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Interleukin-23 subunit alpha (IL-23 subunit alpha) (IL-23-A) (Interleukin-23 subunit p19) (IL-23p19)

 IL23A_HUMAN             Reviewed;         189 AA.
Q9NPF7; Q6NZ80; Q6NZ82; Q9H2A5;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
27-SEP-2017, entry version 131.
RecName: Full=Interleukin-23 subunit alpha;
Short=IL-23 subunit alpha;
Short=IL-23-A;
AltName: Full=Interleukin-23 subunit p19;
Short=IL-23p19;
Flags: Precursor;
Name=IL23A; Synonyms=SGRF; ORFNames=UNQ2498/PRO5798;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH IL12B,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11114383; DOI=10.1016/S1074-7613(00)00070-4;
Oppmann B., Lesley R., Blom B., Timans J.C., Xu Y., Hunte B., Vega F.,
Yu N., Wang J., Singh K.P., Zonin F., Vaisberg E., Churakova T.,
Liu M.-R., Gorman D., Wagner J., Zurawski S., Liu Y.-J., Abrams J.S.,
Moore K.W., Rennick D.M., de Waal-Malefyt R., Hannum C., Bazan J.F.,
Kastelein R.A.;
"Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with
biological activities similar as well as distinct from IL-12.";
Immunity 13:715-725(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Spleen;
Hirata Y., Kosuge Y.;
"SGRF; a novel member of the IL-6/G-CSF family.";
Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, AND INTERACTION WITH IL12RB1 AND IL23R.
PubMed=12023369; DOI=10.4049/jimmunol.168.11.5699;
Parham C., Chirica M., Timans J., Vaisberg E., Travis M., Cheung J.,
Pflanz S., Zhang R., Singh K.P., Vega F., To W., Wagner J.,
O'Farrell A.-M., McClanahan T.K., Zurawski S., Hannum C., Gorman D.,
Rennick D.M., Kastelein R.A., de Waal Malefyt R., Moore K.W.;
"A receptor for the heterodimeric cytokine IL-23 is composed of IL-
12Rbeta1 and a novel cytokine receptor subunit, IL-23R.";
J. Immunol. 168:5699-5708(2002).
[6]
INDUCTION.
PubMed=12421946; DOI=10.4049/jimmunol.169.10.5673;
Pirhonen J., Matikainen S., Julkunen I.;
"Regulation of virus-induced IL-12 and IL-23 expression in human
macrophages.";
J. Immunol. 169:5673-5678(2002).
[7]
INDUCTION.
PubMed=15114670; DOI=10.1002/eji.200324815;
Smits H.H., van Beelen A.J., Hessle C., Westland R., de Jong E.,
Soeteman E., Wold A., Wierenga E.A., Kapsenberg M.L.;
"Commensal Gram-negative bacteria prime human dendritic cells for
enhanced IL-23 and IL-27 expression and enhanced Th1 development.";
Eur. J. Immunol. 34:1371-1380(2004).
[8]
INDUCTION.
PubMed=15486065; DOI=10.1182/blood-2004-05-1718;
Schnurr M., Toy T., Shin A., Wagner M., Cebon J., Maraskovsky E.;
"Extracellular nucleotide signaling by P2 receptors inhibits IL-12 and
enhances IL-23 expression in human dendritic cells: a novel role for
the cAMP pathway.";
Blood 105:1582-1589(2005).
[9]
INDUCTION.
PubMed=15731058; DOI=10.1128/IAI.73.3.1590-1597.2005;
Fedele G., Stefanelli P., Spensieri F., Fazio C., Mastrantonio P.,
Ausiello C.M.;
"Bordetella pertussis-infected human monocyte-derived dendritic cells
undergo maturation and induce Th1 polarization and interleukin-23
expression.";
Infect. Immun. 73:1590-1597(2005).
[10]
DEVELOPMENTAL STAGE.
PubMed=16342235; DOI=10.1002/eji.200535467;
Vanden Eijnden S., Goriely S., De Wit D., Goldman M., Willems F.;
"Preferential production of the IL-12(p40)/IL-23(p19) heterodimer by
dendritic cells from human newborns.";
Eur. J. Immunol. 36:21-26(2006).
[11]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=16424222; DOI=10.4049/jimmunol.176.3.1908;
Piskin G., Sylva-Steenland R.M.R., Bos J.D., Teunissen M.B.M.;
"In vitro and in situ expression of IL-23 by keratinocytes in healthy
skin and psoriasis lesions: enhanced expression in psoriatic skin.";
J. Immunol. 176:1908-1915(2006).
[12]
INDUCTION.
PubMed=16751425; DOI=10.4049/jimmunol.176.12.7768;
Vaknin-Dembinsky A., Balashov K., Weiner H.L.;
"IL-23 is increased in dendritic cells in multiple sclerosis and down-
regulation of IL-23 by antisense oligos increases dendritic cell IL-10
production.";
J. Immunol. 176:7768-7774(2006).
[13]
INDUCTION.
PubMed=16688182; DOI=10.1038/nature04808;
Langowski J.L., Zhang X., Wu L., Mattson J.D., Chen T., Smith K.,
Basham B., McClanahan T.K., Kastelein R.A., Oft M.;
"IL-23 promotes tumour incidence and growth.";
Nature 442:461-465(2006).
[14]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 20-189 IN COMPLEX WITH IL12B,
AND SUBUNIT.
PubMed=18680750; DOI=10.1016/j.jmb.2008.07.051;
Lupardus P.J., Garcia K.C.;
"The structure of interleukin-23 reveals the molecular basis of p40
subunit sharing with interleukin-12.";
J. Mol. Biol. 382:931-941(2008).
-!- FUNCTION: Associates with IL12B to form the IL-23 interleukin, a
heterodimeric cytokine which functions in innate and adaptive
immunity. IL-23 may constitute with IL-17 an acute response to
infection in peripheral tissues. IL-23 binds to a heterodimeric
receptor complex composed of IL12RB1 and IL23R, activates the Jak-
Stat signaling cascade, stimulates memory rather than naive T-
cells and promotes production of proinflammatory cytokines. IL-23
induces autoimmune inflammation and thus may be responsible for
autoimmune inflammatory diseases and may be important for
tumorigenesis. {ECO:0000269|PubMed:11114383,
ECO:0000269|PubMed:12023369, ECO:0000269|PubMed:16424222}.
-!- SUBUNIT: Heterodimer with IL12B; disulfide-linked. The heterodimer
is known as interleukin IL-23. {ECO:0000269|PubMed:18680750}.
-!- INTERACTION:
P29460:IL12B; NbExp=4; IntAct=EBI-2481154, EBI-1029614;
P40855:PEX19; NbExp=5; IntAct=EBI-2481154, EBI-594747;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11114383}.
Note=Secreted upon association with IL12B.
-!- TISSUE SPECIFICITY: Secreted by activated dendritic and phagocytic
cells and keratinocytes. Also expressed by dermal Langerhans cells
(at protein level). {ECO:0000269|PubMed:11114383,
ECO:0000269|PubMed:16424222}.
-!- DEVELOPMENTAL STAGE: Expressed by newborns dendritic cells.
{ECO:0000269|PubMed:16342235}.
-!- INDUCTION: Up-regulated by a wide array of pathogens and pathogen-
products together with self-signals for danger or injury. Up-
regulated in psoriatic dermal tissues, in dendritic cells of
multiple sclerosis patients and in tumors.
{ECO:0000269|PubMed:12421946, ECO:0000269|PubMed:15114670,
ECO:0000269|PubMed:15486065, ECO:0000269|PubMed:15731058,
ECO:0000269|PubMed:16424222, ECO:0000269|PubMed:16688182,
ECO:0000269|PubMed:16751425}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/IL23AID44517ch12q13.html";
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EMBL; AF301620; AAG37232.1; -; mRNA.
EMBL; AB030000; BAA93686.1; -; mRNA.
EMBL; AB030001; BAA93687.1; -; Genomic_DNA.
EMBL; AY359083; AAQ89442.1; -; mRNA.
EMBL; BC066267; AAH66267.1; -; mRNA.
EMBL; BC066268; AAH66268.1; -; mRNA.
EMBL; BC066269; AAH66269.1; -; mRNA.
EMBL; BC067511; AAH67511.1; -; mRNA.
EMBL; BC067512; AAH67512.1; -; mRNA.
EMBL; BC067513; AAH67513.1; -; mRNA.
CCDS; CCDS8916.1; -.
RefSeq; NP_057668.1; NM_016584.2.
RefSeq; XP_011536779.1; XM_011538477.2.
UniGene; Hs.382212; -.
UniGene; Hs.98309; -.
PDB; 3D85; X-ray; 1.90 A; C=20-189.
PDB; 3D87; X-ray; 2.90 A; A/C=20-189.
PDB; 3DUH; X-ray; 2.30 A; C/D=20-189.
PDB; 3QWR; X-ray; 3.25 A; B=20-189.
PDB; 4GRW; X-ray; 2.55 A; A/C=1-189.
PDB; 5MJ3; X-ray; 1.74 A; B=20-189.
PDB; 5MJ4; X-ray; 3.40 A; B=20-189.
PDBsum; 3D85; -.
PDBsum; 3D87; -.
PDBsum; 3DUH; -.
PDBsum; 3QWR; -.
PDBsum; 4GRW; -.
PDBsum; 5MJ3; -.
PDBsum; 5MJ4; -.
ProteinModelPortal; Q9NPF7; -.
SMR; Q9NPF7; -.
BioGrid; 119611; 7.
IntAct; Q9NPF7; 4.
STRING; 9606.ENSP00000228534; -.
ChEMBL; CHEMBL3580502; -.
DrugBank; DB05459; Briakinumab.
DrugBank; DB05679; Ustekinumab.
BioMuta; IL23A; -.
DMDM; 74761641; -.
PaxDb; Q9NPF7; -.
PeptideAtlas; Q9NPF7; -.
PRIDE; Q9NPF7; -.
DNASU; 51561; -.
Ensembl; ENST00000228534; ENSP00000228534; ENSG00000110944.
GeneID; 51561; -.
KEGG; hsa:51561; -.
UCSC; uc001sla.4; human.
CTD; 51561; -.
DisGeNET; 51561; -.
EuPathDB; HostDB:ENSG00000110944.8; -.
GeneCards; IL23A; -.
HGNC; HGNC:15488; IL23A.
HPA; HPA001554; -.
MIM; 605580; gene.
neXtProt; NX_Q9NPF7; -.
OpenTargets; ENSG00000110944; -.
PharmGKB; PA29824; -.
eggNOG; ENOG410IGBY; Eukaryota.
eggNOG; ENOG411142Q; LUCA.
GeneTree; ENSGT00390000006482; -.
HOGENOM; HOG000048728; -.
HOVERGEN; HBG081786; -.
InParanoid; Q9NPF7; -.
KO; K05426; -.
OMA; PMGHVDL; -.
OrthoDB; EOG091G0Q9J; -.
PhylomeDB; Q9NPF7; -.
TreeFam; TF337234; -.
Reactome; R-HSA-447115; Interleukin-12 family signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; Q9NPF7; -.
SIGNOR; Q9NPF7; -.
EvolutionaryTrace; Q9NPF7; -.
GeneWiki; Interleukin_23; -.
GenomeRNAi; 51561; -.
PRO; PR:Q9NPF7; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000110944; -.
CleanEx; HS_IL23A; -.
Genevisible; Q9NPF7; HS.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0070743; C:interleukin-23 complex; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0045519; F:interleukin-23 receptor binding; IEA:Ensembl.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IDA:BHF-UCL.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IMP:BHF-UCL.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:BHF-UCL.
GO; GO:0010536; P:positive regulation of activation of Janus kinase activity; IDA:BHF-UCL.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IDA:BHF-UCL.
GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IDA:BHF-UCL.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IDA:BHF-UCL.
GO; GO:0032733; P:positive regulation of interleukin-10 production; IDA:BHF-UCL.
GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:BHF-UCL.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0043382; P:positive regulation of memory T cell differentiation; ISS:BHF-UCL.
GO; GO:0032816; P:positive regulation of natural killer cell activation; IC:BHF-UCL.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:0090023; P:positive regulation of neutrophil chemotaxis; IEA:Ensembl.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; TAS:BHF-UCL.
GO; GO:0051135; P:positive regulation of NK T cell activation; IDA:BHF-UCL.
GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:BHF-UCL.
GO; GO:0001916; P:positive regulation of T cell mediated cytotoxicity; ISS:BHF-UCL.
GO; GO:0042102; P:positive regulation of T cell proliferation; IDA:BHF-UCL.
GO; GO:0002827; P:positive regulation of T-helper 1 type immune response; IDA:BHF-UCL.
GO; GO:2000330; P:positive regulation of T-helper 17 cell lineage commitment; ISS:BHF-UCL.
GO; GO:2000318; P:positive regulation of T-helper 17 type immune response; ISS:BHF-UCL.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0042509; P:regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0042098; P:T cell proliferation; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:UniProtKB-KW.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR010831; IL-23_alpha.
PANTHER; PTHR15947; PTHR15947; 1.
Pfam; PF16649; IL23; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; Cytokine;
Disulfide bond; Immunity; Inflammatory response; Innate immunity;
Reference proteome; Secreted; Signal; Tissue remodeling.
SIGNAL 1 19 {ECO:0000255}.
CHAIN 20 189 Interleukin-23 subunit alpha.
/FTId=PRO_0000259488.
CONFLICT 122 122 G -> A (in Ref. 1; AAG37232).
{ECO:0000305}.
CONFLICT 147 147 I -> M (in Ref. 4; AAH66267).
{ECO:0000305}.
CONFLICT 168 168 S -> N (in Ref. 4; AAH66267).
{ECO:0000305}.
CONFLICT 173 173 V -> A (in Ref. 4; AAH66269).
{ECO:0000305}.
CONFLICT 189 189 P -> L (in Ref. 4; AAH66269).
{ECO:0000305}.
HELIX 30 46 {ECO:0000244|PDB:5MJ3}.
TURN 49 51 {ECO:0000244|PDB:3D87}.
TURN 53 56 {ECO:0000244|PDB:5MJ4}.
HELIX 61 67 {ECO:0000244|PDB:5MJ3}.
HELIX 73 75 {ECO:0000244|PDB:3D85}.
HELIX 79 85 {ECO:0000244|PDB:5MJ3}.
HELIX 87 104 {ECO:0000244|PDB:5MJ3}.
HELIX 107 110 {ECO:0000244|PDB:5MJ3}.
STRAND 111 113 {ECO:0000244|PDB:5MJ3}.
HELIX 120 135 {ECO:0000244|PDB:5MJ3}.
STRAND 136 138 {ECO:0000244|PDB:3D87}.
HELIX 155 186 {ECO:0000244|PDB:5MJ3}.
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


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