Endoplasmic reticulum membrane sensor NFE2L1 - Q5ZL67 (NF2L1_CHICK)


Protein Feature View of PDB entries mapped to a UniProtKB sequence  

Endoplasmic reticulum membrane sensor that translocates into the nucleus in response to various stresses to act as a transcription factor (By similarity). Constitutes a precursor of the transcription factor NRF1 (By similarity). Able to detect various cellular stresses, such as cholesterol excess, oxidative stress or proteasome inhibition (By similarity). In response to stress, it is released from the endoplasmic reticulum membrane following cleavage and translocates into the nucleus to form the transcription factor NRF1 (By similarity). Acts as a key sensor of cholesterol excess: in excess cholesterol conditions, the endoplasmic reticulum membrane form of the protein directly binds cholesterol via its CRAC motif, preventing cleavage and release of the transcription factor NRF1, thereby allowing expression of genes promoting cholesterol removal (By similarity). Involved in proteasome homeostasis: in response to proteasome inhibition, it is released from the endoplasmic reticulum membrane, translocates to the nucleus and activates expression of genes encoding proteasome subunits (By similarity). UniProt
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Subunit Structure
Interacts (via the bZIP domain) with small MAF protein (MAFF, MAFG or MAFK); required for binding to antioxidant response elements (AREs) on DNA. UniProt
The cholesterol recognition/amino acid consensus (CRAC) region directly binds cholesterol, as well as campesterol and 27-hydroxycholesterol. Has much lower affinity for epicholesterol. UniProt
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