ID   IL24_MOUSE              Reviewed;         181 AA.
AC   Q925S4; Q925J3;
DT   11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=Interleukin-24;
DE            Short=IL-24;
DE   AltName: Full=IL-4-induced secreted protein;
DE   AltName: Full=Melanoma differentiation-associated gene 7 protein;
DE            Short=MDA-7;
DE   AltName: Full=Th2-specific cytokine FISP;
DE   Flags: Precursor;
GN   Name=Il24; Synonyms=Mda7;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=129/SvJ;
RA   Madireddi M.T., Lin J., Su Z.-Z., Shay J.W., Huberman E., Fisher P.B.;
RT   "Genomic structure, chromosomal localization and expression of melanoma
RT   differentiation associated gene-7 (mda-7): potential relationship with
RT   cellular senescence.";
RL   Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
RC   STRAIN=BALB/cJ;
RX   PubMed=11342597; DOI=10.4049/jimmunol.166.10.5859;
RA   Schaefer G., Venkataraman C., Schindler U.;
RT   "FISP (IL-4-induced secreted protein), a novel cytokine-like molecule
RT   secreted by Th2 cells.";
RL   J. Immunol. 166:5859-5863(2001).
RN   [3]
RP   FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX   PubMed=31907348; DOI=10.1038/s41419-019-2209-6;
RA   Wang J., Hu B., Zhao Z., Zhang H., Zhang H., Zhao Z., Ma X., Shen B.,
RA   Sun B., Huang X., Hou J., Xia Q.;
RT   "Intracellular XBP1-IL-24 axis dismantles cytotoxic unfolded protein
RT   response in the liver.";
RL   Cell Death Dis. 11:17-17(2020).
RN   [4]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=35148201; DOI=10.1126/sciimmunol.abi6763;
RA   Davidson S., Yu C.H., Steiner A., Ebstein F., Baker P.J., Jarur-Chamy V.,
RA   Hrovat Schaale K., Laohamonthonkul P., Kong K., Calleja D.J., Harapas C.R.,
RA   Balka K.R., Mitchell J., Jackson J.T., Geoghegan N.D., Moghaddas F.,
RA   Rogers K.L., Mayer-Barber K.D., De Jesus A.A., De Nardo D., Kile B.T.,
RA   Sadler A.J., Poli M.C., Krueger E., Goldbach Mansky R., Masters S.L.;
RT   "Protein kinase R is an innate immune sensor of proteotoxic stress via
RT   accumulation of cytoplasmic IL-24.";
RL   Sci. Immunol. 7:eabi6763-eabi6763(2022).
CC   -!- FUNCTION: Multifunctional cytokine mainly produced by T-cells that
CC       plays a regulatory role in immune response, tissue homeostasis, host
CC       defense, and oncogenesis (PubMed:31907348, PubMed:35148201). Possesses
CC       antiviral functions and induces the type I interferon response during
CC       influenza infection. Signals through two receptor complexes
CC       IL20RA/IL20RB or IL20RB/IL22RA1. In turn, stimulates the JAK1-STAT3 and
CC       MAPK pathways and promotes the secretion of pro-inflammatory mediators
CC       including IL8 and MMP1 (By similarity). Intracellularly, maintains
CC       endoplasmic reticulum homeostasis by restricting the eIF2alpha-CHOP
CC       pathway-mediated stress signal (PubMed:31907348). In addition, acts as
CC       a quality control mechanism for the ubiquitin proteasome system by
CC       alerting the cell to proteasome dysfunction through activation of
CC       PKR/EIF2AK2 (PubMed:35148201). {ECO:0000250|UniProtKB:Q13007,
CC       ECO:0000269|PubMed:31907348, ECO:0000269|PubMed:35148201}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q13007}.
CC   -!- TISSUE SPECIFICITY: Selectively expressed by Th2 cells
CC       (PubMed:11342597). Expressed in the liver (PubMed:31907348).
CC       {ECO:0000269|PubMed:11342597, ECO:0000269|PubMed:31907348}.
CC   -!- INDUCTION: By IL4. {ECO:0000269|PubMed:11342597}.
CC   -!- PTM: Glycosylated. {ECO:0000250|UniProtKB:Q13007}.
CC   -!- PTM: Ubiquitination at Lys-97 promotes proteasomal degradation.
CC       {ECO:0000250|UniProtKB:Q13007}.
CC   -!- DISRUPTION PHENOTYPE: IL24-deficient mice are more sensitive to CCL4-
CC       induced liver injury than WT counterparts.
CC       {ECO:0000269|PubMed:31907348}.
CC   -!- SIMILARITY: Belongs to the IL-10 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK52470.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF235006; AAK52590.1; -; mRNA.
DR   EMBL; AF333251; AAK52470.1; ALT_INIT; mRNA.
DR   CCDS; CCDS15262.2; -.
DR   RefSeq; NP_444325.2; NM_053095.2.
DR   AlphaFoldDB; Q925S4; -.
DR   SMR; Q925S4; -.
DR   STRING; 10090.ENSMUSP00000113064; -.
DR   GlyCosmos; Q925S4; 1 site, No reported glycans.
DR   GlyGen; Q925S4; 1 site.
DR   iPTMnet; Q925S4; -.
DR   PhosphoSitePlus; Q925S4; -.
DR   PaxDb; 10090-ENSMUSP00000113064; -.
DR   DNASU; 93672; -.
DR   GeneID; 93672; -.
DR   KEGG; mmu:93672; -.
DR   AGR; MGI:2135548; -.
DR   CTD; 11009; -.
DR   MGI; MGI:2135548; Il24.
DR   eggNOG; ENOG502SUXZ; Eukaryota.
DR   InParanoid; Q925S4; -.
DR   OrthoDB; 4633010at2759; -.
DR   PhylomeDB; Q925S4; -.
DR   TreeFam; TF333253; -.
DR   BioGRID-ORCS; 93672; 0 hits in 78 CRISPR screens.
DR   PRO; PR:Q925S4; -.
DR   Proteomes; UP000000589; Unplaced.
DR   RNAct; Q925S4; Protein.
DR   GO; GO:0005576; C:extracellular region; IDA:MGI.
DR   GO; GO:0005615; C:extracellular space; ISO:MGI.
DR   GO; GO:0005125; F:cytokine activity; ISA:MGI.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR   GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
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; IPR020444; IL-24.
DR   PANTHER; PTHR48394; INTERLEUKIN-19-RELATED; 1.
DR   PANTHER; PTHR48394:SF3; INTERLEUKIN-24; 1.
DR   Pfam; PF00726; IL10; 1.
DR   PRINTS; PR01937; INTRLEUKIN24.
DR   SUPFAM; SSF47266; 4-helical cytokines; 1.
DR   PROSITE; PS00520; INTERLEUKIN_10; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Cytokine; Disulfide bond; Glycoprotein; Isopeptide bond;
KW   Reference proteome; Secreted; Signal; Ubl conjugation.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..181
FT                   /note="Interleukin-24"
FT                   /id="PRO_0000042240"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..81
FT                   /evidence="ECO:0000250|UniProtKB:Q13007"
FT   CROSSLNK        97
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250|UniProtKB:Q13007"
FT   CONFLICT        31
FT                   /note="S -> F (in Ref. 2; AAK52470)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   181 AA;  20812 MW;  05CA43872D53D555 CRC64;
     MSWGLQILPC LSLILLLWNQ VPGLEGQEFR SGSCQVTGVV LPELWEAFWT VKNTVQTQDD
     ITSIRLLKPQ VLRNVSGAES CYLAHSLLKF YLNTVFKNYH SKIAKFKVLR SFSTLANNFI
     VIMSQLQPSK DNSMLPISES AHQRFLLFRR AFKQLDTEVA LVKAFGEVDI LLTWMQKFYH
     L
//