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Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma)

 IL18_HUMAN              Reviewed;         193 AA.
Q14116; O75599; Q6FGY3; Q6WWJ7;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
30-AUG-2017, entry version 164.
RecName: Full=Interleukin-18;
Short=IL-18;
AltName: Full=Iboctadekin;
AltName: Full=Interferon gamma-inducing factor;
Short=IFN-gamma-inducing factor;
AltName: Full=Interleukin-1 gamma;
Short=IL-1 gamma;
Flags: Precursor;
Name=IL18; Synonyms=IGIF, IL1F4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
PubMed=8666798;
Ushio S., Namba M., Okura T., Hattori K., Nukada Y., Akita K.,
Tanabe F., Konishi K., Micallef M., Fujii M., Torigoe K., Tanimoto T.,
Fukuda S., Ikeda M., Okamura H., Kurimoto M.;
"Cloning of the cDNA for human IFN-gamma-inducing factor, expression
in Escherichia coli, and studies on the biologic activities of the
protein.";
J. Immunol. 156:4274-4279(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEOLYTIC PROCESSING, AND
ALTERNATIVE SPLICING.
PubMed=15326478; DOI=10.1038/sj.onc.1208036;
Gaggero A., De Ambrosis A., Mezzanzanica D., Piazza T., Rubartelli A.,
Figini M., Canevari S., Ferrini S.;
"A novel isoform of pro-interleukin-18 expressed in ovarian tumors is
resistant to caspase-1 and -4 processing.";
Oncogene 23:7552-7560(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Yong D., Guixin D., Lihua H., Haitao W.;
"Cloning and sequencing of the cDNA for precursor hIL-18.";
Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Liu J., Peng X., Yuan J., Qiang B.;
"Cloning of human interleukin 18 cDNA.";
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Urinary bladder;
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).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-193 (ISOFORM 1).
TISSUE=Peripheral blood;
Conti B., Kim S.J., Tinti C., Chun H.S., Joh T.H.;
Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
INDUCTION BY ENDOCANNABINOID ANANDAMIDE.
PubMed=23955712; DOI=10.1038/nm.3265;
Jourdan T., Godlewski G., Cinar R., Bertola A., Szanda G., Liu J.,
Tam J., Han T., Mukhopadhyay B., Skarulis M.C., Ju C., Aouadi M.,
Czech M.P., Kunos G.;
"Activation of the Nlrp3 inflammasome in infiltrating macrophages by
endocannabinoids mediates beta cell loss in type 2 diabetes.";
Nat. Med. 19:1132-1140(2013).
-!- FUNCTION: Augments natural killer cell activity in spleen cells
and stimulates interferon gamma production in T-helper type I
cells.
-!- INTERACTION:
Q13478:IL18R1; NbExp=2; IntAct=EBI-3910835, EBI-9817499;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14116-1; Sequence=Displayed;
Name=2; Synonyms=Delta3pro-IL-18;
IsoId=Q14116-2; Sequence=VSP_044934;
Note=Expressed in ovarian carcinoma but undetectable in normal
ovarian epithelial cells. Resistant to proteolytic activation by
caspase-1 and -4.;
-!- INDUCTION: In macrophages, release is increased by endocannabinoid
anandamide/AEA. {ECO:0000269|PubMed:23955712}.
-!- PTM: The pro-IL-18 precursor is processed by CASP1 or CASP4 to
yield the active form. {ECO:0000269|PubMed:15326478}.
-!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-1 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_1";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
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EMBL; D49950; BAA08706.1; -; mRNA.
EMBL; AY266351; AAP92112.1; -; mRNA.
EMBL; AF077611; AAC27787.1; -; mRNA.
EMBL; AY044641; AAK95950.1; -; mRNA.
EMBL; CR541973; CAG46771.1; -; mRNA.
EMBL; CR542001; CAG46798.1; -; mRNA.
EMBL; AP002007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP002884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471065; EAW67184.1; -; Genomic_DNA.
EMBL; BC007007; AAH07007.1; -; mRNA.
EMBL; BC007461; AAH07461.1; -; mRNA.
EMBL; U90434; AAB50010.1; -; mRNA.
CCDS; CCDS44731.1; -. [Q14116-1]
CCDS; CCDS58180.1; -. [Q14116-2]
RefSeq; NP_001230140.1; NM_001243211.1. [Q14116-2]
RefSeq; NP_001553.1; NM_001562.3. [Q14116-1]
RefSeq; XP_011541107.1; XM_011542805.1. [Q14116-2]
RefSeq; XP_011541108.1; XM_011542806.2. [Q14116-1]
UniGene; Hs.83077; -.
PDB; 1J0S; NMR; -; A=37-193.
PDB; 2VXT; X-ray; 1.49 A; I=37-193.
PDB; 3F62; X-ray; 2.00 A; B=37-193.
PDB; 3WO2; X-ray; 2.33 A; A/B/C/D=37-193.
PDB; 3WO3; X-ray; 3.10 A; A/C/E/G/I/K=37-193.
PDB; 3WO4; X-ray; 3.10 A; A=37-193.
PDB; 4EEE; X-ray; 2.71 A; B/D=37-193.
PDB; 4EKX; X-ray; 1.75 A; B/D=37-193.
PDB; 4HJJ; X-ray; 2.10 A; A=37-192.
PDB; 4R6U; X-ray; 2.80 A; B/D=37-193.
PDB; 4XFS; X-ray; 1.91 A; A/B=37-193.
PDB; 4XFT; X-ray; 2.00 A; A/B=37-193.
PDB; 4XFU; X-ray; 2.85 A; A/B=37-193.
PDBsum; 1J0S; -.
PDBsum; 2VXT; -.
PDBsum; 3F62; -.
PDBsum; 3WO2; -.
PDBsum; 3WO3; -.
PDBsum; 3WO4; -.
PDBsum; 4EEE; -.
PDBsum; 4EKX; -.
PDBsum; 4HJJ; -.
PDBsum; 4R6U; -.
PDBsum; 4XFS; -.
PDBsum; 4XFT; -.
PDBsum; 4XFU; -.
ProteinModelPortal; Q14116; -.
SMR; Q14116; -.
BioGrid; 109819; 12.
DIP; DIP-3785N; -.
IntAct; Q14116; 3.
STRING; 9606.ENSP00000280357; -.
iPTMnet; Q14116; -.
PhosphoSitePlus; Q14116; -.
BioMuta; IL18; -.
DMDM; 3219817; -.
OGP; Q14116; -.
EPD; Q14116; -.
MaxQB; Q14116; -.
PaxDb; Q14116; -.
PeptideAtlas; Q14116; -.
PRIDE; Q14116; -.
DNASU; 3606; -.
Ensembl; ENST00000280357; ENSP00000280357; ENSG00000150782. [Q14116-1]
Ensembl; ENST00000524595; ENSP00000434561; ENSG00000150782. [Q14116-2]
Ensembl; ENST00000528832; ENSP00000434161; ENSG00000150782. [Q14116-1]
GeneID; 3606; -.
KEGG; hsa:3606; -.
UCSC; uc001pnb.2; human. [Q14116-1]
CTD; 3606; -.
DisGeNET; 3606; -.
GeneCards; IL18; -.
HGNC; HGNC:5986; IL18.
HPA; CAB007772; -.
HPA; HPA003980; -.
MIM; 600953; gene.
neXtProt; NX_Q14116; -.
OpenTargets; ENSG00000150782; -.
PharmGKB; PA29802; -.
eggNOG; ENOG410J3U9; Eukaryota.
eggNOG; ENOG410ZGS8; LUCA.
GeneTree; ENSGT00390000001053; -.
HOGENOM; HOG000048723; -.
HOVERGEN; HBG000388; -.
InParanoid; Q14116; -.
KO; K05482; -.
OMA; VPGHDDK; -.
OrthoDB; EOG091G0NGF; -.
PhylomeDB; Q14116; -.
TreeFam; TF336297; -.
Reactome; R-HSA-448706; Interleukin-1 processing.
Reactome; R-HSA-449836; Other interleukin signaling.
Reactome; R-HSA-6783783; Interleukin-10 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SIGNOR; Q14116; -.
EvolutionaryTrace; Q14116; -.
GeneWiki; Interleukin_18; -.
GenomeRNAi; 3606; -.
PMAP-CutDB; Q14116; -.
PRO; PR:Q14116; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000150782; -.
CleanEx; HS_IL18; -.
ExpressionAtlas; Q14116; baseline and differential.
Genevisible; Q14116; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005125; F:cytokine activity; ISS:BHF-UCL.
GO; GO:0032148; P:activation of protein kinase B activity; IDA:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IDA:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:UniProtKB.
GO; GO:0042033; P:chemokine biosynthetic process; TAS:UniProtKB.
GO; GO:0042632; P:cholesterol homeostasis; ISS:BHF-UCL.
GO; GO:0042253; P:granulocyte macrophage colony-stimulating factor biosynthetic process; TAS:UniProtKB.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0006954; P:inflammatory response; IDA:UniProtKB.
GO; GO:0042095; P:interferon-gamma biosynthetic process; TAS:UniProtKB.
GO; GO:0042231; P:interleukin-13 biosynthetic process; TAS:UniProtKB.
GO; GO:0035655; P:interleukin-18-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0042094; P:interleukin-2 biosynthetic process; TAS:UniProtKB.
GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; IMP:UniProtKB.
GO; GO:0030101; P:natural killer cell activation; IEA:Ensembl.
GO; GO:0045662; P:negative regulation of myoblast differentiation; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:UniProtKB.
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:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISS:BHF-UCL.
GO; GO:0032819; P:positive regulation of natural killer cell proliferation; IDA:BHF-UCL.
GO; GO:0042346; P:positive regulation of NF-kappaB import into nucleus; IEA:Ensembl.
GO; GO:0051142; P:positive regulation of NK T cell proliferation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:BHF-UCL.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:BHF-UCL.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; 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; IDA:BHF-UCL.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:CACAO.
GO; GO:0030155; P:regulation of cell adhesion; IDA:UniProtKB.
GO; GO:0030431; P:sleep; ISS:UniProtKB.
GO; GO:0042088; P:T-helper 1 type immune response; IDA:UniProtKB.
GO; GO:0070328; P:triglyceride homeostasis; ISS:BHF-UCL.
GO; GO:0042092; P:type 2 immune response; TAS:UniProtKB.
InterPro; IPR015529; IL-18.
InterPro; IPR000975; IL-1_fam.
InterPro; IPR008996; IL1/FGF.
PANTHER; PTHR10078:SF66; PTHR10078:SF66; 1.
Pfam; PF00340; IL1; 1.
PIRSF; PIRSF015162; Interleukin_18; 1.
PRINTS; PR01933; INTRLEUKIN18.
SUPFAM; SSF50353; SSF50353; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytokine;
Reference proteome; Secreted.
PROPEP 1 36 {ECO:0000250}.
/FTId=PRO_0000015343.
CHAIN 37 193 Interleukin-18.
/FTId=PRO_0000015344.
VAR_SEQ 27 30 Missing (in isoform 2).
{ECO:0000303|PubMed:15326478}.
/FTId=VSP_044934.
CONFLICT 66 66 F -> L (in Ref. 3; AAC27787).
{ECO:0000305}.
CONFLICT 86 86 S -> R (in Ref. 3; AAC27787).
{ECO:0000305}.
CONFLICT 191 191 N -> S (in Ref. 3; AAC27787).
{ECO:0000305}.
STRAND 42 49 {ECO:0000244|PDB:2VXT}.
STRAND 55 58 {ECO:0000244|PDB:2VXT}.
STRAND 64 67 {ECO:0000244|PDB:2VXT}.
HELIX 71 76 {ECO:0000244|PDB:2VXT}.
TURN 77 81 {ECO:0000244|PDB:2VXT}.
STRAND 83 91 {ECO:0000244|PDB:2VXT}.
TURN 92 94 {ECO:0000244|PDB:2VXT}.
STRAND 95 111 {ECO:0000244|PDB:2VXT}.
HELIX 113 115 {ECO:0000244|PDB:2VXT}.
STRAND 118 121 {ECO:0000244|PDB:2VXT}.
STRAND 126 131 {ECO:0000244|PDB:2VXT}.
STRAND 137 142 {ECO:0000244|PDB:2VXT}.
STRAND 145 156 {ECO:0000244|PDB:2VXT}.
STRAND 159 166 {ECO:0000244|PDB:2VXT}.
STRAND 169 176 {ECO:0000244|PDB:2VXT}.
TURN 178 180 {ECO:0000244|PDB:4HJJ}.
HELIX 183 185 {ECO:0000244|PDB:2VXT}.
STRAND 187 191 {ECO:0000244|PDB:2VXT}.
SEQUENCE 193 AA; 22326 MW; 323C62C203788D55 CRC64;
MAAEPVEDNC INFVAMKFID NTLYFIAEDD ENLESDYFGK LESKLSVIRN LNDQVLFIDQ
GNRPLFEDMT DSDCRDNAPR TIFIISMYKD SQPRGMAVTI SVKCEKISTL SCENKIISFK
EMNPPDNIKD TKSDIIFFQR SVPGHDNKMQ FESSSYEGYF LACEKERDLF KLILKKEDEL
GDRSIMFTVQ NED


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