IL1B_DELLE
ID IL1B_DELLE Reviewed; 266 AA.
AC Q8WNR2;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Interleukin-1 beta;
DE Short=IL-1 beta;
DE Flags: Precursor;
GN Name=IL1B;
OS Delphinapterus leucas (Beluga whale).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC Monodontidae; Delphinapterus.
OX NCBI_TaxID=9749;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11768130;
RA Denis F., Archambault D.;
RT "Molecular cloning and characterization of beluga whale (Delphinapterus
RT leucas) interleukin-1beta and tumor necrosis factor-alpha.";
RL Can. J. Vet. Res. 65:233-240(2001).
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. Promotes Th17 differentiation of T-cells.
CC Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-
CC helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF
CC production synergistically with TNF and IL6. Involved in transduction
CC of inflammation downstream of pyroptosis: its mature form is
CC specifically released in the extracellular milieu by passing through
CC the gasdermin-D (GSDMD) pore. {ECO:0000250|UniProtKB:P01584}.
CC -!- SUBUNIT: Monomer. In its precursor form, weakly interacts with full-
CC length MEFV; the mature cytokine does not interact at all. Interacts
CC with integrins ITGAV:ITGBV and ITGA5:ITGB1; integrin-binding is
CC required for IL1B signaling. Interacts with cargo receptor TMED10; the
CC interaction is direct and is required for the secretion of IL1B mature
CC form. Interacts with HSP90AB1; the interaction facilitates cargo
CC translocation into the ERGIC. Interacts with HSP90B1; the interaction
CC facilitates cargo translocation into the ERGIC.
CC {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 -!- 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}.
CC -!- SIMILARITY: Belongs to the IL-1 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF320322; AAL56945.1; -; mRNA.
DR AlphaFoldDB; Q8WNR2; -.
DR SMR; Q8WNR2; -.
DR STRING; 9749.Q8WNR2; -.
DR Ensembl; ENSDLET00000007436; ENSDLEP00000006711; ENSDLEG00000005000.
DR OrthoDB; 1243742at2759; -.
DR Proteomes; UP000248483; Unplaced.
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:0019904; F:protein domain specific binding; IEA:Ensembl.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEA:Ensembl.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR GO; GO:0030213; P:hyaluronan biosynthetic process; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0070498; P:interleukin-1-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0031663; P:lipopolysaccharide-mediated signaling pathway; IEA:Ensembl.
DR GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
DR GO; GO:0070487; P:monocyte aggregation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:2001240; P:negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
DR GO; GO:1903597; P:negative regulation of gap junction assembly; IEA:Ensembl.
DR GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
DR GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
DR GO; GO:0060559; P:positive regulation of calcidiol 1-monooxygenase activity; IEA:Ensembl.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0030335; P:positive regulation of cell migration; IEA:Ensembl.
DR GO; GO:0045917; P:positive regulation of complement activation; IEA:Ensembl.
DR GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IEA:Ensembl.
DR GO; GO:0060252; P:positive regulation of glial cell proliferation; IEA:Ensembl.
DR GO; GO:0032725; P:positive regulation of granulocyte macrophage colony-stimulating factor production; IEA:Ensembl.
DR GO; GO:0034116; P:positive regulation of heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IEA:Ensembl.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IEA:Ensembl.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IEA:Ensembl.
DR GO; GO:0032757; P:positive regulation of interleukin-8 production; IEA:Ensembl.
DR GO; GO:0043406; P:positive regulation of MAP kinase activity; IEA:Ensembl.
DR GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
DR GO; GO:0071639; P:positive regulation of monocyte chemotactic protein-1 production; IEA:Ensembl.
DR GO; GO:0035505; P:positive regulation of myosin light chain kinase activity; IEA:Ensembl.
DR GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
DR GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IEA:Ensembl.
DR GO; GO:0031394; P:positive regulation of prostaglandin biosynthetic process; IEA:Ensembl.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IEA:Ensembl.
DR GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IEA:Ensembl.
DR GO; GO:0043491; P:protein kinase B signaling; IEA:Ensembl.
DR GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
DR GO; GO:1903140; P:regulation of establishment of endothelial barrier; IEA:Ensembl.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
DR GO; GO:0050796; P:regulation of insulin secretion; IEA:Ensembl.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0030730; P:sequestering of triglyceride; IEA:Ensembl.
DR GO; GO:0010573; P:vascular endothelial growth factor production; ISS:UniProtKB.
DR InterPro; IPR003296; IL-1_beta.
DR InterPro; IPR020877; IL-1_CS.
DR InterPro; IPR000975; IL-1_fam.
DR InterPro; IPR003502; IL-1_propep.
DR InterPro; IPR008996; IL1/FGF.
DR PANTHER; PTHR10078; PTHR10078; 1.
DR PANTHER; PTHR10078:SF30; PTHR10078:SF30; 1.
DR Pfam; PF00340; IL1; 1.
DR Pfam; PF02394; IL1_propep; 1.
DR PRINTS; PR00264; INTERLEUKIN1.
DR SUPFAM; SSF50353; SSF50353; 1.
DR PROSITE; PS00253; INTERLEUKIN_1; 1.
PE 2: Evidence at transcript level;
KW Cytokine; Cytoplasm; Inflammatory response; Lysosome; Mitogen; Pyrogen;
KW Reference proteome; Secreted.
FT PROPEP 1..113
FT /evidence="ECO:0000250"
FT /id="PRO_0000045163"
FT CHAIN 114..266
FT /note="Interleukin-1 beta"
FT /id="PRO_0000045164"
FT SITE 168
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 176
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 178
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 187
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 201
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
SQ SEQUENCE 266 AA; 30219 MW; 03025F37F54A362A CRC64;
MATVPEPTNE VMAYYSDEND LLFEADGPKQ MKCCVQPLDL NSMGDGSIHL QISHQLYNKS
LRRVVSVIVA VEKLQKIPCS QTFQDDGLRS IFSLIFEEEP VIFETYDDDL LCDAGVQSLT
CKLQDRDQKS LVLASPCVLK ALHLLARDVN REVVFCMSFV QGDESNDKIP VALGLKEKNL
YLSCVMKGDR PTLQLEEVDP KTYPKWKMEK RFVFNKTEIK NSVEFESALY PNWYISTSQA
EEKPIFLGRS KGGHDITDFT MEIISP
