Rel (Relish; CG11992; UniProt Q94527) notes
Identity
- Compound NF-kappaB family transcription factor resembling mammalian p105/p100: N-terminal Rel homology domain (RHD) plus C-terminal IkappaB-like ankyrin-repeat domain
PMID:8816802.
Activation (Imd/PGRP pathway)
- Signal-induced endoproteolytic cleavage; RHD (REL-68) goes to the nucleus, IkappaB-like part (REL-49) stays in cytoplasm
PMID:11269501,
PMID:11269501.
- Cleavage is Cactus-independent PMID:11400160.
- IKK (IKKbeta/Kenny) phosphorylates Relish S528/S529, needed for Pol II recruitment, not for cleavage
PMID:19497884.
- REL-68 alone activates Diptericin PMID:19135474.
- Forms homo- and heterodimers with Dif and Dorsal PMID:20679214.
Immune roles
- Required for humoral immunity (antibacterial and some antifungal peptides), not cellular immunity
PMID:10619029.
- Antiviral: STING-IKKbeta-Relish axis PMID:30119996;
2'3'-cGAMP protection requires Relish PMID:33262294.
- Feedback: Relish induces negative regulators (miR-317, miR-308, miR-275, IMZF, lncRNAs) to restore homeostasis (PMIDs 36155909, 37358278, 37804878, 38762126, 37956726).
- Relish restrains JAK/STAT by interfering with Domeless dimerization PMID:35905720.
Non-immune / context-specific
Deep research
- Falcon deep research (
Rel-deep-research-falcon.md) arrived after the first commit; it agrees that Relish is a [file:DROME/Rel/Rel-deep-research-falcon.md "sequence-specific transcription factor, not an enzyme, transporter, or secreted antimicrobial peptide"].
Review decisions
- Core: RNA Pol II-specific DNA-binding transcription activator, nuclear, in PGRP (Imd) and STING pathways.
- Generic protein binding removed except DIF-Relish dimerization (MODIFY to protein heterodimerization activity).
- ARBA IEA development terms (cell development, system development, anatomical part development) marked over-annotated.