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 | 0006357 | biological_process | regulation of transcription by RNA polymerase II |
| A | 0006629 | biological_process | lipid metabolic process |
| A | 0006695 | biological_process | cholesterol biosynthetic process |
| A | 0008142 | molecular_function | oxysterol binding |
| A | 0008202 | biological_process | steroid metabolic process |
| A | 0008203 | biological_process | cholesterol metabolic process |
| A | 0008289 | molecular_function | lipid binding |
| A | 0032868 | biological_process | response to insulin |
| 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 | 0033993 | biological_process | response to lipid |
| A | 0036316 | biological_process | SREBP-SCAP complex retention in endoplasmic reticulum |
| A | 0070542 | biological_process | response to fatty acid |
| 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 | 22 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 33 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 22 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 18 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 21 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 17 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"source":"UniProtKB","id":"A1T557","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Site: {"description":"Required for the recognition of 25-hydroxycholesterol","evidences":[{"source":"PubMed","id":"17428920","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by PCK1","evidences":[{"source":"PubMed","id":"32322062","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=1","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=2","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 46 |
| Details | Topological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"P97260","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=3","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 11 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"source":"UniProtKB","id":"P97260","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=4","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI17 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=5","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI18 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=6","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI19 |
| Number of Residues | 20 |
| Details | Transmembrane: {"description":"Helical; Name=7","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI20 |
| Number of Residues | 158 |
| Details | Domain: {"description":"SSD","evidences":[{"source":"PROSITE-ProRule","id":"PRU00199","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI21 |
| Number of Residues | 2 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
