ID   IL1B_ONCMY              Reviewed;         260 AA.
AC   Q9YGD3;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Interleukin-1 beta;
DE   Flags: Precursor;
GN   Name=il1b;
OS   Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Oncorhynchus.
OX   NCBI_TaxID=8022;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Liver;
RX   PubMed=10092880; DOI=10.1046/j.1432-1327.1999.00121.x;
RA   Zou J., Cunningham C., Secombes C.J.;
RT   "The rainbow trout Oncorhynchus mykiss interleukin-1 beta gene has a
RT   different organization to mammals and undergoes incomplete splicing.";
RL   Eur. J. Biochem. 259:901-908(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Leukocyte;
RA   Zou J., Grabowski P., Cunningham C., Secombes C.;
RT   "Molecular cloning of rainbow trout Oncorhynchus mykiss interleukin-1-beta
RT   reveals no evidence of an ICE cut site.";
RL   Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15123302; DOI=10.1016/s1050-4648(03)00114-1;
RA   Wang T., Johnson N., Zou J., Bols N., Secombes C.J.;
RT   "Sequencing and expression of the second allele of the interleukin-1beta1
RT   gene in rainbow trout (Oncorhynchus mykiss): identification of a novel SINE
RT   in the third intron.";
RL   Fish Shellfish Immunol. 16:335-358(2004).
CC   -!- FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the
CC       major endogenous pyrogen, induces prostaglandin synthesis, neutrophil
CC       influx and activation, T-cell activation and cytokine production, B-
CC       cell activation and antibody production, and fibroblast proliferation
CC       and collagen production. Involved in transduction of inflammation
CC       downstream of pyroptosis: its mature form is specifically released in
CC       the extracellular milieu by passing through the gasdermin-D (GSDMD)
CC       pore. {ECO:0000250|UniProtKB:P01584}.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P01584}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
CC       {ECO:0000250|UniProtKB:P01584}. Secreted
CC       {ECO:0000250|UniProtKB:P01584}. Lysosome
CC       {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome
CC       {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic. In
CC       response to inflammasome-activating signals, such as ATP for NLRP3
CC       inflammasome or bacterial flagellin for NLRC4 inflammasome, 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:P01584}.
CC   -!- TISSUE SPECIFICITY: All three isoforms are expressed in gill, kidney,
CC       liver and spleen. Isoform 1 is also expressed in blood. None of the
CC       isoforms are expressed in brain. {ECO:0000269|PubMed:10092880}.
CC   -!- MISCELLANEOUS: IL1B production occurs in 2 steps, each being controlled
CC       by different stimuli. First, inflammatory signals, such as LPS,
CC       stimulate the synthesis and promote the accumulation of cytosolic
CC       stores of pro-IL1B (priming). Then additional signals are required for
CC       inflammasome assembly, leading to CASP1 activation, pro-IL1B processing
CC       and eventually secretion of the active cytokine. IL1B processing and
CC       secretion are temporarily associated. {ECO:0000250|UniProtKB:P01584}.
CC   -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
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DR   EMBL; AJ004821; CAA06157.1; -; Genomic_DNA.
DR   EMBL; AJ223954; CAA11684.1; -; mRNA.
DR   EMBL; AJ278242; CAB93352.1; -; Genomic_DNA.
DR   RefSeq; NP_001117819.1; NM_001124347.2.
DR   AlphaFoldDB; Q9YGD3; -.
DR   SMR; Q9YGD3; -.
DR   Ensembl; ENSOMYT00000011239; ENSOMYP00000010168; ENSOMYG00000005094.
DR   GeneID; 100136024; -.
DR   KEGG; omy:100136024; -.
DR   GeneTree; ENSGT00950000182943; -.
DR   OrthoDB; 1243742at2759; -.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR   GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR   GO; GO:0043400; P:cortisol secretion; IDA:AgBase.
DR   GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR   GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase.
DR   GO; GO:0002690; P:positive regulation of leukocyte chemotaxis; IDA:AgBase.
DR   GO; GO:0050766; P:positive regulation of phagocytosis; IDA:AgBase.
DR   GO; GO:0001934; P:positive regulation of protein phosphorylation; IDA:AgBase.
DR   GO; GO:0051924; P:regulation of calcium ion transport; IDA:AgBase.
DR   GO; GO:0042098; P:T cell proliferation; IMP:AgBase.
DR   InterPro; IPR003296; IL-1_beta.
DR   InterPro; IPR000975; IL-1_fam.
DR   InterPro; IPR008996; IL1/FGF.
DR   PANTHER; PTHR10078; PTHR10078; 1.
DR   PANTHER; PTHR10078:SF30; PTHR10078:SF30; 1.
DR   Pfam; PF00340; IL1; 1.
DR   PRINTS; PR00264; INTERLEUKIN1.
DR   SUPFAM; SSF50353; SSF50353; 1.
PE   2: Evidence at transcript level;
KW   Cytokine; Cytoplasm; Inflammatory response; Lysosome; Mitogen; Pyrogen;
KW   Secreted.
FT   PROPEP          1..?
FT                   /id="PRO_0000015323"
FT   CHAIN           ?..260
FT                   /note="Interleukin-1 beta"
FT                   /id="PRO_0000015324"
SQ   SEQUENCE   260 AA;  29127 MW;  0DC77991EA53E97F CRC64;
     MDFESNYSLI KNTSESAAWS SKLPQGLDLE VSHHPITMRH IANLIIAMER LKGGEGVTMG
     TEFKDKDLLN FLLESAVEEH IVLELESAPP ASRRAAGFSS TSQYECSVTD SENKCWVLMN
     EAMELHAMML QGGSSYHKVH LNLSSYVTPV PIETEARPVA LGIKGSNLYL SCSKSGGRPT
     LHLEEVADKD QLKSISQQSD MVRFLFYRRN TGVDISTLES ASFRNWFIST DMQQDYTKPV
     DMCQKAAPNR LTTFTIQRHN