A0A147BGY7 · A0A147BGY7_IXORI
- Protein7-dehydrocholesterol reductase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids718 (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 | |
Biological Process | brassinosteroid biosynthetic process | |
Biological Process | cholesterol biosynthetic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended name7-dehydrocholesterol reductase
- EC number
- Alternative names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Chelicerata > Arachnida > Acari > Parasitiformes > Ixodida > Ixodoidea > Ixodidae > Ixodinae > Ixodes
Accessions
- Primary accessionA0A147BGY7
Subcellular Location
UniProt Annotation
GO Annotation
Membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 307-333 | Helical | ||||
Sequence: AFGWGPTLASLCWLLLLPVLALAVQLL | ||||||
Transmembrane | 353-377 | Helical | ||||
Sequence: LRWQLFAGYAGFLLAQALLQALPVG | ||||||
Transmembrane | 398-419 | Helical | ||||
Sequence: LNGWVNLLATAAAFGCLVYYGF | ||||||
Transmembrane | 425-448 | Helical | ||||
Sequence: QLYSLQLLVAVLLTATVLSVLLYI | ||||||
Transmembrane | 516-537 | Helical | ||||
Sequence: CLGYGFATSAACQLVYICMAFY | ||||||
Transmembrane | 552-573 | Helical | ||||
Sequence: ALGYVSLVANLALLPLLSSLPA | ||||||
Transmembrane | 585-604 | Helical | ||||
Sequence: LYCLASVGAIFLLGLALLHL | ||||||
Transmembrane | 670-688 | Helical | ||||
Sequence: ALPYTAVLLQALFLVVRVF |
Keywords
- Cellular component
Structure
Family & Domains
Features
Showing features for compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-17 | Basic and acidic residues | ||||
Sequence: ESTADMAPDKKTKTQPS | ||||||
Region | 1-240 | Disordered | ||||
Sequence: ESTADMAPDKKTKTQPSEGRPTTRSNSGSRLASAAARDKSSSPSRGRSPKPSSPGKRQASRSRSRSQGRVGRPKSPGKVGRPKGSGKSPPGRPGRKPSPAKKSPGRKPSPVKKSPARKPPSKSPARSNARASSSDRSPVKSAAPKSPGRKSPARVPAKRADTPRAQSKSPSRPSMAGGRRSVSPAAKEQETNRKGAATPPRLPVGTPGQTVTPRSPLRRRSVPTPWSGAERPDSKGNSVL | ||||||
Compositional bias | 18-66 | Polar residues | ||||
Sequence: EGRPTTRSNSGSRLASAAARDKSSSPSRGRSPKPSSPGKRQASRSRSRS | ||||||
Compositional bias | 99-113 | Basic residues | ||||
Sequence: PAKKSPGRKPSPVKK | ||||||
Compositional bias | 125-140 | Polar residues | ||||
Sequence: ARSNARASSSDRSPVK |
Sequence similarities
Belongs to the ERG4/ERG24 family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusFragment
- Length718
- Mass (Da)78,374
- Last updated2016-06-08 v1
- Checksum417E462D6A2731F4
Features
Showing features for non-terminal residue, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 1 | |||||
Sequence: E | ||||||
Compositional bias | 1-17 | Basic and acidic residues | ||||
Sequence: ESTADMAPDKKTKTQPS | ||||||
Compositional bias | 18-66 | Polar residues | ||||
Sequence: EGRPTTRSNSGSRLASAAARDKSSSPSRGRSPKPSSPGKRQASRSRSRS | ||||||
Compositional bias | 99-113 | Basic residues | ||||
Sequence: PAKKSPGRKPSPVKK | ||||||
Compositional bias | 125-140 | Polar residues | ||||
Sequence: ARSNARASSSDRSPVK |