id: O75845
gene_symbol: SC5D
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: >-
  SC5D encodes lathosterol oxidase (sterol-C5-desaturase / delta7-sterol
  5(6)-desaturase; EC 1.14.19.20), a non-heme di-iron oxidoreductase of the
  sterol desaturase family that is anchored as a multi-pass protein in the
  endoplasmic reticulum membrane. It introduces the C5-6 double bond into
  lathosterol, converting it to 7-dehydrocholesterol (7-DHC) using molecular
  oxygen and electrons delivered from cytochrome b5. This is the penultimate
  step of cholesterol biosynthesis (the Kandutsch-Russell arm), immediately
  upstream of DHCR7, which reduces 7-DHC to cholesterol; the enzyme can act on
  additional Delta(7)-sterols such as 5alpha-cholesta-7,24-dien-3beta-ol in the
  Bloch arm. The three conserved histidine-box motifs coordinate the di-iron
  center that constitutes the active site. Loss-of-function variants cause
  lathosterolosis, an autosomal recessive disorder with elevated lathosterol and
  a Smith-Lemli-Opitz-like multiple-malformation / dysmorphism phenotype with
  liver disease and lysosomal storage; the mouse knockout is perinatal-lethal
  with craniofacial and limb patterning defects consistent with impaired
  hedgehog signalling from cholesterol deficiency. Because its product 7-DHC is
  a highly reactive radical-trapping sterol, SC5D also indirectly modulates
  ferroptosis sensitivity.
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: >-
      Phylogenetic (IBA) inference that SC5D acts in the endoplasmic reticulum
      membrane. This matches the experimentally determined subcellular location
      and the multi-pass membrane topology predicted from the sequence.
    action: ACCEPT
    reason: >-
      SC5D is a sterol desaturase-family enzyme of cholesterol biosynthesis, a
      pathway localized to the ER membrane; the human protein was shown to be an
      integral ER membrane protein experimentally (PMID:10786622).
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
- term:
    id: GO:0050046
    label: delta7-sterol 5(6)-desaturase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetic (IBA) inference of the precise catalytic activity: SC5D
      introduces the C5(6) double bond into Delta(7)-sterols. This is the
      enzyme's core molecular function and is confirmed experimentally.
    action: ACCEPT
    reason: >-
      Directly supported by cloning/complementation and by the UniProt
      CATALYTIC ACTIVITY (RHEA:54320/46556; EC 1.14.19.20). Represents the core
      MF of the gene.
    supported_by:
    - reference_id: PMID:10786622
      supporting_text: "introduce C5-6 double bond into lathosterol in cholesterol biosynthesis"
- term:
    id: GO:0000248
    label: C-5 sterol desaturase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: >-
      Phylogenetic (IBA) inference of C-5 sterol desaturase activity, the
      more general parent of the specific Delta(7)-sterol 5(6)-desaturase
      reaction. Correct family-level molecular function.
    action: ACCEPT
    reason: >-
      Consistent with the sterol desaturase family assignment and experimental
      characterization; a valid, if slightly more general, statement of the
      core catalytic function.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Belongs to the sterol desaturase family"
- term:
    id: GO:0005506
    label: iron ion binding
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: >-
      InterPro2GO inference of iron ion binding. SC5D is a non-heme di-iron
      sterol desaturase whose three conserved histidine-box motifs coordinate
      the catalytic iron center; UniProt lists an Fe cation cofactor.
    action: ACCEPT
    reason: >-
      Well-supported for this enzyme family: the His-box motifs (138-143,
      151-155, 228-233) form the metal-binding active site and the cofactor is
      an Fe cation, so iron ion binding is an accurate molecular function.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Name=Fe cation"
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "The histidine box domains may contain the active site"
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: located_in
  review:
    summary: >-
      Electronic (UniProt/rat-ortholog) transfer of ER membrane localization.
      Redundant with the experimental IDA and IBA ER-membrane annotations and
      consistent with the multi-pass membrane topology.
    action: ACCEPT
    reason: >-
      Correct localization, independently supported by the human IDA
      (PMID:10786622) and by the predicted transmembrane helices.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
- term:
    id: GO:0008610
    label: lipid biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: >-
      InterPro2GO inference of the broad process "lipid biosynthetic process".
      SC5D acts in cholesterol (a sterol lipid) biosynthesis, so this is correct
      but general relative to the specific cholesterol/sterol biosynthesis
      terms also annotated.
    action: ACCEPT
    reason: >-
      Not wrong: cholesterol biosynthesis is-a lipid biosynthetic process. It is
      a broad parent, but per curation guidance broad correct IEA parents can be
      accepted; the more specific term (GO:0006695) captures the core process.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Steroid biosynthesis; cholesterol biosynthesis"
- term:
    id: GO:0050046
    label: delta7-sterol 5(6)-desaturase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: >-
      Electronic (UniProt, via rat ortholog and RHEA/EC mapping) transfer of the
      precise Delta(7)-sterol 5(6)-desaturase activity. Redundant with the IBA
      and IDA/EXP annotations of the same activity.
    action: ACCEPT
    reason: >-
      Correct core catalytic function backed by the RHEA reactions and EC
      1.14.19.20 in the UniProt record.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "EC=1.14.19.20"
- term:
    id: GO:0000248
    label: C-5 sterol desaturase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: enables
  review:
    summary: >-
      Ensembl-Compara ortholog transfer (from rat) of C-5 sterol desaturase
      activity. Consistent with the experimental and phylogenetic annotations of
      the same family-level function.
    action: ACCEPT
    reason: >-
      Accurate family-level molecular function; redundant with the IBA/EXP
      annotations of GO:0000248.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Belongs to the sterol desaturase family"
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: involved_in
  review:
    summary: >-
      Electronic (UniProt/UniPathway) transfer of cholesterol biosynthetic
      process. SC5D catalyzes the penultimate step of cholesterol biosynthesis,
      so this is the correct core biological process.
    action: ACCEPT
    reason: >-
      Directly matches the enzyme's role and the UniProt PATHWAY statement;
      independently supported by human IDA and disease evidence.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Steroid biosynthesis; cholesterol biosynthesis"
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6807047
  qualifier: involved_in
  review:
    summary: >-
      Reactome (TAS) placement of SC5D in cholesterol biosynthesis via the
      desmosterol/Bloch pathway. Correct: SC5D also desaturates the Bloch-arm
      intermediate 5alpha-cholesta-7,24-dien-3beta-ol.
    action: ACCEPT
    reason: >-
      SC5D participates in both the Bloch and Kandutsch-Russell arms; its
      Delta(7)-sterol 5(6)-desaturase activity applies to the corresponding
      Bloch intermediate. Core biological process.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Steroid biosynthesis; cholesterol biosynthesis"
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9969901
  qualifier: involved_in
  review:
    summary: >-
      Reactome (TAS) placement of SC5D in cholesterol biosynthesis from
      zymosterol (modified Kandutsch-Russell pathway), the lathosterol arm in
      which SC5D acts. Correct core biological process.
    action: ACCEPT
    reason: >-
      This is the canonical arm containing the SC5D-catalyzed lathosterol ->
      7-dehydrocholesterol step; well supported.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Catalyzes the penultimate step"
- term:
    id: GO:0050046
    label: delta7-sterol 5(6)-desaturase activity
  evidence_type: EXP
  original_reference_id: PMID:38297129
  qualifier: enables
  review:
    summary: >-
      Experimental (EXP) annotation of Delta(7)-sterol 5(6)-desaturase activity
      from the Nature ferroptosis study, which characterized SC5D FUNCTION and
      CATALYTIC ACTIVITY as the enzyme producing 7-DHC. Confirms the core
      catalytic function.
    action: ACCEPT
    reason: >-
      Experimental support for the precise reaction; underpins the UniProt
      CATALYTIC ACTIVITY entries. Core molecular function.
    supported_by:
    - reference_id: PMID:38297129
      supporting_text: "an unexpected prosurvival"
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Catalyzes the penultimate step"
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IDA
  original_reference_id: PMID:10786622
  qualifier: is_active_in
  review:
    summary: >-
      Experimental (IDA) determination that SC5D is an integral endoplasmic
      reticulum membrane protein, from the cloning study that also demonstrated
      the enzymatic activity by yeast-mutant complementation.
    action: ACCEPT
    reason: >-
      Primary experimental evidence for the ER-membrane location; the core
      cellular component for this enzyme.
    supported_by:
    - reference_id: PMID:10786622
      supporting_text: "Mammalian SC5D was presumed as an integral"
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
- term:
    id: GO:0006695
    label: cholesterol biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:10786622
  qualifier: involved_in
  review:
    summary: >-
      Experimental (IDA) annotation to cholesterol biosynthetic process from the
      cloning/complementation study, which functionally showed SC5D introduces
      the C5-6 double bond into lathosterol in cholesterol biosynthesis. This is
      the correct core biological process.
    action: ACCEPT
    reason: >-
      Direct experimental support for SC5D's role in cholesterol biosynthesis.
      A more specific child term (GO:0033490, cholesterol biosynthetic process
      via lathosterol) is proposed separately as a NEW annotation to capture the
      precise lathosterol arm.
    supported_by:
    - reference_id: PMID:10786622
      supporting_text: "introduce C5-6 double bond into lathosterol in cholesterol biosynthesis"
- term:
    id: GO:0033490
    label: cholesterol biosynthetic process via lathosterol
  evidence_type: IDA
  original_reference_id: PMID:10786622
  qualifier: involved_in
  review:
    summary: >-
      Proposed more specific annotation: SC5D acts in the lathosterol arm of
      cholesterol biosynthesis, catalyzing lathosterol -> 7-dehydrocholesterol.
      UniProt assigns this precise child term (GO:0033490, IDA:UniProtKB); it is
      not yet in GOA and is added here as a NEW, more informative annotation.
    action: NEW
    reason: >-
      Sharper than the generic GO:0006695: the lathosterol-specific arm is the
      exact pathway context of the SC5D reaction, matching the UniProt IDA
      annotation.
    supported_by:
    - reference_id: PMID:10786622
      supporting_text: "introduce C5-6 double bond into lathosterol in cholesterol biosynthesis"
- term:
    id: GO:0050046
    label: delta7-sterol 5(6)-desaturase activity
  evidence_type: IDA
  original_reference_id: PMID:10786622
  qualifier: enables
  review:
    summary: >-
      Experimental (IDA) annotation of Delta(7)-sterol 5(6)-desaturase activity.
      The human cDNA functionally complemented a sterol-C5-desaturase-defective
      yeast mutant, directly demonstrating the catalytic activity.
    action: ACCEPT
    reason: >-
      Direct experimental demonstration of the core catalytic function via
      yeast complementation.
    supported_by:
    - reference_id: PMID:10786622
      supporting_text: "functional complementation of a defective yeast mutant proves that the human and"
- term:
    id: GO:0110076
    label: negative regulation of ferroptosis
  evidence_type: IMP
  original_reference_id: PMID:38297129
  qualifier: involved_in
  review:
    summary: >-
      Loss-of-function (IMP) evidence that SC5D negatively regulates ferroptosis.
      As a distal-cholesterol-biosynthesis enzyme, SC5D produces 7-DHC, a potent
      radical-trapping sterol that shields (phospho)lipids from autoxidation;
      loss of SC5D lowers 7-DHC and sensitizes cells to ferroptosis. This is a
      real but indirect, non-core role mediated by the 7-DHC product.
    action: KEEP_AS_NON_CORE
    reason: >-
      Supported experimentally, but the effect is a downstream/indirect
      consequence of SC5D's catalytic product (7-DHC) rather than a distinct
      molecular activity of SC5D itself; the core function is C5-sterol
      desaturation in cholesterol biosynthesis. Keep as a non-core process.
    supported_by:
    - reference_id: PMID:38297129
      supporting_text: "we now show that 7-DHC accumulation"
- term:
    id: GO:0110076
    label: negative regulation of ferroptosis
  evidence_type: IMP
  original_reference_id: PMID:38297130
  qualifier: involved_in
  review:
    summary: >-
      Loss-of-function (IMP) evidence from a genome-wide CRISPR screen: SC5D is
      an anti-ferroptotic distal-cholesterol-biosynthesis gene. SC5D knockout
      increased ferroptosis susceptibility and lowered 7-DHC, and re-expression
      rescued the phenotype. Indirect, non-core role via the 7-DHC product.
    action: KEEP_AS_NON_CORE
    reason: >-
      Well supported experimentally in this full-text study, but mechanistically
      the protection is conferred by the SC5D reaction product 7-DHC, not by an
      independent SC5D activity; keep as a non-core biological process.
    supported_by:
    - reference_id: PMID:38297130
      supporting_text: "individual deletion of CYP51A1, MSMO1, EBP and SC5D in HEK293T cells increased the susceptibility to ferroptosis"
    - reference_id: PMID:38297130
      supporting_text: "Re-expression of SC5D reversed the severity of ferroptosis induced by RSL3 in SC5D KO cells"
- term:
    id: GO:0000248
    label: C-5 sterol desaturase activity
  evidence_type: EXP
  original_reference_id: PMID:12189593
  qualifier: enables
  review:
    summary: >-
      Experimental (EXP) annotation of C-5 sterol desaturase activity based on
      the first human lathosterolosis patient, in whom the SC5D-catalyzed
      conversion of lathosterol to 7-dehydrocholesterol was blocked and the
      enzyme activity was deficient. Supports the core catalytic function.
    action: ACCEPT
    reason: >-
      Human patient data directly link SC5D to C-5 sterol desaturase activity
      (loss of activity blocks lathosterol -> 7-DHC). Core molecular function.
    supported_by:
    - reference_id: PMID:12189593
      supporting_text: "showing a block in the conversion of lathosterol into"
    - reference_id: PMID:12189593
      supporting_text: "was deficient in the patient's"
- term:
    id: GO:0000248
    label: C-5 sterol desaturase activity
  evidence_type: EXP
  original_reference_id: PMID:12812989
  qualifier: enables
  review:
    summary: >-
      Experimental (EXP) annotation of C-5 sterol desaturase activity supported
      by the human patient and Sc5d-null mouse study, which established that
      lathosterol 5-desaturase catalyzes the conversion of lathosterol to
      7-dehydrocholesterol in the next-to-last step of cholesterol synthesis.
    action: ACCEPT
    reason: >-
      Combined human and mouse loss-of-function evidence for the core catalytic
      function; elevated lathosterol and decreased cholesterol on enzyme loss.
    supported_by:
    - reference_id: PMID:12812989
      supporting_text: "catalyzes the conversion of lathosterol to"
    - reference_id: PMID:12812989
      supporting_text: "had elevated lathosterol and decreased cholesterol"
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-1655852
  qualifier: located_in
  review:
    summary: >-
      Reactome (TAS) ER-membrane localization associated with expression of
      lathosterol oxidase (SC5D). Consistent with the experimental IDA and the
      multi-pass membrane topology.
    action: ACCEPT
    reason: >-
      Redundant with the experimentally determined ER membrane location; correct
      core cellular component.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-195664
  qualifier: located_in
  review:
    summary: >-
      Reactome (TAS) ER-membrane localization for the SC5D-catalyzed desaturation
      of cholesta-7,24-dien-3beta-ol (a Bloch-arm reaction). Consistent with the
      established ER location.
    action: ACCEPT
    reason: >-
      Correct core cellular component; the reaction it is attached to takes place
      in the ER, as noted by Reactome, and matches the human IDA.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-6807053
  qualifier: located_in
  review:
    summary: >-
      Reactome (TAS) ER-membrane localization for the SC5D reaction that
      desaturates lathosterol to 7-dehydrocholesterol. Consistent with the
      experimental and predicted ER-membrane location.
    action: ACCEPT
    reason: >-
      Correct core cellular component; matches human IDA and topology.
    supported_by:
    - reference_id: file:human/SC5D/SC5D-uniprot.txt
      supporting_text: "Endoplasmic reticulum membrane"
core_functions:
- description: >-
    Lathosterol oxidase / Delta(7)-sterol C5(6)-desaturase that introduces the
    C5-6 double bond into lathosterol to form 7-dehydrocholesterol, the
    penultimate step of cholesterol biosynthesis, acting in the endoplasmic
    reticulum membrane.
  molecular_function:
    id: GO:0050046
    label: delta7-sterol 5(6)-desaturase activity
  directly_involved_in:
  - id: GO:0006695
    label: cholesterol biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:10786622
    supporting_text: "introduce C5-6 double bond into lathosterol in cholesterol biosynthesis"
  - reference_id: file:human/SC5D/SC5D-uniprot.txt
    supporting_text: "Catalyzes the penultimate step"
- description: >-
    C-5 sterol desaturase activity: family-level oxidoreductase function that
    installs the Delta(5) double bond of sterols, dependent on a non-heme di-iron
    center coordinated by conserved histidine-box motifs, driving the lathosterol
    arm of cholesterol biosynthesis.
  molecular_function:
    id: GO:0000248
    label: C-5 sterol desaturase activity
  directly_involved_in:
  - id: GO:0033490
    label: cholesterol biosynthetic process via lathosterol
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:12812989
    supporting_text: "catalyzes the conversion of lathosterol to"
  - reference_id: file:human/SC5D/SC5D-uniprot.txt
    supporting_text: "Belongs to the sterol desaturase family"
proposed_new_terms: []
suggested_questions:
- question: >-
    Is SC5D's role in modulating ferroptosis (via 7-DHC) physiologically
    relevant in normal tissues, or primarily a cancer-context phenomenon?
- question: >-
    To what extent does SC5D contribute to the Bloch versus Kandutsch-Russell
    arms of cholesterol biosynthesis in different human tissues?
suggested_experiments:
- description: >-
    Reconstitute purified human SC5D with cytochrome b5 / cytochrome b5 reductase
    to measure the di-iron-dependent desaturation kinetics on lathosterol versus
    5alpha-cholesta-7,24-dien-3beta-ol and confirm cofactor stoichiometry.
  hypothesis: >-
    SC5D is a non-heme di-iron desaturase that uses electrons from cytochrome b5
    to desaturate multiple Delta(7)-sterol substrates.
- description: >-
    Site-directed mutagenesis of the three histidine-box motifs to test their
    requirement for iron binding and catalysis, complementing the disease-variant
    (R29Q, Y46S, G211D) structure-function analysis.
  hypothesis: >-
    The conserved histidine-box motifs coordinate the catalytic di-iron center
    and are essential for C5-sterol desaturase activity.
references:
- id: GO_REF:0000002
  title: Gene Ontology annotation through association of InterPro records with GO
    terms
  findings: []
- id: GO_REF:0000033
  title: Annotation inferences using phylogenetic trees
  findings: []
- id: GO_REF:0000107
  title: Automatic transfer of experimentally verified manual GO annotation data to
    orthologs using Ensembl Compara
  findings: []
- id: GO_REF:0000120
  title: Combined Automated Annotation using Multiple IEA Methods
  findings: []
- id: file:human/SC5D/SC5D-uniprot.txt
  title: UniProtKB entry O75845 (SC5D_HUMAN), Lathosterol oxidase
  findings: []
- id: PMID:10786622
  title: cDNA cloning of the mammalian sterol C5-desaturase and the expression in
    yeast mutant.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Cloning and yeast-complementation study establishing SC5D catalytic
      activity and ER-membrane localization; source of the UniProt RecName, EC
      number, and subcellular location. Abstract-only in cache but claims
      confirmed against the UniProt record.
- id: PMID:12189593
  title: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome
    due to deficiency of 3beta-hydroxysteroid-delta5-desaturase.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      First human lathosterolosis patient (R29Q, G211D); documents block in
      lathosterol to 7-DHC conversion and deficient SC5D activity.
- id: PMID:12812989
  title: 'Lathosterolosis: an inborn error of human and murine cholesterol synthesis
    due to lathosterol 5-desaturase deficiency.'
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: >-
      Sc5d-null mouse and human Y46S patient; states SC5D catalyzes the
      next-to-last step of cholesterol synthesis; elevated lathosterol / reduced
      cholesterol on loss.
- id: PMID:38297129
  title: 7-Dehydrocholesterol is an endogenous suppressor of ferroptosis.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Nature study characterizing SC5D function/catalytic activity/pathway and
      the anti-ferroptotic role of its product 7-DHC. Abstract-only in cache; the
      ferroptosis role is indirect (via 7-DHC), hence treated as non-core.
- id: PMID:38297130
  title: 7-Dehydrocholesterol dictates ferroptosis sensitivity.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: >-
      Full text available; genome-wide CRISPR screen shows SC5D is an
      anti-ferroptotic distal-cholesterol-biosynthesis gene whose product 7-DHC
      suppresses ferroptosis. Supports GO:0110076 as a non-core role.
- id: Reactome:R-HSA-1655852
  title: Expression of Lathosterol Oxidase (SC5D, SC5DL)
  findings: []
- id: Reactome:R-HSA-195664
  title: Cholesta-7,24-dien-3beta-ol is desaturated to form cholesta-5,7,24-trien-3beta-ol
  findings: []
- id: Reactome:R-HSA-6807047
  title: Cholesterol biosynthesis via desmosterol (Bloch pathway)
  findings: []
- id: Reactome:R-HSA-6807053
  title: SC5D desaturates LTHSOL to 7-dehydroCHOL
  findings: []
- id: Reactome:R-HSA-9969901
  title: Cholesterol biosynthesis from zymosterol (modified Kandutsch-Russell pathway)
  findings: []