7ETW
Cryo-EM structure of Scap/Insig complex in the present of digitonin.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005515 | molecular_function | protein binding |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0006641 | biological_process | triglyceride metabolic process |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0006991 | biological_process | response to sterol depletion |
| A | 0008142 | molecular_function | oxysterol binding |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0010894 | biological_process | negative regulation of steroid biosynthetic process |
| A | 0016020 | cellular_component | membrane |
| A | 0016126 | biological_process | sterol biosynthetic process |
| A | 0032869 | biological_process | cellular response to insulin stimulus |
| A | 0032933 | biological_process | SREBP signaling pathway |
| A | 0032937 | cellular_component | SREBP-SCAP-Insig complex |
| A | 0036316 | biological_process | SREBP-SCAP complex retention in endoplasmic reticulum |
| A | 0042472 | biological_process | inner ear morphogenesis |
| A | 0042474 | biological_process | middle ear morphogenesis |
| A | 0045717 | biological_process | negative regulation of fatty acid biosynthetic process |
| A | 0060021 | biological_process | roof of mouth development |
| A | 0060363 | biological_process | cranial suture morphogenesis |
| A | 0140311 | molecular_function | protein sequestering activity |
| B | 0000139 | cellular_component | Golgi membrane |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0032933 | biological_process | SREBP signaling pathway |
| B | 0032934 | molecular_function | sterol binding |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 136 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000250|UniProtKB:P97260 |
| Chain | Residue | Details |
| B | MET1-HIS18 | |
| B | PHE301-LYS312 | |
| B | LYS366-GLY401 | |
| B | ARG445-ARG518 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=1 => ECO:0000255 |
| Chain | Residue | Details |
| B | GLY19-ALA39 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 419 |
| Details | TOPO_DOM: Lumenal => ECO:0000250|UniProtKB:P97260 |
| Chain | Residue | Details |
| B | CYS40-GLU279 | |
| B | CYS334-ASN344 | |
| B | VAL423 | |
| B | ARG540-TYR709 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=2 => ECO:0000255 |
| Chain | Residue | Details |
| B | ILE280-TYR300 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=3 => ECO:0000255 |
| Chain | Residue | Details |
| B | TRP313-LEU333 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=4 => ECO:0000255 |
| Chain | Residue | Details |
| B | GLY345-THR365 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=5 => ECO:0000255 |
| Chain | Residue | Details |
| B | ILE402-VAL422 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=6 => ECO:0000255 |
| Chain | Residue | Details |
| B | GLY424-ILE444 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=7 => ECO:0000255 |
| Chain | Residue | Details |
| B | LEU519-LEU539 |
| site_id | SWS_FT_FI10 |
| Number of Residues | 20 |
| Details | TRANSMEM: Helical; Name=8 => ECO:0000255 |
| Chain | Residue | Details |
| B | LYS710-TYR730 |
| site_id | SWS_FT_FI11 |
| Number of Residues | 3 |
| Details | CARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255 |
| Chain | Residue | Details |
| B | ASN263 | |
| B | ASN590 | |
| B | ASN641 |
| site_id | SWS_FT_FI12 |
| Number of Residues | 3 |
| Details | CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q6GQT6 |
| Chain | Residue | Details |
| B | LYS454 | |
| B | LYS466 |
