描述：
Mouse interleukin-36 receptor antagonist (IL-36Ra; previously IL-1F5; also named FIL-1δ
[delta], IL-1HY1, IL-1H3, and IL-1L1) is a member of the IL-1 family of proteins. IL-1 family
members include IL-1β, IL-1α, IL-1ra, IL-18 and IL-1F5 through F10. All family members show
a 12 β-strand, β-trefoil configuration, and are believed to have arisen from a common
ancestral gene that underwent multiple duplications. The mouse IL-36Ra/IL-1F5 gene maps
to a region on mouse chromosome 2 that contains all other IL1 family members (except IL-18),
supporting an evolutionary relationship with the IL-1 family. It is particularly close to the gene
for IL-1ra and is likely a relatively recent duplication of that gene. IL-36Ra/IL-1F5 is synthesized
as a 156 amino acid (aa) protein that contains no signal sequence, no prosegment and no
potential Nlinked glycosylation site(s). Nevertheless, it appears to be secreted as a 17 kDa
monomer. In humans, there is an alternate start site that potentially gives rise to an alternate
splice form. This translated product has a premature stop codon, resulting in a truncated 16 aa
peptide. Mouse to human, full length IL-36Ra/IL-1F5 has 90% aa identity. Within the family,
IL-36Ra/IL-1F5 is 48%, 30%, 35%, 35%, 35%, 37% and 43% aa identical to IL1ra, IL1β, IL36α/
IL-1F6, IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9 and IL-1F10, respectively. Cells reported to
express IL-36Ra/IL-1F5 include monocytes, B cells, dendritic cells/Langerhans cells,
keratinocytes, and gastric fundus Parietal and Chief cells. The receptor for IL-36Ra/IL-1F5 has
not been positively identified. Indirect evidence suggests it is IL-1 Rrp2 and/or IL-1 RAcP. In
either case, activity association with receptor binding is unclear. It was initially reported
to be an antagonist of IL-36γ activity. This would be consistent with its hypothesized
relationship to IL-1ra.
原厂资料：
Mouse interleukin-36 receptor antagonist (IL-36Ra; previously IL-1F5; also named FIL-1δ
[delta], IL-1HY1, IL-1H3, and IL-1L1) is a member of the IL-1 family of proteins. IL-1 family
members include IL-1β, IL-1α, IL-1ra, IL-18 and IL-1F5 through F10. All family members show
a 12 β-strand, β-trefoil configuration, and are believed to have arisen from a common
ancestral gene that underwent multiple duplications. The mouse IL-36Ra/IL-1F5 gene maps
to a region on mouse chromosome 2 that contains all other IL1 family members (except IL-18),
supporting an evolutionary relationship with the IL-1 family. It is particularly close to the gene
for IL-1ra and is likely a relatively recent duplication of that gene. IL-36Ra/IL-1F5 is synthesized
as a 156 amino acid (aa) protein that contains no signal sequence, no prosegment and no
potential Nlinked glycosylation site(s). Nevertheless, it appears to be secreted as a 17 kDa
monomer. In humans, there is an alternate start site that potentially gives rise to an alternate
splice form. This translated product has a premature stop codon, resulting in a truncated 16 aa
peptide. Mouse to human, full length IL-36Ra/IL-1F5 has 90% aa identity. Within the family,
IL-36Ra/IL-1F5 is 48%, 30%, 35%, 35%, 35%, 37% and 43% aa identical to IL1ra, IL1β, IL36α/
IL-1F6, IL-37/IL-1F7, IL-36β/IL-1F8, IL-36γ/IL-1F9 and IL-1F10, respectively. Cells reported to
express IL-36Ra/IL-1F5 include monocytes, B cells, dendritic cells/Langerhans cells,
keratinocytes, and gastric fundus Parietal and Chief cells. The receptor for IL-36Ra/IL-1F5 has
not been positively identified. Indirect evidence suggests it is IL-1 Rrp2 and/or IL-1 RAcP. In
either case, activity association with receptor binding is unclear. It was initially reported
to be an antagonist of IL-36γ activity. This would be consistent with its hypothesized
relationship to IL-1ra.
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