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IL1B_PUSHI
ID   IL1B_PUSHI              Reviewed;         270 AA.
AC   Q2HZH0;
DT   17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 53.
DE   RecName: Full=Interleukin-1 beta;
DE            Short=IL-1 beta;
DE   Flags: Precursor;
GN   Name=IL1B;
OS   Pusa hispida (Ringed seal) (Phoca hispida).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Phocidae; Pusa.
OX   NCBI_TaxID=9718;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bozza M., Atkinson S.;
RT   "Cloning and sequencing of interleukin-1 beta (IL-1b) from cDNA libraries
RT   of Alaskan pinniped species: Steller sea lion (Eumetopias jubatus) harbor
RT   seal (Phoca vitulina richardsi) and ringed seal (Phoca hispida).";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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; DQ358051; ABC87314.1; -; mRNA.
DR   AlphaFoldDB; Q2HZH0; -.
DR   SMR; Q2HZH0; -.
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: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: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: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   Secreted.
FT   PROPEP          1..118
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000253758"
FT   CHAIN           119..270
FT                   /note="Interleukin-1 beta"
FT                   /id="PRO_0000253759"
FT   SITE            173
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            183
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
FT   SITE            192
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
SQ   SEQUENCE   270 AA;  31053 MW;  36972890C6A2FB2E CRC64;
     MATVPEPTSE MMSYYYSDNE NDLFFEADGP RKMKCCFQDL NNSSLKDEGI QLHISHQLQN
     KSLRHFVSVV VALEKLKKIS LPCSQPLQDD DLKNVFCCIF EEEPIVCEVY DDDAFVCDAP
     LQSLDCKFRD KNQKSLVLYN SYELRALHLN GSSVNQQAVF RMSFLQGDEN SNKIPVALCI
     KEKNLYLSCV MKDGKPTLQL EMLDPRVYPK KKMEKRFVFN KTEVKKILEF ESSQFPNWYI
     STSKAEAMPV FLGNTKGGQD ITDFTMEFSS
 
 
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