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IL1B_LAMGL
ID   IL1B_LAMGL              Reviewed;         267 AA.
AC   Q865X8;
DT   16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=Interleukin-1 beta;
DE            Short=IL-1 beta;
DE   Flags: Precursor;
GN   Name=IL1B;
OS   Lama glama (Llama).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Tylopoda; Camelidae; Lama.
OX   NCBI_TaxID=9844;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Odbileg R., Lee S.-I., Yoshida R., Chang K.-S., Ohashi K., Sugimoto C.,
RA   Onuma M.;
RT   "Cloning and sequence analysis of cytokine cDNAs of llama and camel.";
RL   Submitted (APR-2003) 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; AB107644; BAC75381.1; -; mRNA.
DR   AlphaFoldDB; Q865X8; -.
DR   SMR; Q865X8; -.
DR   PRIDE; Q865X8; -.
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..114
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015303"
FT   CHAIN           115..267
FT                   /note="Interleukin-1 beta"
FT                   /id="PRO_0000015304"
FT   SITE            169
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
FT   SITE            177
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            188
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
FT   SITE            202
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
SQ   SEQUENCE   267 AA;  30521 MW;  FAB5FCD80092F0FC CRC64;
     MATVPEPTSE MMAYYSDNDN DLLFEADGPK QRKCCVQPPD LGSLGDEGIQ LQISHQLYNK
     SFRQVVSLIV AMEKLSKCTY SQYFQDDDLR NIFSLIFEEE PVTFETCADD FVCDAVVQSL
     YCKLQDKEQK SMVLASPYVL QALHLLAQDM SREVVFCMSF VQGDENNSKT PVVLGLKEKN
     LYLSCVMKGD KPTLQLEALD PKSYPRKNME KRFVFYKTEI KDRVEFESAL YPNWYISTST
     AEQRPVFLGQ SRGGQDITDF TMETLSP
 
 
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