SREBP cleavage activating protein

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SREBF chaperone
Identifiers
Symbol SCAP
Entrez 22937
HUGO 30634
OMIM 601510
RefSeq NM_012235
UniProt Q12770
Other data
Locus Chr. 3 p21.31

SREBP cleavage-activating protein (SCAP) is a regulatory protein that is required for the proteolytic cleavage of the sterol regulatory element binding protein (SREBP). SCAP is an integral membrane protein located in the endoplasmic reticulum (ER). One of the cytosolic regions of SCAP contains a hexapeptide amino acid sequence, MELADL, that functions to detect cellular cholesterol. When cholesterol is present, SCAP undergoes a conformational change that prevents it from activating SREBP and cholesterol synthesis does not occur.[1]

Scap has 8 transmembrane domains and both the N terminal and C terminal face the cytoplasm. Also, it binds SREBP by a series of consecutive WD repeats on it's C-terminus.[2]

[edit] References

  1. ^ Sun LP, Seemann J, Goldstein JL, Brown MS (2007). "Sterol-regulated transport of SREBPs from endoplasmic reticulum to Golgi: Insig renders sorting signal in Scap inaccessible to COPII proteins". Proc. Natl. Acad. Sci. U.S.A. 104 (16): 6519–26. doi:10.1073/pnas.0700907104. PMID 17428919. 
  2. ^ Brown MS, Goldstein JL (1999). "A proteolytic pathway that controls the cholesterol content of membranes, cells, and blood". Proc. Natl. Acad. Sci. U.S.A. 96 (20): 11041–8. doi:10.1073/pnas.96.20.11041. PMID 10500120. 
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