IL1B_MACMU
ID IL1B_MACMU Reviewed; 269 AA.
AC P48090;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Interleukin-1 beta;
DE Short=IL-1 beta;
DE Flags: Precursor;
GN Name=IL1B;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Blood;
RX PubMed=7561102;
RA Villinger F.J., Brar S.S., Mayne A.E., Chikkala N., Ansari A.A.;
RT "Comparative sequence analysis of cytokine genes from human and nonhuman
RT primates.";
RL J. Immunol. 155:3946-3954(1995).
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}.
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DR EMBL; U19845; AAA86709.1; -; mRNA.
DR RefSeq; NP_001036221.1; NM_001042756.1.
DR AlphaFoldDB; P48090; -.
DR SMR; P48090; -.
DR STRING; 9544.ENSMMUP00000026007; -.
DR GeneID; 704701; -.
DR KEGG; mcc:704701; -.
DR CTD; 3553; -.
DR eggNOG; ENOG502S3E9; Eukaryota.
DR InParanoid; P48090; -.
DR OrthoDB; 1243742at2759; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0005178; F:integrin binding; ISS:UniProtKB.
DR GO; GO:0005149; F:interleukin-1 receptor binding; IEA:InterPro.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0001660; P:fever generation; IEA:UniProtKB-KW.
DR GO; GO:0006955; P:immune response; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR GO; GO:0051781; P:positive regulation of cell division; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IBA:GO_Central.
DR GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IBA:GO_Central.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; ISS:UniProtKB.
DR GO; GO:2000556; P:positive regulation of T-helper 1 cell cytokine production; ISS:UniProtKB.
DR GO; GO:0050999; P:regulation of nitric-oxide synthase activity; IBA:GO_Central.
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..116
FT /evidence="ECO:0000250"
FT /id="PRO_0000015307"
FT CHAIN 117..269
FT /note="Interleukin-1 beta"
FT /id="PRO_0000015308"
FT SITE 171
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 179
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 181
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 190
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
FT SITE 204
FT /note="Important for interaction with integrin"
FT /evidence="ECO:0000250|UniProtKB:P01584"
SQ SEQUENCE 269 AA; 30481 MW; A7CD59EBAC120EC7 CRC64;
MAEVPELASE MMAYYSGNED DLFFDVDGPK QMKCSFQDLD LCPLGGGIQL QISHEHYNEG
FRQAVSVVVA MEKLRKMLVP CPQIFQDNDL STLIPFIFEE EPVFLDTRNN DACVHDAPVR
SLHCTLRDAQ LKSLVMSGPY ELKALHLQGQ DLEQQVVFSM SFVQGEESND KIPVALGLKA
KNLYLSCVLK DDKPTLQLES VDPKNYPKKK MEKRFVFNKI EINNKLEFES AQFPNWYIST
SQAENMPVFL GGTRGGQDIT DFTMQFVSS
