| Primary Identifier | IPR032350 | Type | Domain |
| Short Name | Nbr1_FW |
| description | This entry represents the FW domain found in Nbr1 and similar eukaryotic proteins, including JOKA2 from Solanum tuberosum. In the fungus Chaetomium thermophilum it has been shown to bind the alpha-mannosidase Ams1, a cargo of selective autophagy in both budding yeast and fission yeast, and delivers Ams1 to the vacuole by autophagy in heterologous fission yeast. The FW domain has also been shown to interact with the microtubule-associated protein MAP1B []. Structurally, the FW domain adopts an immunoglobulin-like ��-sandwich structure and recognises the quaternary structure of the Ams1 tetramer [].Nbr1 (Next to BRCA1 gene 1) is a ubiquitin-binding autophagy adapter that participates in different processes, including host defence or intracellular homeostasis []. Nbr1-like molecules contain an N-terminal PB1 domain, one (animals, plants) or more (fungi) ZZ domains, an FW domain, and a C-terminal UBA domain [].JOKA2 activates ATG8CL-mediated selective autophagy, and contributes to defense against the fungal pathogen Phytophtora infestans [, ].ILRUN is a negative regulator of the innate antiviral response that blocks IRF3-dependent cytokine production, including IFNA, IFNB and TNF. ILRUN interacts with IRF3 and inhibits its recruitment to type I IFN promoter sequences, while also reducing nuclear levels of the coactivators EP300 and CREBBP []. It is a paralog of NRBF2. |
