P01582 · IL1A_MOUSE
- ProteinInterleukin-1 alpha
- GeneIl1a
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids270 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameInterleukin-1 alpha
- Short namesIL-1 alpha
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionP01582
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
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.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Deletion mice show reduced nociceptive sensitivity compared to control mice in models of inflammatory and nerve injury-induced pain when associated with IL1B deletion.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 6 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for propeptide, glycosylation, modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Propeptide | PRO_0000015273 | 1-114 | ||||
Sequence: MAKVPDLFEDLKNCYSENEDYSSAIDHLSLNQKSFYDASYGSLHETCTDQFVSLRTSETSKMSNFTFKESRVTVSATSSNGKILKKRRLSFSETFTEDDLQSITHDLEETIQPR | ||||||
Glycosylation | 64 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Modified residue | 85 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 90 | Phosphoserine | ||||
Sequence: S | ||||||
Chain | PRO_0000015274 | 115-270 | Interleukin-1 alpha | |||
Sequence: SAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS | ||||||
Glycosylation | 139 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N | ||||||
Glycosylation | 143 | N-linked (GlcNAc...) asparagine | ||||
Sequence: N |
Post-translational modification
Acetylated within its nuclear localization sequence, which impacts subcellular localization.
Proteolytic processed by CAPN1 in a calcium-dependent manner. Cleavage from 31 kDa precursor to 18 kDa biologically active molecules.
Phosphorylated. Phosphorylation greatly enhances susceptibility to digestion and promotes the conversion of pre-IL1A alpha to the biologically active IL1A.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Monomer. Interacts with TMED10; the interaction mediates the translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and thereby secretion. Interacts with IL1R1. Interacts with S100A13; this interaction is the first step in the export of IL1A, followed by direct translocation of this complex across the plasma membrane.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 85-89 | Nuclear localization signal (NLS) | ||||
Sequence: KKRRL |
Domain
The similarity among the IL-1 precursors suggests that the amino ends of these proteins serve some as yet undefined function.
Sequence similarities
Belongs to the IL-1 family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length270
- Mass (Da)31,023
- Last updated1986-07-21 v1
- Checksum7F60AC4F330D5B11
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
X01450 EMBL· GenBank· DDBJ | CAA25682.1 EMBL· GenBank· DDBJ | mRNA | ||
AF010237 EMBL· GenBank· DDBJ | AAC28999.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003727 EMBL· GenBank· DDBJ | AAH03727.1 EMBL· GenBank· DDBJ | mRNA |