Sterol-sensing domain of SREBP cleavage-activation

Definition

Sterol regulatory element-binding proteins (SREBPs) are membrane-bound transcription factors that promote lipid synthesis in animal cells. They are embedded in the membranes of the endoplasmic reticulum (ER) in a helical hairpin orientation and are released from the ER by a two-step proteolytic process. Proteolysis begins when the SREBPs are cleaved at Site-1, which is located at a leucine residue in the middle of the hydrophobic loop in the lumen of the ER PMID:9488713. Upon proteolytic processing SREBP can activate the expression of genes involved in cholesterol biosynthesis and uptake. SCAP stimulates cleavage of SREBPs via fusion of the their two C-termini PMID:17604677. This domain is the transmembrane region that traverses the membrane eight times and is the sterol-sensing domain of the cleavage protein PMID:12482938. WD40 domains are found towards the C-terminus.

8 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

Download CSV (8 proteins: gene, accession, name)

• DISP1
• DISP3
• HMGCR
• NPC1
• NPC1L1
• PTCH1
• PTCH2
• SCAP