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Il1r1

Domain

The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.

Function

Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the coreceptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex. Involved in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (By similarity).

Isoform 2

Unable to mediate canonical IL-1 signaling. Cooperates with IL1RAP isoform 3 to mediate IL1B-induced neuronal activity including IL1B-potentiated NMDA-induced calcium influx mediated by Akt kinase activation.

Post-translational modifications

A soluble form (sIL1R1) is probably produced by proteolytic cleavage at the cell surface (shedding).

Rapidly phosphorylated on Tyr-499 in response to IL-1, which creates a SH2 binding site for the PI 3-kinase regulatory subunit PIK3R1.

Sequence Similarities

Belongs to the interleukin-1 receptor family.

Tissue Specificity

Isoform 2 is expressed in various brain tissues.

Cellular localization

Alternative names

CD121a, Il-1r1, Il1ra, Il1r1, Interleukin-1 receptor type 1, IL-1R-1, IL-1RT-1, IL-1RT1, CD121 antigen-like family member A, Interleukin-1 receptor alpha, Interleukin-1 receptor type I, p80, IL-1R-alpha

swissprot:P13504 entrezGene:16177

Other research areas