描述：
Human interleukin-36 receptor antagonist [IL-36Ra; previously IL-1F5 and also named FIL-1δ
(delta), IL-1HY1, IL-1H3, and IL1L1] is a member of the IL-1 family of proteins. IL-1 family
members include IL-1β, IL-1α, IL-1ra, IL-18 and IL1F5F10. All family members show a 12
βstrand, βtrefoil configuration, and all family members are believed to have arisen from a
common ancestral gene that underwent multiple duplications. The human IL-36Ra/IL-1F5
gene is in closest proximity to the gene for IL1ra and is likely a relatively recent duplication
of the IL1ra gene. IL-36Ra/IL-1F5 is synthesized as a 155 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.There is an alternate start site that potentially
gives rise to an alternate splice form. The translated product, however, has a premature stop
codon, resulting in a truncated 16 aa peptide. Human to mouse, full length IL-1F5 has 90% aa
identity. Within the family, IL-36Ra/IL1F5 is 50% aa identical to IL1ra, and 32%, 31%, 35%,
37%, 32% and 42% aa identical to 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 IL1 Rrp2 and/or IL-1 RAcP. In either case, activity association with receptor binding is
also unclear. It was initially reported to be an antagonist of IL-36γ/IL-1F9 activity. This would
be consistent with its hypothesized relationship to IL-1ra. Studies, however, find IL-36Ra/IL-1F5
antagonist activity difficult to demonstrate.
原厂资料：
Human interleukin-36 receptor antagonist [IL-36Ra; previously IL-1F5 and also named FIL-1δ
(delta), IL-1HY1, IL-1H3, and IL1L1] is a member of the IL-1 family of proteins. IL-1 family
members include IL-1β, IL-1α, IL-1ra, IL-18 and IL1F5F10. All family members show a 12
βstrand, βtrefoil configuration, and all family members are believed to have arisen from a
common ancestral gene that underwent multiple duplications. The human IL-36Ra/IL-1F5
gene is in closest proximity to the gene for IL1ra and is likely a relatively recent duplication
of the IL1ra gene. IL-36Ra/IL-1F5 is synthesized as a 155 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.There is an alternate start site that potentially
gives rise to an alternate splice form. The translated product, however, has a premature stop
codon, resulting in a truncated 16 aa peptide. Human to mouse, full length IL-1F5 has 90% aa
identity. Within the family, IL-36Ra/IL1F5 is 50% aa identical to IL1ra, and 32%, 31%, 35%,
37%, 32% and 42% aa identical to 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 IL1 Rrp2 and/or IL-1 RAcP. In either case, activity association with receptor binding is
also unclear. It was initially reported to be an antagonist of IL-36γ/IL-1F9 activity. This would
be consistent with its hypothesized relationship to IL-1ra. Studies, however, find IL-36Ra/IL-1F5
antagonist activity difficult to demonstrate.
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