Q12770: Sterol regulatory element-binding protein cleavage-activating protein (SCAP)

Sterol regulatory element-binding protein cleavage-activating protein (SCAP) is a 1279-residue protein from Homo sapiens. This is its AlphaFold structure prediction, created 1 Aug 2025. UniProt accession: Q12770.

Gene
SCAP
Organism
Homo sapiens
Length
1279 residues
Mean pLDDT
65.3
Model
AF-Q12770-F1 v6
Model created
1 Aug 2025
PDB structures
2

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Model confidence (pLDDT)

The mean pLDDT of this model is 65.3 (low overall). pLDDT is AlphaFold's per-residue confidence score from 0 to 100. In MolViewer, choose the B-factor color scheme to color the model by pLDDT, because AlphaFold stores it in the B-factor column.

pLDDT bandMeaningShare of residues
Above 90Very high: backbone and side chains are usually accurate8%
70 to 90Confident: backbone generally right49%
50 to 70Low: treat with caution13%
Below 50Very low: often disordered regions30%

What pLDDT means and how to read it

Function

Escort protein required for cholesterol as well as lipid homeostasis (By similarity). Regulates export of the SCAP-SREBP complex from the endoplasmic reticulum to the Golgi upon low cholesterol, thereby regulating the processing of sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2 (PubMed:26311497). At high sterol concentrations, formation of a ternary complex with INSIG (INSIG1 or INSIG2) leads to mask the ER export signal in SCAP, promoting retention of the complex in the endoplasmic reticulum (By similarity). Low sterol concentrations trigger release of INSIG, a conformational change in the SSD domain of SCAP, unmasking of the ER export signal,…

Subunit structure

Membrane region forms a homotetramer (By similarity). Component of the SCAP-SREBP complex (composed of SCAP and SREBF1/SREBP1 or SREBF2/SREBP2); interacts with SREBF1/SREBP1 or SREBF2/SREBP2 through its C-terminal cytoplasmic domain (PubMed:26311497). Forms a ternary complex with INSIG1 or INSIG2 through its transmembrane domains at high sterol concentrations (PubMed:17428920, PubMed:26160948).…

Subcellular location

Endoplasmic reticulum membrane, Golgi apparatus membrane, Cytoplasmic vesicle, COPII-coated vesicle membrane

Experimental structures in the PDB

Compare the prediction with experimentally determined structures of the same protein:

PDB IDMethodResolutionChains and residues
6M49EM3.7 ÅB=1-735
7ETWEM4.1 ÅB=1-735

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