A0A8S9XU06 · A0A8S9XU06_APOLU
- Protein7-dehydrocholesterol reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids758 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Catalyzes the last step of the cholesterol synthesis pathway, which transforms cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol,7-DHC) into cholesterol by reducing the C7-C8 double bond of its sterol core. Can also metabolize cholesta-5,7,24-trien-3beta-ol (7-dehydrodemosterol, 7-DHD) to desmosterol, which is then metabolized by the Delta24-sterol reductase (DHCR24) to cholesterol. Modulates ferroptosis (a form of regulated cell death driven by iron-dependent lipid peroxidation) through the metabolic breakdown of the anti-ferroptotic metabolites 7-DHC and 7-DHD which, when accumulated, divert the propagation of peroxyl radical-mediated damage from phospholipid components to its sterol core, protecting plasma and mitochondrial membranes from phospholipid autoxidation.
Catalytic activity
- 7-dehydrodesmosterol + NADPH + H+ = desmosterol + NADP+This reaction proceeds in the forward direction.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | membrane | |
Molecular Function | 7-dehydrocholesterol reductase activity | |
Molecular Function | cysteine-type peptidase activity | |
Biological Process | brassinosteroid biosynthetic process | |
Biological Process | cholesterol biosynthetic process | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name7-dehydrocholesterol reductase
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Paraneoptera > Hemiptera > Heteroptera > Panheteroptera > Cimicomorpha > Miridae > Mirini > Apolygus
Accessions
- Primary accessionA0A8S9XU06
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 12-31 | Helical | ||||
Sequence: LVPPIFIVLFTALVQIVAQF | ||||||
Transmembrane | 51-67 | Helical | ||||
Sequence: TSWIVVLTFVFWAYLFL | ||||||
Transmembrane | 124-141 | Helical | ||||
Sequence: ILGTLSLVALLLCFYLFL | ||||||
Transmembrane | 204-220 | Helical | ||||
Sequence: YSQPVFATFFLHTIYLV | ||||||
Transmembrane | 241-261 | Helical | ||||
Sequence: GYYLCWGSIAWVPCFFTYNSY | ||||||
Transmembrane | 273-292 | Helical | ||||
Sequence: STAWVAIGIGLSAIAIQYLI | ||||||
Transmembrane | 351-379 | Helical | ||||
Sequence: VYALCVCIPGYGLGFTPFIYFFFLLVFVI |
Keywords
- Cellular component
PTM/Processing
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 454-514 | Cathepsin propeptide inhibitor | ||||
Sequence: WKLYKLVHSKTYEDEFEDAMRLELFKKSRREILEHNIKYELGLVKYTKGLNQFSDMLPEEL | ||||||
Domain | 541-757 | Peptidase C1A papain C-terminal | ||||
Sequence: IKAHVDWNAQGAVTEVKNQGHCGSCWAFASIGALEGQHFLKTKQLIPLSEQNLVDCAKGRRYHNRGCHGGWMNTAFQYIKDNRGVDTEDSYPYEAQDDECRFRKSNVGAKDAGFEQIPPGDEEALKAAVATKGPVAVAIDVKNSFYSYKRGVYFEQMCSPHTPRHAVLVVGYGSEGGEDYWLVKNSWGRGWGDDGFVKMARNRNDHCGIASYASYPL |
Sequence similarities
Belongs to the ERG4/ERG24 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length758
- Mass (Da)86,123
- Last updated2022-10-12 v1
- ChecksumAD672DCB81409AD9
Keywords
- Technical term