描述：
Human interleukin 1 family member 7 (IL-1F7), also named FIL1Z, IL1H4, and IL1RP1,
belongs to the IL1 cytokine family, which currently has ten members. With the exception
of IL18 that maps to human chromosome 11, all other IL1 family members map to the
same cluster on human chromosome 2. Five alternatively spliced transcripts that arise through
alternate exon usage have been described. These transcripts encode five different IL-1F7
isoforms (IL-1F7a through e also referred to as isofoms 1 through 5) that have distinct
expression profiles. Polymorphism in the protein sequence of IL-1F7 isoforms also exists.
Like IL1α, IL1β and IL18, all of the IL-1F7 variants lack a typical signal peptide. The longest
IL-1F7 transcript, referred to as IL-1F7b or IL-1F7 isoform 1, encodes a 218 amino acid (aa)
residues proprotein containing a 45 aa propeptide, which is removed by caspase1 to generate
the 173 aa mature segment. MatureIL-1F7b and other IL-1F7 variants lack potential Nlinked
glycosylation sites. The secreted mature IL-17F7b was reported to exist as a nondisulfide linked
homodimers in solution, IL-1F7 shares approximately 21%, 24%, and 30% aa sequence identity
with mature IL-1α, IL-1β and IL-1ra, respectively. Mouse IL-1F7 has not been reported, but
human IL-1F7 is active on mouse cells. IL-1F7b binds to IL-18 Rα with low affinity but does not
exert any IL18 agonistic or antagonistic effects. IL-1F7b also binds to the IL18BP to enhance
the antagonistic effects of IL18BP. It has been proposed that IL-1F7b form a trimeric complex
with IL18BP and IL18 Rβ. This complex blocks IL18 activity by sequestering the signal
transducing subunit and preventing it from participating in IL18 signaling.
原厂资料：
Human interleukin 1 family member 7 (IL-1F7), also named FIL1Z, IL1H4, and IL1RP1,
belongs to the IL1 cytokine family, which currently has ten members. With the exception
of IL18 that maps to human chromosome 11, all other IL1 family members map to the
same cluster on human chromosome 2. Five alternatively spliced transcripts that arise through
alternate exon usage have been described. These transcripts encode five different IL-1F7
isoforms (IL-1F7a through e also referred to as isofoms 1 through 5) that have distinct
expression profiles. Polymorphism in the protein sequence of IL-1F7 isoforms also exists.
Like IL1α, IL1β and IL18, all of the IL-1F7 variants lack a typical signal peptide. The longest
IL-1F7 transcript, referred to as IL-1F7b or IL-1F7 isoform 1, encodes a 218 amino acid (aa)
residues proprotein containing a 45 aa propeptide, which is removed by caspase1 to generate
the 173 aa mature segment. MatureIL-1F7b and other IL-1F7 variants lack potential Nlinked
glycosylation sites. The secreted mature IL-17F7b was reported to exist as a nondisulfide linked
homodimers in solution, IL-1F7 shares approximately 21%, 24%, and 30% aa sequence identity
with mature IL-1α, IL-1β and IL-1ra, respectively. Mouse IL-1F7 has not been reported, but
human IL-1F7 is active on mouse cells. IL-1F7b binds to IL-18 Rα with low affinity but does not
exert any IL18 agonistic or antagonistic effects. IL-1F7b also binds to the IL18BP to enhance
the antagonistic effects of IL18BP. It has been proposed that IL-1F7b form a trimeric complex
with IL18BP and IL18 Rβ. This complex blocks IL18 activity by sequestering the signal
transducing subunit and preventing it from participating in IL18 signaling.
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