IL18_BOVIN
ID IL18_BOVIN Reviewed; 193 AA.
AC Q9TU73; A9QWR6; Q3SZF6;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Interleukin-18;
DE Short=IL-18;
DE AltName: Full=Interferon gamma-inducing factor;
DE Short=IFN-gamma-inducing factor;
DE AltName: Full=Interleukin-1 gamma;
DE Short=IL-1 gamma;
DE Flags: Precursor;
GN Name=IL18; Synonyms=IGIF;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=10547157; DOI=10.1089/107999099313118;
RA Shoda L.K., Zarlenga D.S., Hirano A., Brown W.C.;
RT "Cloning of a cDNA encoding bovine interleukin-18 and analysis of IL-18
RT expression in macrophages and its IFN-gamma-inducing activity.";
RL J. Interferon Cytokine Res. 19:1169-1177(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Belted Galloway; TISSUE=Peripheral blood;
RG U.S. Veterinary Immune Reagent Network;
RA Hudgens T., Tompkins D., Baldwin C.L.;
RT "U.S. veterinary immune reagent network: expressed bovine gene sequences.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pro-inflammatory cytokine primarily involved in epithelial
CC barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK)
CC cell immune responses. Upon binding to IL18R1 and IL18RAP, forms a
CC signaling ternary complex which activates NF-kappa-B, triggering
CC synthesis of inflammatory mediators. Synergizes with IL12/interleukin-
CC 12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural
CC killer (NK) cells. Involved in transduction of inflammation downstream
CC of pyroptosis: its mature form is specifically released in the
CC extracellular milieu by passing through the gasdermin-D (GSDMD) pore.
CC {ECO:0000250|UniProtKB:Q14116}.
CC -!- SUBUNIT: Forms a ternary complex with ligand-binding receptor subunit
CC IL18R1 and signaling receptor subunit IL18RAP at the plasma membrane.
CC Mature IL18 first binds to IL18R1 forming a low affinity binary
CC complex, which then interacts with IL18RAP to form a high affinity
CC ternary complex that signals inside the cell. Interacts with cargo
CC receptor TMED10; the interaction mediates the translocation from the
CC cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate
CC compartment) and thereby secretion. {ECO:0000250|UniProtKB:Q14116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14116}.
CC Secreted {ECO:0000250|UniProtKB:Q14116}. Note=The precursor is
CC cytosolic. In response to inflammasome-activating signals, cleaved and
CC secreted. Mature form is secreted and released in the extracellular
CC milieu by passing through the gasdermin-D (GSDMD) pore. In contrast,
CC the precursor form is not released, due to the presence of an acidic
CC region that is proteolytically removed by CASP1 during maturation. The
CC secretion is dependent on protein unfolding and facilitated by the
CC cargo receptor TMED10. {ECO:0000250|UniProtKB:Q14116}.
CC -!- PTM: The pro-IL-18 precursor is processed by CASP1 or CASP4 to yield
CC the active form. {ECO:0000250|UniProtKB:Q14116}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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DR EMBL; AF124789; AAF08686.1; -; mRNA.
DR EMBL; EU276078; ABX72076.1; -; mRNA.
DR EMBL; BC102879; AAI02880.1; -; mRNA.
DR RefSeq; NP_776516.1; NM_174091.2.
DR AlphaFoldDB; Q9TU73; -.
DR SMR; Q9TU73; -.
DR STRING; 9913.ENSBTAP00000055793; -.
DR PaxDb; Q9TU73; -.
DR Ensembl; ENSBTAT00000065052; ENSBTAP00000055793; ENSBTAG00000000277.
DR GeneID; 281249; -.
DR KEGG; bta:281249; -.
DR CTD; 3606; -.
DR VEuPathDB; HostDB:ENSBTAG00000000277; -.
DR VGNC; VGNC:30126; IL18.
DR eggNOG; ENOG502SDJZ; Eukaryota.
DR GeneTree; ENSGT00390000001053; -.
DR HOGENOM; CLU_113349_0_0_1; -.
DR InParanoid; Q9TU73; -.
DR OMA; GKNFCLY; -.
DR OrthoDB; 1190337at2759; -.
DR TreeFam; TF336297; -.
DR Proteomes; UP000009136; Chromosome 15.
DR Bgee; ENSBTAG00000000277; Expressed in abdominal lymph node and 100 other tissues.
DR ExpressionAtlas; Q9TU73; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005125; F:cytokine activity; ISS:UniProtKB.
DR GO; GO:0045515; F:interleukin-18 receptor binding; ISS:UniProtKB.
DR GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
DR GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
DR GO; GO:0008283; P:cell population proliferation; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0042632; P:cholesterol homeostasis; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; ISS:UniProtKB.
DR GO; GO:0061436; P:establishment of skin barrier; ISS:UniProtKB.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0035655; P:interleukin-18-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
DR GO; GO:0042267; P:natural killer cell mediated cytotoxicity; IEA:Ensembl.
DR GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
DR GO; GO:0042119; P:neutrophil activation; IEA:Ensembl.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0042104; P:positive regulation of activated T cell proliferation; IEA:Ensembl.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; IEA:Ensembl.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032740; P:positive regulation of interleukin-17 production; IEA:Ensembl.
DR GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Ensembl.
DR GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0051142; P:positive regulation of NK T cell proliferation; IEA:Ensembl.
DR GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IEA:Ensembl.
DR GO; GO:0042088; P:T-helper 1 type immune response; IEA:Ensembl.
DR GO; GO:0070328; P:triglyceride homeostasis; IEA:Ensembl.
DR InterPro; IPR015529; IL-18.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR008996; IL1/FGF.
DR Pfam; PF00340; IL1; 1.
DR PIRSF; PIRSF015162; Interleukin_18; 1.
DR PRINTS; PR01933; INTRLEUKIN18.
DR SUPFAM; SSF50353; SSF50353; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Cytoplasm; Inflammatory response; Reference proteome; Secreted.
FT PROPEP 1..36
FT /evidence="ECO:0000250|UniProtKB:P70380"
FT /id="PRO_0000015337"
FT CHAIN 37..193
FT /note="Interleukin-18"
FT /id="PRO_0000015338"
SQ SEQUENCE 193 AA; 22347 MW; 65720F199DEA49C4 CRC64;
MAAEQVEDYC ISFVEMKFIN NTLYFVAEND EDLESDHFGK LEPKLSIIRN LNDQVLFINQ
GNQPVFEDMP DSDCSDNAPQ TIFIIYMYKD SLTRGLAVTI SVQCKKMSTL SCENKIVSFK
EMNPPDNIDN EESDIIFFQR SVPGHDDKIQ FESSLYKGYF LACKKENDLF KLILKKQDDN
RDKSVMFTVQ NQN
