LMPD Database

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LMP013185

UniProt Annotations

Entry Information
Gene Namesterol regulatory element binding transcription factor 2
Protein EntrySRBP2_RAT
UniProt IDQ3T1I5
SpeciesRat
Comments
Comment typeDescription
FunctionTranscriptional activator required for lipid homeostasis. Regulates transcription of the LDL receptor gene as well as the cholesterol and to a lesser degree the fatty acid synthesis pathway (By similarity). Binds the sterol regulatory element 1 (SRE-1) (5'-ATCACCCCAC-3') found in the flanking region of the LDRL and HMG-CoA synthase genes (By similarity)
PtmAt low cholesterol the SCAP/SREBP complex is recruited into COPII vesicles for export from the ER. In the Golgi complex SREBPs are cleaved sequentially by site-1 and site-2 protease. The first cleavage by site-1 protease occurs within the luminal loop, the second cleavage by site-2 protease occurs within the first transmembrane domain and releases the transcription factor from the Golgi membrane. Apoptosis triggers cleavage by the cysteine proteases caspase-3 and caspase-7 (By similarity)
PtmPhosphorylated by AMPK, leading to suppress protein processing and nuclear translocation, and repress target gene expression
SimilarityBelongs to the SREBP family
SimilarityContains 1 bHLH (basic helix-loop-helix) domain
Subcellular LocationEndoplasmic reticulum membrane ; Multi-pass membrane protein . Golgi apparatus membrane ; Multi-pass membrane protein . Cytoplasmic vesicle, COPII-coated vesicle membrane ; Multi-pass membrane protein . Note=Moves from the endoplasmic reticulum to the Golgi in the absence of sterols
Subcellular LocationProcessed sterol regulatory element-binding protein 2: Nucleus {ECO:0000250|UniProtKB:Q12772, ECO:0000255|PROSITE-ProRule:PRU00981}.
SubunitForms a tight complex with SCAP in the ER membrane. Efficient DNA binding of the soluble transcription factor fragment requires dimerization with another bHLH protein. Interacts with LMNA. Component of SCAP/SREBP complex composed of SREBF2, SCAP and RNF139; the complex hampers the interaction between SCAP and SEC24B, thereby reducing SREBF2 proteolytic processing. Interacts (via C-terminal domain) with RNF139 (By similarity)