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IL1B_HORSE
ID   IL1B_HORSE              Reviewed;         268 AA.
AC   Q28386; O18995; O77744;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Interleukin-1 beta;
DE            Short=IL-1 beta;
DE   Flags: Precursor;
GN   Name=IL1B;
OS   Equus caballus (Horse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Perissodactyla; Equidae; Equus.
OX   NCBI_TaxID=9796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX   PubMed=8578682; DOI=10.1016/0165-2427(95)05441-8;
RA   Kato H., Ohashi T., Nakamura N., Nishimura Y., Watari T., Goitsuka R.,
RA   Tsujimoto H., Hasegawa A.;
RT   "Molecular cloning of equine interleukin-1 alpha and -beta cDNAs.";
RL   Vet. Immunol. Immunopathol. 48:221-231(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
RX   PubMed=9622738;
RA   Howard R.D., McIlwraith C.W., Trotter G.W., Nyborg J.K.;
RT   "Cloning of equine interleukin-1 alpha and equine interleukin-1 beta and
RT   determination of their full-length cDNA sequences.";
RL   Am. J. Vet. Res. 59:704-711(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
RX   PubMed=8921838; DOI=10.1016/0378-1119(96)00262-4;
RA   Kato H., Youn H.Y., Ohashi T., Watari T., Goitsuka R., Tsujimoto H.,
RA   Hasegawa A.;
RT   "Identification of an alternatively spliced transcript of equine
RT   interleukin-1 beta.";
RL   Gene 177:11-16(1996).
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   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=Long;
CC         IsoId=Q28386-1; Sequence=Displayed;
CC       Name=Short;
CC         IsoId=Q28386-2; Sequence=VSP_002648;
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; D42147; BAA07718.1; -; mRNA.
DR   EMBL; U92481; AAC39256.1; -; mRNA.
DR   EMBL; D42165; BAA22528.1; -; mRNA.
DR   PIR; JC5646; JC5646.
DR   RefSeq; NP_001075995.1; NM_001082526.1.
DR   RefSeq; NP_001304190.1; NM_001317261.1. [Q28386-1]
DR   AlphaFoldDB; Q28386; -.
DR   SMR; Q28386; -.
DR   STRING; 9796.ENSECAP00000053627; -.
DR   PaxDb; Q28386; -.
DR   GeneID; 100034237; -.
DR   GeneID; 100052414; -.
DR   KEGG; ecb:100034237; -.
DR   CTD; 3553; -.
DR   InParanoid; Q28386; -.
DR   OrthoDB; 1243742at2759; -.
DR   Proteomes; UP000002281; 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   Alternative splicing; Cytokine; Cytoplasm; Inflammatory response; Lysosome;
KW   Mitogen; Pyrogen; Reference proteome; Secreted.
FT   PROPEP          1..115
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015299"
FT   CHAIN           116..268
FT                   /note="Interleukin-1 beta"
FT                   /id="PRO_0000015300"
FT   SITE            170
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            180
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
FT   SITE            189
FT                   /note="Important for interaction with integrin"
FT                   /evidence="ECO:0000250|UniProtKB:P01584"
FT   VAR_SEQ         101..154
FT                   /note="Missing (in isoform Short)"
FT                   /evidence="ECO:0000303|PubMed:8921838"
FT                   /id="VSP_002648"
FT   CONFLICT        45
FT                   /note="D -> N (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        55
FT                   /note="H -> Q (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        64..65
FT                   /note="AM -> VV (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        71
FT                   /note="V -> M (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        110..111
FT                   /note="EG -> DD (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        118
FT                   /note="M -> V (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        245
FT                   /note="S -> K (in Ref. 2; AAC39256)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   268 AA;  30268 MW;  336F27792A1542EA CRC64;
     MAAVPDTSDM MTYCSGNEND LFFEEDGPKQ MKGSFQDLDL SSMGDGGIQL QFSHHLYNKT
     FKHAMSIIVA VEKLKKIPVP CSQAFQDDDL RSLFSVIFEE EPIICDNWDE GYVCDAAMHS
     VNCRLRDIYH KSLVLSGACE LQAVHLNGEN TNQQVVFCMS FVQGEEETDK IPVALGLKEK
     NLYLSCGMKD GKPTLQLETV DPNTYPKRKM EKRFVFNKME IKGNVEFESA MYPNWYISTS
     QAEKSPVFLG NTRGGRDITD FIMEITSA
 
 
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