Q63264
uniprot
Q63264
canonical
amino_acid_sequence
MATVPELNCEIAAFDSEENDLFFEADRPQKIKDCFQALDLGCPDESIQLQISQQHLDKSFRKAVSLIVAVEKLWQLPMSCPWSFQDEDPSTFFSFIFEEEPVLCDSWDDDDLLVCDVPIRQLHCRLRDEQQKCLVLSDPCELKALHLNGQNISQQVVFSMSFVQGETSNDKIPVALGLKGLNLYLSCVMKDGTPTLQLESVDPKQYPKKKMEKRFVFNKIEVKTKVEFESAQFPNWYISTSQAEHRPVFLGNSNGRDIVDFTMEPVSS
uniprot
proteins
function
FUNCTION: Potent pro-inflammatory cytokine. Initially discovered as the major endogenous pyrogen, induces prostaglandin synthesis, neutrophil influx and activation, T-cell activation and cytokine production, B-cell activation and antibody production, and fibroblast proliferation and collagen production. Promotes Th17 differentiation of T-cells. Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells. Plays a role in angiogenesis by inducing VEGF production synergistically with TNF and IL6. Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. {ECO:0000250|UniProtKB:P01584}.
uniprot
proteins
mass_dalton
30644
uniprot
proteins
post_translational_modification
PTM: Activation of the IL1B precursor involves a CASP1-catalyzed proteolytic cleavage. Processing and secretion are temporarily associated. {ECO:0000250|UniProtKB:P01584}.
uniprot
proteins
protein_family
IL-1 family
uniprot
proteins
pubmed
23955712
uniprot
proteins
sequence_length
268
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P01584}. Secreted {ECO:0000250|UniProtKB:P01584}. Lysosome {ECO:0000250|UniProtKB:P01584}. Secreted, extracellular exosome {ECO:0000250|UniProtKB:P10749}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000250|UniProtKB:P01584}.
uniprot
proteins