Il1a
entrez
16175
canonical
uniprot
P01582
canonical
ensembl
ENSMUSG00000027399
resolver
ensp
ENSMUSP00000028882
resolver
enst
ENSMUST00000028882
resolver
genesymbol
Il1a
resolver
uniprot
Q3U0Y6
resolver
uniprot_entry
IL1A_MOUSE
resolver
uniprot_entry
Q3U0Y6_MOUSE
resolver
amino_acid_sequence
MAKVPDLFEDLKNCYSENEDYSSAIDHLSLNQKSFYDASYGSLHETCTDQFVSLRTSETSKMSNFTFKESRVTVSATSSNGKILKKRRLSFSETFTEDDLQSITHDLEETIQPRSAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS
uniprot
proteins
function
FUNCTION: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems (PubMed:16256210). After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 receptor complex. Signaling involves the recruitment of adapter molecules such as MYD88, IRAK1 or IRAK4. In turn, mediates the activation of NF-kappa-B and the three MAPK pathways p38, p42/p44 and JNK pathways (PubMed:1386364). Within the cell, acts as an alarmin and cell death results in its liberation in the extracellular space after disruption of the cell membrane to induce inflammation and alert the host to injury or damage. In addition to its role as a danger signal, which occurs when the cytokine is passively released by cell necrosis, directly senses DNA damage and acts as a signal for genotoxic stress without loss of cell integrity (By similarity). {ECO:0000250|UniProtKB:P01583, ECO:0000269|PubMed:1386364, ECO:0000269|PubMed:16256210}.
uniprot
proteins
mass_dalton
31023
uniprot
proteins
post_translational_modification
PTM: Acetylated within its nuclear localization sequence, which impacts subcellular localization. {ECO:0000250|UniProtKB:P01583}.; PTM: Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules. {ECO:0000250|UniProtKB:P01583}.; PTM: Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A. {ECO:0000250|UniProtKB:P01583}.
uniprot
proteins
protein_family
IL-1 family
uniprot
proteins
pubmed
1386364
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16256210
uniprot
proteins
pubmed
3126184
uniprot
proteins
pubmed
6209582
uniprot
proteins
sequence_length
270
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P01583}. Cytoplasm {ECO:0000250|UniProtKB:P01583}. Secreted {ECO:0000250|UniProtKB:P01583}. Note=The lack of a specific hydrophobic segment in the precursor sequence suggests that IL-1 is released by damaged cells or is secreted by a mechanism differing from that used for other secretory proteins. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion. Recruited to DNA damage sites and secreted after genotoxic stress. {ECO:0000250|UniProtKB:P01583}.
uniprot
proteins