IL1B_PIG
ID IL1B_PIG Reviewed; 267 AA.
AC P26889;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1992, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Interleukin-1 beta;
DE Short=IL-1 beta;
DE Flags: Precursor;
GN Name=IL1B;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8325511; DOI=10.1016/0378-1119(93)90281-7;
RA Huether M.J., Lin G., Smith D.M., Murtaugh M.P., Molitor T.W.;
RT "Cloning, sequencing and regulation of an mRNA encoding porcine
RT interleukin-1 beta.";
RL Gene 129:285-289(1993).
RN [2]
RP INTERACTION WITH ASFV L83L.
RX PubMed=29605728; DOI=10.1016/j.virusres.2018.03.017;
RA Borca M.V., O'Donnell V., Holinka L.G., Ramirez-Medina E., Clark B.A.,
RA Vuono E.A., Berggren K., Alfano M., Carey L.B., Richt J.A., Risatti G.R.,
RA Gladue D.P.;
RT "The L83L ORF of African swine fever virus strain Georgia encodes for a
RT non-essential gene that interacts with the host protein IL-1beta.";
RL Virus Res. 249:116-123(2018).
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: (Microbial infection) Interacts with African swine fever virus
CC (ASFV) protein L83L. {ECO:0000269|PubMed:29605728}.
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; M86725; AAA02584.1; -; mRNA.
DR PIR; JN0724; JN0724.
DR RefSeq; NP_999220.1; NM_214055.1.
DR AlphaFoldDB; P26889; -.
DR SMR; P26889; -.
DR PaxDb; P26889; -.
DR PRIDE; P26889; -.
DR Ensembl; ENSSSCT00000062058; ENSSSCP00000044922; ENSSSCG00000039214.
DR Ensembl; ENSSSCT00060081761; ENSSSCP00060035415; ENSSSCG00060059921.
DR Ensembl; ENSSSCT00070040964; ENSSSCP00070034382; ENSSSCG00070020471.
DR Ensembl; ENSSSCT00070041049; ENSSSCP00070034458; ENSSSCG00070020471.
DR GeneID; 397122; -.
DR KEGG; ssc:397122; -.
DR CTD; 3553; -.
DR eggNOG; ENOG502S3E9; Eukaryota.
DR GeneTree; ENSGT00950000182943; -.
DR HOGENOM; CLU_083639_0_0_1; -.
DR InParanoid; P26889; -.
DR OMA; QHYSKGF; -.
DR OrthoDB; 1243742at2759; -.
DR TreeFam; TF300203; -.
DR Proteomes; UP000008227; Chromosome 3.
DR Proteomes; UP000314985; Chromosome 3.
DR Bgee; ENSSSCG00000039214; Expressed in blood and 19 other tissues.
DR Genevisible; P26889; SS.
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:2000866; P:positive regulation of estradiol secretion; IDA:CACAO.
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 1: Evidence at protein level;
KW Cytokine; Cytoplasm; Host-virus interaction; Inflammatory response;
KW Lysosome; Mitogen; Pyrogen; Reference proteome; Secreted.
FT PROPEP 1..114
FT /evidence="ECO:0000250"
FT /id="PRO_0000015313"
FT CHAIN 115..267
FT /note="Interleukin-1 beta"
FT /id="PRO_0000015314"
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; 30404 MW; 7F6B92B784D5086F CRC64;
MAIVPEPAKE VMANYGDNNN DLLFEADGPK EMKCCTQNLD LGSLRNGSIQ LQISHQLWNK
SIRQMVSVIV AVEKPMKNPS SQAFCDDDQK SIFSFIFEEE PIILETCNDD FVCDANVQSM
ECKLQDKDHK SLVLAGPHML KALHLLTGDL KREVVFCMSF VQGDDSNNKI PVTLGIKGKN
LYLSCVMKDN TPTLQLEDID PKRYPKRDME KRFVFYKTEI KNRVEFESAL YPNWYISTSQ
AEQKPVFLGN SKGRQDITDF TMEVLSP
