id: Q9UBM7
gene_symbol: DHCR7
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: 7-dehydrocholesterol reductase (7-DHC reductase; Delta7-sterol reductase;
  EC 1.3.1.21) is an NADPH-dependent oxidoreductase of the endoplasmic reticulum membrane
  that catalyses the final step of cholesterol biosynthesis, reducing the C7-C8 double
  bond of 7-dehydrocholesterol (7-DHC) to yield cholesterol. It is the terminal enzyme
  of the Kandutsch-Russell arm of the sterol biosynthetic pathway and can also reduce
  7-dehydrodesmosterol to desmosterol. Because 7-DHC is also the immediate precursor
  of vitamin D3, DHCR7 activity partitions 7-DHC between cholesterol and vitamin D3
  synthesis, and its activity is modulated by physical interaction with the other terminal
  sterol reductase DHCR24. It is a multi-pass integral membrane protein of the ERG4/ERG24
  sterol-reductase family. Loss-of-function mutations cause Smith-Lemli-Opitz syndrome
  (SLOS), an autosomal-recessive cholesterol-biosynthesis malformation disorder characterised
  by elevated 7-DHC and low cholesterol with microcephaly, 2-3 toe syndactyly and developmental
  delay.
existing_annotations:
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: DHCR7 is an integral endoplasmic reticulum membrane enzyme; this is where
      its terminal cholesterol-biosynthesis reaction takes place.
    action: ACCEPT
    reason: The ER-membrane localization is well supported experimentally (subcellular
      fractionation/immunolocalization) and by the multi-pass transmembrane topology.
      The is_active_in qualifier correctly captures that catalysis occurs at the ER
      membrane. This is a core cellular-component annotation.
    supported_by:
    - reference_id: PMID:9878250
      supporting_text: these two related proteins are in the endoplasmic reticulum
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: DHCR7 catalyses the last step of cholesterol biosynthesis, converting
      7-dehydrocholesterol to cholesterol.
    action: ACCEPT
    reason: This is the central biological process for DHCR7 and is supported by biochemistry,
      disease genetics (SLOS), and phylogenetic inference. Core biological-process
      annotation.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The Delta7-sterol reductase is the ultimate enzyme of cholesterol
        biosynthesis in vertebrates and is absent from yeast.
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: The specific molecular function of DHCR7 - NADPH-dependent reduction of
      the C7-C8 double bond of 7-dehydrocholesterol to cholesterol (EC 1.3.1.21).
    action: ACCEPT
    reason: This is the precise, correct molecular-function term and the core function
      of the gene. Strongly supported by direct enzymatic characterization across
      orthologs and phylogenetic inference.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: remove the C7-8 double bond in 7-dehydrocholesterol
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: ER membrane localization inferred from the UniProt Subcellular Location
      vocabulary mapping.
    action: ACCEPT
    reason: Correct and consistent with experimental localization; this IEA mirrors
      the curated Swiss-Prot subcellular location.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
- term:
    id: GO:0016020
    label: membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: located_in
  review:
    summary: Generic membrane localization from InterPro domain mapping.
    action: MARK_AS_OVER_ANNOTATED
    reason: 'DHCR7 is a multi-pass membrane protein, so ''membrane'' is not wrong,
      but it is far less informative than the specific and experimentally supported
      GO:0005789 endoplasmic reticulum membrane already annotated. Retain only as a
      generic parent.'
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: Multi-pass membrane protein
- term:
    id: GO:0016126
    label: sterol biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: Sterol biosynthetic process, the broader biosynthetic category encompassing
      cholesterol biosynthesis.
    action: ACCEPT
    reason: Correct-branch parent of the specific cholesterol biosynthetic process;
      DHCR7 acts in sterol/cholesterol biosynthesis. Reasonable broader annotation
      from InterPro.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: Belongs to the ERG4/ERG24 family
- term:
    id: GO:0016628
    label: oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP
      as acceptor
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: General oxidoreductase activity (CH-CH group donors, NAD/NADP acceptor)
      inferred from InterPro.
    action: MARK_AS_OVER_ANNOTATED
    reason: 'This is a correct-branch but overly general parent of the specific and
      experimentally established GO:0047598 7-dehydrocholesterol reductase activity.
      DHCR7 does reduce a C-C double bond using NADPH, so the term is not wrong, but
      the specific term should be preferred.'
    proposed_replacement_terms:
    - id: GO:0047598
      label: 7-dehydrocholesterol reductase activity
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The conversion to cholesterol depends on NADPH
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: 7-dehydrocholesterol reductase activity (EC 1.3.1.21) from automated annotation
      (ARBA/RHEA/EC mapping).
    action: ACCEPT
    reason: Correct specific molecular function, consistent with the RHEA:23984 / EC
      1.3.1.21 reaction and experimental evidence. Core function.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: EC=1.3.1.21
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6807047
  qualifier: involved_in
  review:
    summary: Cholesterol biosynthetic process, asserted via the Reactome Bloch-pathway
      (via desmosterol) module.
    action: ACCEPT
    reason: DHCR7 participates in cholesterol biosynthesis; the Reactome pathway assertion
      is consistent with the enzyme's established role. Core biological process.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The Delta7-sterol reductase is the ultimate enzyme of cholesterol
        biosynthesis in vertebrates and is absent from yeast.
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9969901
  qualifier: involved_in
  review:
    summary: Cholesterol biosynthetic process, asserted via the Reactome modified Kandutsch-Russell
      (from zymosterol) module - the arm terminated by DHCR7.
    action: ACCEPT
    reason: Consistent with DHCR7's role as the terminal enzyme of the Kandutsch-Russell
      arm of cholesterol synthesis. Core biological process.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The Delta7-sterol reductase is the ultimate enzyme of cholesterol
        biosynthesis in vertebrates and is absent from yeast.
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: Cholesterol biosynthetic process from automated UniPathway (UPA00063)
      mapping.
    action: ACCEPT
    reason: Correct pathway assignment consistent with the curated UniProt PATHWAY
      annotation (cholesterol biosynthesis). Core biological process.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'PATHWAY: Steroid biosynthesis; cholesterol biosynthesis.'
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: EXP
  original_reference_id: PMID:9465114
  qualifier: enables
  review:
    summary: Direct demonstration that the cloned human enzyme removes the C7-C8 double
      bond of 7-dehydrocholesterol, converting it to cholesterol in an NADPH-dependent
      manner.
    action: ACCEPT
    reason: Experimental evidence directly establishing the core molecular function.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: Microsomes from Saccharomyces cerevisiae strains heterologously
        expressing the human cDNA remove the C7-8 double bond in 7-dehydrocholesterol.
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IDA
  original_reference_id: GO_REF:0000052
  qualifier: located_in
  review:
    summary: Immunofluorescence (Human Protein Atlas) localizes DHCR7 to the endoplasmic
      reticulum.
    action: ACCEPT
    reason: Consistent with the more specific ER membrane localization; ER is the correct
      compartment. Retained as the (broader) directly observed compartment.
    supported_by:
    - reference_id: PMID:9878250
      supporting_text: these two related proteins are in the endoplasmic reticulum
- term:
    id: GO:0033963
    label: cholesterol-5,6-oxide hydrolase activity
  evidence_type: IMP
  original_reference_id: PMID:20615952
  qualifier: enables
  review:
    summary: DHCR7, together with EBP (D8D7I), constitutes the microsomal antiestrogen
      binding site (AEBS) that carries cholesterol-5,6-epoxide hydrolase (ChEH) activity;
      co-expression of both subunits reconstitutes ChEH and double knockdown abolishes
      it.
    action: KEEP_AS_NON_CORE
    reason: This is a genuine, experimentally supported (IMP) secondary/moonlighting
      activity in which DHCR7 acts as a subunit of the heterodimeric AEBS complex,
      and it is recorded by UniProt (AltName "Cholesterol-5,6-epoxide hydrolase subunit
      DHCR7", EC 3.3.2.11). It is not the core reductase function and DHCR7 alone confers
      only weak activity (the activity requires the EBP-DHCR7 dimer), so it is kept
      as non-core rather than accepted as a core function. Not removed, as the full-text
      experimental evidence supports it.
    supported_by:
    - reference_id: PMID:20615952
      supporting_text: whereas their coexpression fully
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: The precise role of
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IMP
  original_reference_id: PMID:38297129
  qualifier: involved_in
  review:
    summary: Genetic/functional manipulation of DHCR7 (including SLOS variants and
      active-site mutagenesis) confirms its role in cholesterol biosynthesis via 7-DHC
      reduction.
    action: ACCEPT
    reason: Mutagenesis and variant characterization in this study confirm that DHCR7
      converts 7-DHC to cholesterol, supporting its role in the cholesterol biosynthetic
      process. Core biological process.
    supported_by:
    - reference_id: PMID:38297129
      supporting_text: we identify proferroptotic activity of 7-dehydrocholesterol
        reductase (DHCR7) and an unexpected prosurvival function of its substrate,
        7-dehydrocholesterol (7-DHC)
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IMP
  original_reference_id: PMID:38297130
  qualifier: involved_in
  review:
    summary: CRISPR screening and functional analysis place DHCR7 as the enzyme that
      metabolizes 7-DHC for cholesterol synthesis in distal cholesterol biosynthesis.
    action: ACCEPT
    reason: Independently confirms DHCR7's role in cholesterol biosynthesis via 7-DHC
      reduction. Core biological process.
    supported_by:
    - reference_id: PMID:38297130
      supporting_text: metabolized by 7-DHC reductase (DHCR7) for cholesterol synthesis
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: IMP
  original_reference_id: PMID:38297129
  qualifier: enables
  review:
    summary: Active-site mutagenesis (e.g., N274K, L306R cause loss of activity) and
      SLOS variant characterization confirm the 7-DHC reductase activity of DHCR7.
    action: ACCEPT
    reason: Direct functional (mutagenesis) evidence for the core molecular function.
    supported_by:
    - reference_id: PMID:38297129
      supporting_text: we identify proferroptotic activity of 7-dehydrocholesterol
        reductase (DHCR7)
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: IMP
  original_reference_id: PMID:38297130
  qualifier: enables
  review:
    summary: Functional evidence that DHCR7 is the reductase metabolizing 7-DHC in
      distal cholesterol biosynthesis.
    action: ACCEPT
    reason: Supports the core molecular function through loss/gain-of-function analysis
      of DHCR7 and 7-DHC levels.
    supported_by:
    - reference_id: PMID:38297130
      supporting_text: metabolized by 7-DHC reductase (DHCR7) for cholesterol synthesis
- term:
    id: GO:0160020
    label: positive regulation of ferroptosis
  evidence_type: IMP
  original_reference_id: PMID:38297129
  qualifier: involved_in
  review:
    summary: DHCR7 promotes ferroptosis by consuming its substrate 7-DHC, a potent
      radical-trapping (anti-ferroptotic) sterol; DHCR7 loss raises 7-DHC and confers
      ferroptosis resistance.
    action: KEEP_AS_NON_CORE
    reason: This is a real, experimentally supported (IMP) regulatory consequence of
      DHCR7's enzymatic activity - by depleting the anti-ferroptotic metabolite 7-DHC,
      DHCR7 acts as a pro-ferroptotic factor. It is downstream of, and secondary to,
      the core biosynthetic function, so it is kept as non-core rather than a defining
      function.
    supported_by:
    - reference_id: PMID:38297129
      supporting_text: we identify proferroptotic activity of 7-dehydrocholesterol
        reductase (DHCR7) and an unexpected prosurvival function of its substrate,
        7-dehydrocholesterol (7-DHC)
- term:
    id: GO:0160020
    label: positive regulation of ferroptosis
  evidence_type: IMP
  original_reference_id: PMID:38297130
  qualifier: involved_in
  review:
    summary: Genome-wide CRISPR screening identifies DHCR7 as a pro-ferroptotic gene
      acting by lowering the anti-ferroptotic metabolite 7-DHC.
    action: KEEP_AS_NON_CORE
    reason: Independently supports the pro-ferroptotic regulatory role, which is a
      secondary consequence of DHCR7's core reductase activity. Kept as non-core.
    supported_by:
    - reference_id: PMID:38297130
      supporting_text: DHCR7 functions as a pro-ferroptotic gene
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:32694168
  qualifier: enables
  review:
    summary: DHCR7 physically interacts with the ER/nuclear-envelope transmembrane
      protein TMEM147 (Q9BVK8), whose depletion reduces DHCR7 protein levels and affects
      cholesterol homeostasis.
    action: MARK_AS_OVER_ANNOTATED
    reason: The interaction with TMEM147 is genuine and experimentally documented,
      but the bare 'protein binding' (GO:0005515) term is uninformative about molecular
      function. The specific interaction and its regulatory relevance are recorded
      here rather than captured by this generic term. Per curation policy the IPI is
      not removed.
    supported_by:
    - reference_id: PMID:32694168
      supporting_text: physically interacts with the key sterol reductase DHCR7
- term:
    id: GO:0005515
    label: protein binding
  evidence_type: IPI
  original_reference_id: PMID:25637936
  qualifier: enables
  review:
    summary: DHCR7 physically and functionally interacts with the other terminal cholesterol-synthesis
      reductase DHCR24 (Q15392); the two enzymes co-immunoprecipitate and DHCR24 controls
      DHCR7 activity.
    action: MARK_AS_OVER_ANNOTATED
    reason: The DHCR7-DHCR24 interaction is a well-established, functionally important
      physical interaction (a proposed cholesterol-synthesis metabolon), but 'protein
      binding' is too generic to convey function. The specific interacting partner
      and its regulatory role are documented here. IPI retained per policy.
    supported_by:
    - reference_id: PMID:25637936
      supporting_text: 24-Dehydrocholesterol reductase (DHCR24) and 7-dehydrocholesterol
        reductase (DHCR7) coimmunoprecipitate, and when the DHCR24 gene is knocked
        down by siRNA, DHCR7 activity is also ablated.
- term:
    id: GO:0050661
    label: NADP binding
  evidence_type: ISS
  original_reference_id: GO_REF:0000024
  qualifier: enables
  review:
    summary: DHCR7 binds NADP(H) as the redox cofactor for the reduction of 7-DHC to
      cholesterol.
    action: ACCEPT
    reason: Supported by multiple predicted NADP(+) binding-site residues (UniProt
      BINDING features) and by the NADPH-dependence of the catalysed reaction. Consistent
      with the family cofactor requirement; a correct molecular-function annotation.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The conversion to cholesterol depends on NADPH
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: /ligand="NADP(+)"
- term:
    id: GO:0016020
    label: membrane
  evidence_type: HDA
  original_reference_id: PMID:19946888
  qualifier: located_in
  review:
    summary: DHCR7 identified in a high-throughput membrane proteome of an NK-like
      cell line.
    action: MARK_AS_OVER_ANNOTATED
    reason: A high-throughput proteomic membrane assignment; 'membrane' is correct
      but generic. The specific and experimentally supported ER membrane localization
      is preferred and already annotated.
    supported_by:
    - reference_id: PMID:19946888
      supporting_text: approximately 40% of the identified proteins were predicted
        as plausible membrane proteins
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1655827
  qualifier: located_in
  review:
    summary: ER membrane localization asserted by Reactome.
    action: ACCEPT
    reason: Correct, specific cellular-component localization consistent with experimental
      data. Core cellular component.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-196402
  qualifier: located_in
  review:
    summary: ER membrane localization asserted by Reactome.
    action: ACCEPT
    reason: Correct, specific cellular-component localization consistent with experimental
      data. Core cellular component.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6807055
  qualifier: located_in
  review:
    summary: ER membrane localization asserted by the Reactome reaction 'DHCR7 reduces
      7-dehydroCHOL to CHOL'.
    action: ACCEPT
    reason: Correct, specific cellular-component localization consistent with experimental
      data. Core cellular component.
    supported_by:
    - reference_id: file:human/DHCR7/DHCR7-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IMP
  original_reference_id: PMID:9465114
  qualifier: involved_in
  review:
    summary: Functional expression of the cloned enzyme, and its identification as
      the ultimate cholesterol-biosynthesis enzyme defective in SLOS, support its role
      in cholesterol biosynthesis.
    action: ACCEPT
    reason: Supported by the reconstitution of 7-DHC-to-cholesterol conversion on expression
      of the human cDNA. Core biological process.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: The Delta7-sterol reductase is the ultimate enzyme of cholesterol
        biosynthesis in vertebrates and is absent from yeast.
- term:
    id: GO:0005640
    label: nuclear outer membrane
  evidence_type: IDA
  original_reference_id: PMID:9878250
  qualifier: located_in
  review:
    summary: DHCR7 was localized to the endoplasmic reticulum, contiguous with the
      nuclear outer membrane, in the study characterizing the LBR/sterol-reductase
      gene family.
    action: KEEP_AS_NON_CORE
    reason: The nuclear outer membrane is continuous with the ER membrane, so this
      IDA is plausible and not contradicted, but it is a peripheral aspect of the localization;
      the core compartment is the ER membrane. Retained as non-core. Not removed, as
      it is an experimental (IDA) observation whose full text we have not read.
    supported_by:
    - reference_id: PMID:9878250
      supporting_text: these two related proteins are in the endoplasmic reticulum
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IDA
  original_reference_id: PMID:9878250
  qualifier: located_in
  review:
    summary: Directly localizes DHCR7 to the endoplasmic reticulum in the study characterizing
      the human LBR/sterol-reductase multigene family.
    action: ACCEPT
    reason: Direct experimental (IDA) localization to the ER, consistent with the more
      specific ER membrane annotation. Correct compartment.
    supported_by:
    - reference_id: PMID:9878250
      supporting_text: these two related proteins are in the endoplasmic reticulum
- term:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  evidence_type: IDA
  original_reference_id: PMID:9465114
  qualifier: enables
  review:
    summary: Direct assay of the heterologously expressed human enzyme demonstrating
      NADPH-dependent reduction of the C7-C8 double bond of 7-dehydrocholesterol.
    action: ACCEPT
    reason: Direct experimental (IDA) evidence for the core molecular function.
    supported_by:
    - reference_id: PMID:9465114
      supporting_text: Microsomes from Saccharomyces cerevisiae strains heterologously
        expressing the human cDNA remove the C7-8 double bond in 7-dehydrocholesterol.
core_functions:
- description: NADPH-dependent 7-dehydrocholesterol reductase catalysing the final,
    terminal step of cholesterol biosynthesis - reduction of the C7-C8 double bond
    of 7-dehydrocholesterol to cholesterol - at the endoplasmic reticulum membrane.
  supported_by:
  - reference_id: PMID:9465114
    supporting_text: Microsomes from Saccharomyces cerevisiae strains heterologously
      expressing the human cDNA remove the C7-8 double bond in 7-dehydrocholesterol.
  molecular_function:
    id: GO:0047598
    label: 7-dehydrocholesterol reductase activity
  directly_involved_in:
  - id: GO:0006695
    label: cholesterol biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000024
  title: Manual transfer of experimentally-verified manual GO annotation data to orthologs
    by curator judgment of sequence similarity
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000044
  title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location
    vocabulary mapping, accompanied by conservative changes to GO terms applied by
    UniProt
  findings: []
- id: GO_REF:0000052
  title: Gene Ontology annotation based on curation of immunofluorescence data
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/DHCR7/DHCR7-uniprot.txt
  title: UniProtKB entry Q9UBM7 (DHCR7_HUMAN)
  findings: []
- id: PMID:19946888
  title: Defining the membrane proteome of NK cells.
  findings: []
  reference_review:
    relevance: LOW
    correctness: VERIFIED
    review_notes: High-throughput NK-cell membrane proteome; supports only a generic
      membrane localization, not a specific function of DHCR7.
- id: PMID:20615952
  title: Identification and pharmacological characterization of cholesterol-5,6-epoxide
    hydrolase as a target for tamoxifen and AEBS ligands.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Establishes that DHCR7 with EBP forms the AEBS carrying cholesterol-5,6-epoxide
      hydrolase activity; a genuine secondary (moonlighting) activity, non-core.
- id: PMID:25637936
  title: The terminal enzymes of cholesterol synthesis, DHCR24 and DHCR7, interact
    physically and functionally.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Full-text available; demonstrates DHCR7-DHCR24 physical/functional
      interaction and the cholesterol/vitamin D3 partitioning role of DHCR7.
- id: PMID:32694168
  title: TMEM147 interacts with lamin B receptor, regulates its localization and levels,
    and affects cholesterol homeostasis.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Reports a physical interaction between DHCR7 and TMEM147 affecting
      DHCR7 protein levels and cholesterol homeostasis.
- id: PMID:38297129
  title: 7-Dehydrocholesterol is an endogenous suppressor of ferroptosis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Establishes DHCR7 as pro-ferroptotic via depletion of the anti-ferroptotic
      metabolite 7-DHC; includes active-site mutagenesis confirming reductase activity.
- id: PMID:38297130
  title: 7-Dehydrocholesterol dictates ferroptosis sensitivity.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Full-text available; independent confirmation of DHCR7's pro-ferroptotic
      role and its 7-DHC reductase function in distal cholesterol biosynthesis.
- id: PMID:9465114
  title: Molecular cloning and expression of the human delta7-sterol reductase.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Primary cloning/characterization; directly establishes the NADPH-dependent
      7-DHC reductase (EC 1.3.1.21) core function.
- id: PMID:9878250
  title: The human lamin B receptor/sterol reductase multigene family.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: Establishes DHCR7 as a member of the LBR/sterol-reductase family
      localized to the endoplasmic reticulum.
- id: Reactome:R-HSA-1655827
  title: Expression of 7-Dehydrocholesterol Reductase (DHCR7)
  findings: []
- id: Reactome:R-HSA-196402
  title: Cholesta-5,7,24-trien-3beta-ol is reduced to desmosterol
  findings: []
- id: Reactome:R-HSA-6807047
  title: Cholesterol biosynthesis via desmosterol (Bloch pathway)
  findings: []
- id: Reactome:R-HSA-6807055
  title: DHCR7 reduces 7-dehydroCHOL to CHOL
  findings: []
- id: Reactome:R-HSA-9969901
  title: Cholesterol biosynthesis from zymosterol (modified Kandutsch-Russell pathway)
  findings: []