; -; Genomic_DNA.
DR EMBL; AY359083; AAQ89442.1; -; mRNA.
DR EMBL; BC066267; AAH66267.1; -; mRNA.
DR EMBL; BC066268; AAH66268.1; -; mRNA.
DR EMBL; BC066269; AAH66269.1; -; mRNA.
DR EMBL; BC067511; AAH67511.1; -; mRNA.
DR EMBL; BC067512; AAH67512.1; -; mRNA.
DR EMBL; BC067513; AAH67513.1; -; mRNA.
DR CCDS; CCDS8916.1; -.
DR RefSeq; NP_057668.1; NM_016584.2.
DR RefSeq; XP_011536779.1; XM_011538477.2.
DR PDB; 3D85; X-ray; 1.90 A; C=20-189.
DR PDB; 3D87; X-ray; 2.90 A; A/C=20-189.
DR PDB; 3DUH; X-ray; 2.30 A; C/D=20-189.
DR PDB; 3QWR; X-ray; 3.25 A; B=20-189.
DR PDB; 4GRW; X-ray; 2.55 A; A/C=1-189.
DR PDB; 5MJ3; X-ray; 1.74 A; B=20-189.
DR PDB; 5MJ4; X-ray; 3.40 A; B=20-189.
DR PDB; 5MXA; X-ray; 2.50 A; B=1-189.
DR PDB; 5MZV; X-ray; 2.80 A; B=1-189.
DR PDB; 5NJD; X-ray; 3.90 A; B/D/F/H/J/L=1-189.
DR PDB; 6UIB; X-ray; 2.74 A; A=20-189.
DR PDB; 6WDQ; X-ray; 3.40 A; B=28-189.
DR PDBsum; 3D85; -.
DR PDBsum; 3D87; -.
DR PDBsum; 3DUH; -.
DR PDBsum; 3QWR; -.
DR PDBsum; 4GRW; -.
DR PDBsum; 5MJ3; -.
DR PDBsum; 5MJ4; -.
DR PDBsum; 5MXA; -.
DR PDBsum; 5MZV; -.
DR PDBsum; 5NJD; -.
DR PDBsum; 6UIB; -.
DR PDBsum; 6WDQ; -.
DR AlphaFoldDB; Q9NPF7; -.
DR SMR; Q9NPF7; -.
DR BioGRID; 119611; 9.
DR ComplexPortal; CPX-3290; Interleukin-23 complex.
DR ComplexPortal; CPX-383; Interleukin-23-receptor complex.
DR IntAct; Q9NPF7; 6.
DR STRING; 9606.ENSP00000228534; -.
DR ChEMBL; CHEMBL2364154; -.
DR DrugBank; DB05459; Briakinumab.
DR DrugBank; DB11834; Guselkumab.
DR DrugBank; DB14762; Risankizumab.
DR DrugBank; DB14004; Tildrakizumab.
DR DrugBank; DB05679; Ustekinumab.
DR DrugCentral; Q9NPF7; -.
DR BioMuta; IL23A; -.
DR DMDM; 74761641; -.
DR MassIVE; Q9NPF7; -.
DR PaxDb; Q9NPF7; -.
DR PeptideAtlas; Q9NPF7; -.
DR PRIDE; Q9NPF7; -.
DR ABCD; Q9NPF7; 22 sequenced antibodies.
DR Antibodypedia; 803; 632 antibodies from 38 providers.
DR DNASU; 51561; -.
DR Ensembl; ENST00000228534.6; ENSP00000228534.4; ENSG00000110944.9.
DR GeneID; 51561; -.
DR KEGG; hsa:51561; -.
DR MANE-Select; ENST00000228534.6; ENSP00000228534.4; NM_016584.3; NP_057668.1.
DR UCSC; uc001sla.4; human.
DR CTD; 51561; -.
DR DisGeNET; 51561; -.
DR GeneCards; IL23A; -.
DR HGNC; HGNC:15488; IL23A.
DR HPA; ENSG00000110944; Tissue enriched (urinary).
DR MIM; 605580; gene.
DR neXtProt; NX_Q9NPF7; -.
DR OpenTargets; ENSG00000110944; -.
DR PharmGKB; PA29824; -.
DR VEuPathDB; HostDB:ENSG00000110944; -.
DR eggNOG; ENOG502STAQ; Eukaryota.
DR GeneTree; ENSGT00390000006482; -.
DR HOGENOM; CLU_122915_0_0_1; -.
DR InParanoid; Q9NPF7; -.
DR OMA; WARCQQL; -.
DR OrthoDB; 1344829at2759; -.
DR PhylomeDB; Q9NPF7; -.
DR TreeFam; TF337234; -.
DR PathwayCommons; Q9NPF7; -.
DR Reactome; R-HSA-6785807; Interleukin-4 and Interleukin-13 signaling.
DR Reactome; R-HSA-9020933; Interleukin-23 signaling.
DR SignaLink; Q9NPF7; -.
DR SIGNOR; Q9NPF7; -.
DR BioGRID-ORCS; 51561; 12 hits in 1024 CRISPR screens.
DR EvolutionaryTrace; Q9NPF7; -.
DR GeneWiki; Interleukin_23; -.
DR GenomeRNAi; 51561; -.
DR Pharos; Q9NPF7; Tclin.
DR PRO; PR:Q9NPF7; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9NPF7; protein.
DR Bgee; ENSG00000110944; Expressed in left testis and 109 other tissues.
DR Genevisible; Q9NPF7; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0070743; C:interleukin-23 complex; IDA:BHF-UCL.
DR GO; GO:0072536; C:interleukin-23 receptor complex; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR GO; GO:0045519; F:interleukin-23 receptor binding; IEA:Ensembl.
DR GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IC:ComplexPortal.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
DR GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
DR GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
DR GO; GO:0032816; P:positive regulation of natural killer cell activation; IC:BHF-UCL.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
DR GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; TAS:BHF-UCL.
DR GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
DR GO; GO:0046427; P:positive regulation of receptor signaling pathway via JAK-STAT; IDA:ComplexPortal.
DR GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
DR GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL.
DR GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:BHF-UCL.
DR GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; IDA:ComplexPortal.
DR GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
DR GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
DR GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.10; -; 1.
DR InterPro; IPR009079; 4_helix_cytokine-like_core.
DR InterPro; IPR010831; IL-23_alpha.
DR PANTHER; PTHR15947; PTHR15947; 1.
DR Pfam; PF16649; IL23; 1.
DR SUPFAM; SSF47266; SSF47266; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antiviral defense; Cytokine; Disulfide bond; Immunity;
KW Inflammatory response; Innate immunity; Reference proteome; Secreted;
KW Signal; Tissue remodeling.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..189
FT /note="Interleukin-23 subunit alpha"
FT /id="PRO_0000259488"
FT DISULFID 73
FT /note="Interchain (with C-119 in IL12A)"
FT /evidence="ECO:0000269|PubMed:29287995,
FT ECO:0000269|PubMed:32479512"
FT DISULFID 77..89
FT /evidence="ECO:0000269|PubMed:29287995,
FT ECO:0000269|PubMed:32479512, ECO:0000269|PubMed:33606986"
FT CONFLICT 122
FT /note="G -> A (in Ref. 1; AAG37232)"
FT /evidence="ECO:0000305"
FT CONFLICT 147
FT /note="I -> M (in Ref. 4; AAH66267)"
FT /evidence="ECO:0000305"
FT CONFLICT 168
FT /note="S -> N (in Ref. 4; AAH66267)"
FT /evidence="ECO:0000305"
FT CONFLICT 173
FT /note="V -> A (in Ref. 4; AAH66269)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="P -> L (in Ref. 4; AAH66269)"
FT /evidence="ECO:0000305"
FT HELIX 30..46
FT /evidence="ECO:0007829|PDB:5MJ3"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:3D87"
FT TURN 53..56
FT /evidence="ECO:0007829|PDB:5MJ4"
FT HELIX 61..67
FT /evidence="ECO:0007829|PDB:5MJ3"
FT HELIX 73..75
FT /evidence="ECO:0007829|PDB:3D85"
FT HELIX 79..85
FT /evidence="ECO:0007829|PDB:5MJ3"
FT HELIX 87..104
FT /evidence="ECO:0007829|PDB:5MJ3"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5MJ3"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:5MJ3"
FT STRAND 117..119
FT /evidence="ECO:0007829|PDB:6WDQ"
FT HELIX 120..135
FT /evidence="ECO:0007829|PDB:5MJ3"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:3D87"
FT HELIX 155..186
FT /evidence="ECO:0007829|PDB:5MJ3"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:6WDQ"
SQ SEQUENCE 189 AA; 20730 MW; 51B5C0F188EC1B9F CRC64;
MLGSRAVMLL LLLPWTAQGR AVPGGSSPAW TQCQQLSQKL CTLAWSAHPL VGHMDLREEG
DEETTNDVPH IQCGDGCDPQ GLRDNSQFCL QRIHQGLIFY EKLLGSDIFT GEPSLLPDSP
VGQLHASLLG LSQLLQPEGH HWETQQIPSL SPSQPWQRLL LRFKILRSLQ AFVAVAARVF
AHGAATLSP
