Q7ZXH1 · DHCR7_XENLA
- Protein7-dehydrocholesterol reductase
- Genedhcr7
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids473 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score3/5
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 (By similarity).
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 (By similarity).
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 (By similarity).
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 (By similarity).
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 (By similarity).
Catalytic activity
- cholesterol + NADP+ = 7-dehydrocholesterol + H+ + NADPHThis reaction proceeds in the backward direction.
- 7-dehydrodesmosterol + H+ + NADPH = desmosterol + NADP+This reaction proceeds in the forward direction.
Pathway
Steroid biosynthesis; cholesterol biosynthesis.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 356 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 360 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 393 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: M | ||||||
Binding site | 398 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: W | ||||||
Binding site | 405-406 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: NY | ||||||
Binding site | 445 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 449-453 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: CSSKY | ||||||
Binding site | 460 | NADP+ (UniProtKB | ChEBI) | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endoplasmic reticulum membrane | |
Molecular Function | 7-dehydrocholesterol reductase activity | |
Molecular Function | NADP binding | |
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
- Short names7-DHC reductase
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Amphibia > Batrachia > Anura > Pipoidea > Pipidae > Xenopodinae > Xenopus > Xenopus
Accessions
- Primary accessionQ7ZXH1
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Endoplasmic reticulum membrane ; Multi-pass membrane protein
Features
Showing features for transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Transmembrane | 36-56 | Helical | ||||
Sequence: FSLASVIFLLAFAPLIVYYFV | ||||||
Transmembrane | 97-117 | Helical | ||||
Sequence: IYLAWVSFQVFLYMFLPDILH | ||||||
Transmembrane | 175-195 | Helical | ||||
Sequence: WIPLLWCANLLGYSVATFALV | ||||||
Transmembrane | 264-284 | Helical | ||||
Sequence: VTNSMILVNVLQAIYVVDFFW | ||||||
Transmembrane | 304-324 | Helical | ||||
Sequence: LGWGDCVWLPYLYTLQGLYLV | ||||||
Transmembrane | 329-349 | Helical | ||||
Sequence: ELSTTAAVAVLLLGLIGYYIF | ||||||
Transmembrane | 419-439 | Helical | ||||
Sequence: ACGFDHLLPYFYFIYMTILLV |
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000207506 | 1-473 | 7-dehydrocholesterol reductase | |||
Sequence: MGERRRANASRGDKKVANGEKQHVGQWGRAWEVDYFSLASVIFLLAFAPLIVYYFVMSCDQYQCALTAPVLDLYSGKARLSDIWDKTPALTWTAVKIYLAWVSFQVFLYMFLPDILHKFVPGYEGGVQEGARTPAGLINKYQVNGLQAWTITHLLWFANAYHFHWFSPTIVIDNWIPLLWCANLLGYSVATFALVKANFFPTNANDCKFTGNFFYDYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSYAAKQQELYGQVTNSMILVNVLQAIYVVDFFWNESWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYNPVELSTTAAVAVLLLGLIGYYIFRMTNHQKDLFRRTNGNCKIWGKKPKSIECFYVSADGKRHYSKLMISGFWGVARHLNYTGDLMGSLAYCLACGFDHLLPYFYFIYMTILLVHRCIRDEHRCSSKYGKDWKLYTSAVPYRLLPGLF |
Expression
Gene expression databases
Structure
Sequence
- Sequence statusComplete
- Length473
- Mass (Da)54,823
- Last updated2003-06-01 v1
- Checksum8EB14E8186BDC463
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BC044995 EMBL· GenBank· DDBJ | AAH44995.1 EMBL· GenBank· DDBJ | mRNA |