P01582 · IL1A_MOUSE

  • Protein
    Interleukin-1 alpha
  • Gene
    Il1a
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

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).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcell surface
Cellular Componentcytosol
Cellular Componentextracellular space
Cellular Componentnucleus
Molecular Functioncopper ion binding
Molecular Functioncytokine activity
Molecular Functioninterleukin-1 receptor binding
Biological Processcellular response to heat
Biological Processcellular response to lipopolysaccharide
Biological Processconnective tissue replacement involved in inflammatory response wound healing
Biological Processcytokine-mediated signaling pathway
Biological Processectopic germ cell programmed cell death
Biological Processextrinsic apoptotic signaling pathway in absence of ligand
Biological Processfever generation
Biological Processheart development
Biological Processimmune response
Biological Processinflammatory response
Biological Processintracellular sodium ion homeostasis
Biological Processkeratinization
Biological Processnegative regulation of cell population proliferation
Biological Processnegative regulation of establishment of Sertoli cell barrier
Biological Processpositive regulation of angiogenesis
Biological Processpositive regulation of canonical NF-kappaB signal transduction
Biological Processpositive regulation of cell division
Biological Processpositive regulation of ERK1 and ERK2 cascade
Biological Processpositive regulation of gene expression
Biological Processpositive regulation of immature T cell proliferation in thymus
Biological Processpositive regulation of interleukin-2 production
Biological Processpositive regulation of interleukin-6 production
Biological Processpositive regulation of JNK cascade
Biological Processpositive regulation of mitotic nuclear division
Biological Processpositive regulation of neutrophil migration
Biological Processpositive regulation of prostaglandin secretion
Biological Processpositive regulation of protein secretion
Biological Processpositive regulation of steroid biosynthetic process
Biological Processpositive regulation of stress-activated MAPK cascade
Biological Processpositive regulation of transcription by RNA polymerase II
Biological Processpositive regulation of tumor necrosis factor production
Biological Processpositive regulation of vascular endothelial growth factor production
Biological Processregulation of actin cytoskeleton organization
Biological Processresponse to copper ion
Biological Processresponse to gamma radiation
Biological Processresponse to hypoxia
Biological Processresponse to L-ascorbic acid
Biological Processresponse to organonitrogen compound
Biological Processresponse to ozone
Biological Processspermatogenesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Interleukin-1 alpha
  • Short names
    IL-1 alpha

Gene names

    • Name
      Il1a

Organism names

  • Taxonomic identifier
  • Strains
    • BALB/cJ
    • FVB/N
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus

Accessions

  • Primary accession
    P01582

Proteomes

Organism-specific databases

Subcellular Location

Nucleus
Cytoplasm
Secreted
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

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.

Go to variant viewer

PTM/Processing

Features

Showing features for propeptide, glycosylation, modified residue, chain.

TypeIDPosition(s)Description
PropeptidePRO_00000152731-114
Glycosylation64N-linked (GlcNAc...) asparagine
Modified residue85N6-acetyllysine
Modified residue90Phosphoserine
ChainPRO_0000015274115-270Interleukin-1 alpha
Glycosylation139N-linked (GlcNAc...) asparagine
Glycosylation143N-linked (GlcNAc...) asparagine

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

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.

TypeIDPosition(s)Description
Region85-89Nuclear localization signal (NLS)

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 status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    270
  • Mass (Da)
    31,023
  • Last updated
    1986-07-21 v1
  • Checksum
    7F60AC4F330D5B11
MAKVPDLFEDLKNCYSENEDYSSAIDHLSLNQKSFYDASYGSLHETCTDQFVSLRTSETSKMSNFTFKESRVTVSATSSNGKILKKRRLSFSETFTEDDLQSITHDLEETIQPRSAPYTYQSDLRYKLMKLVRQKFVMNDSLNQTIYQDVDKHYLSTTWLNDLQQEVKFDMYAYSSGGDDSKYPVTLKISDSQLFVSAQGEDQPVLLKELPETPKLITGSETDLIFFWKSINSKNYFTSAAYPELFIATKEQSRVHLARGLPSMTDFQIS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Genome annotation databases

Similar Proteins

Disclaimer

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