id: Q9H8P0
gene_symbol: SRD5A3
product_type: PROTEIN
status: INITIALIZED
taxon:
  id: NCBITaxon:9606
  label: Homo sapiens
description: SRD5A3 is an endoplasmic reticulum membrane, NADPH-dependent polyprenal
  reductase that acts in the terminal steps of de novo dolichol biosynthesis. In the
  currently accepted pathway it catalyzes the reduction of the alpha-isoprene unit
  of a di-trans,poly-cis-polyprenal to the corresponding dolichal, an intermediate
  in converting polyprenol to dolichol; the resulting dolichol is phosphorylated to
  dolichol-phosphate, the essential lipid carrier used to assemble the lipid-linked
  oligosaccharide precursor for protein N-linked glycosylation. It is a multi-pass
  member of the steroid 5-alpha-reductase family (polyprenal reductase subfamily;
  yeast ortholog DFG10). Loss-of-function mutations cause SRD5A3-congenital disorder
  of glycosylation (SRD5A3-CDG, CDG type Iq) and Kahrizi syndrome, characterized by
  ocular coloboma, cerebellar vermis hypoplasia, and intellectual disability. Despite
  its name, SRD5A3 is not a physiological steroid 5-alpha-reductase; a weak in-vitro
  testosterone-to-dihydrotestosterone activity was reported at its discovery in prostate
  cancer, but its established physiological role is in dolichol synthesis and glycosylation,
  not steroid metabolism.
existing_annotations:
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: is_active_in
  review:
    summary: Phylogenetically inferred ER localization, consistent with the experimentally
      determined localization of SRD5A3 (an ER-membrane dolichol-pathway enzyme).
    action: ACCEPT
    reason: SRD5A3 acts in the ER membrane where dolichol biosynthesis and lipid-linked
      oligosaccharide assembly occur; this is directly supported experimentally.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetically inferred involvement in dolichol-linked oligosaccharide
      (LLO) biosynthesis. SRD5A3 supplies dolichol/dolichol-phosphate, the lipid carrier
      on which the LLO precursor is built, so this pathway-level BP is appropriate,
      though not the most specific reaction SRD5A3 catalyzes.
    action: ACCEPT
    reason: SRD5A3 is required for LLO synthesis; loss of SRD5A3 severely reduces newly
      synthesized LLO and can be rescued by exogenous dolichol-phosphate, placing it
      upstream of LLO assembly.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene
        unit of polyprenols to form dolichols, required for synthesis of dolichol-linked
        monosaccharides, and the oligosaccharide precursor used for N-glycosylation
- term:
    id: GO:0160198
    label: polyprenal reductase activity
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: enables
  review:
    summary: Phylogenetically inferred polyprenal reductase activity, the current core
      molecular function of SRD5A3. This is the term carried by GOA (polyprenAL reductase
      activity, GO:0160198), matching the revised pathway in which SRD5A3 reduces polyprenal
      to dolichal rather than polyprenol directly to dolichol.
    action: ACCEPT
    reason: Represents the core molecular function at the correct current level of
      specificity; consistent with the IDA/EXP experimental annotations and UniProt
      EC 1.3.1.94.
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: SRD5A3 catalyzes only the second reaction
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IBA
  original_reference_id: GO_REF:0000033
  qualifier: involved_in
  review:
    summary: Phylogenetically inferred involvement in dolichyl monophosphate biosynthesis,
      the current core biological process for SRD5A3. GO:0019408 (dolichol biosynthetic
      process) was obsoleted in favor of GO:0043048, so this is the correct current
      BP for the polyprenol-to-dolichol/dolichol-phosphate route.
    action: ACCEPT
    reason: SRD5A3 catalyzes a committed reductive step supplying dolichol for dolichol-phosphate
      synthesis; supported by strong IDA evidence in human cells.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene
        unit of polyprenols to form dolichols
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IEA
  original_reference_id: GO_REF:0000044
  qualifier: located_in
  review:
    summary: Electronic mapping from the UniProt subcellular-location keyword. SRD5A3
      is a multi-pass ER membrane protein, so this is correct and represents the core
      localization.
    action: ACCEPT
    reason: Consistent with experimental ER localization and the multi-pass membrane
      topology annotated in UniProt.
    supported_by:
    - reference_id: file:human/SRD5A3/SRD5A3-uniprot.txt
      supporting_text: 'SUBCELLULAR LOCATION: Endoplasmic reticulum membrane'
    - reference_id: file:human/SRD5A3/SRD5A3-uniprot.txt
      supporting_text: Multi-pass membrane protein
- term:
    id: GO:0006629
    label: lipid metabolic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: Broad InterPro-to-GO mapping. Correct in that SRD5A3 acts in polyisoprenoid
      lipid (dolichol) metabolism, but far too general to convey its function.
    action: KEEP_AS_NON_CORE
    reason: Not wrong but uninformative; the specific dolichyl monophosphate biosynthetic
      process (GO:0043048) already captures the lipid-metabolic role more precisely.
    supported_by:
    - reference_id: file:human/SRD5A3/SRD5A3-uniprot.txt
      supporting_text: 'PATHWAY: Protein modification; protein glycosylation'
- term:
    id: GO:0016627
    label: oxidoreductase activity, acting on the CH-CH group of donors
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: enables
  review:
    summary: InterPro-to-GO mapping to a high-level oxidoreductase class. SRD5A3 is
      an NADPH-dependent reductase that reduces a C=C double bond (the alpha-isoprene
      unit), so this parent term is correct but general.
    action: KEEP_AS_NON_CORE
    reason: Accurate but non-specific; the specific polyprenal reductase activity (GO:0160198)
      is the informative core MF.
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: as a NADPH-dependent reductase in two non-consecutive steps
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000002
  qualifier: involved_in
  review:
    summary: InterPro-to-GO mapping (IPR039698, Dfg10/SRD5A3) to dolichyl monophosphate
      biosynthesis. This matches the experimentally supported core BP.
    action: ACCEPT
    reason: Correct BP for the SRD5A3/Dfg10 family; duplicates the IDA/IBA annotations
      to the same term.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: required for synthesis of dolichol-linked monosaccharides, and
        the oligosaccharide precursor used for N-glycosylation
- term:
    id: GO:0047751
    label: 3-oxo-5-alpha-steroid 4-dehydrogenase (NADP+) activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Electronic annotation derived from the EC 1.3.1.22 (steroid) mapping via
      RHEA/EC (GO_REF:0000120). SRD5A3 is not a physiological steroid 5-alpha-reductase;
      its established function is polyprenal reduction in dolichol synthesis. The steroid
      EC was assigned on the basis of the gene name and weak in-vitro activity, and
      this purely electronic EC-mapping is a wrong inference of the enzyme's biological
      function.
    action: REMOVE
    reason: Demonstrably wrong electronic EC/RHEA-to-GO inference. Physiological substrate
      is polyprenal, not a steroid; null patients have a congenital disorder of glycosylation,
      not a steroid/androgen phenotype, and phylogeny argues the ancestral substrate
      was not a steroid. Per policy, wrong IEA EC-mappings are appropriate REMOVE targets.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: suggesting that the substrate of the enzyme encoded by the common
        ancestral gene was potentially not a steroid
- term:
    id: GO:0160198
    label: polyprenal reductase activity
  evidence_type: IEA
  original_reference_id: GO_REF:0000120
  qualifier: enables
  review:
    summary: Electronic annotation from EC 1.3.1.94 (RHEA:80727) mapping. This is the
      correct core molecular function, matching the experimental annotations and UniProt
      RecName (Polyprenal reductase).
    action: ACCEPT
    reason: Correct EC-based mapping to the physiological reaction; corroborates the
      IDA/EXP/IBA annotations to GO:0160198.
    supported_by:
    - reference_id: file:human/SRD5A3/SRD5A3-uniprot.txt
      supporting_text: EC=1.3.1.94
- term:
    id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  evidence_type: IEA
  original_reference_id: GO_REF:0000107
  qualifier: involved_in
  review:
    summary: Orthology-based transfer (Ensembl Compara) from mouse Srd5a3 of the LLO
      biosynthesis BP. Consistent with the human experimental data and the IBA annotation
      to the same term.
    action: ACCEPT
    reason: Correct pathway-level BP inferred from a well-supported ortholog; duplicates
      the IBA annotation.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: the oligosaccharide precursor used for N-glycosylation
- term:
    id: GO:0006702
    label: androgen biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-193048
  qualifier: involved_in
  review:
    summary: Reactome-derived annotation placing SRD5A3 in androgen biosynthesis, based
      on the prostate-cancer report that SRD5A3 can convert testosterone to dihydrotestosterone
      in vitro (Uemura et al. 2008). SRD5A3 is named a steroid 5-alpha-reductase and
      shows weak in-vitro DHT-forming activity, but its physiological function is dolichol
      synthesis, not androgen metabolism; this is an over-annotation of a marginal
      side activity.
    action: MARK_AS_OVER_ANNOTATED
    reason: The steroid/androgen activity is weak, in-vitro, and derives from the gene
      name and the context of its discovery in hormone-refractory prostate cancer;
      loss-of-function causes a glycosylation disorder, not an androgen-deficiency phenotype.
      Retained (experimental basis, TAS) but flagged as over-annotation rather than
      removed.
    supported_by:
    - reference_id: PMID:17986282
      supporting_text: validated its ability to produce DHT from testosterone, similar
        to type
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-446199
  qualifier: involved_in
  review:
    summary: Reactome-authored annotation (Synthesis of dolichyl-phosphate) to the
      core dolichyl monophosphate biosynthetic process. Consistent with the experimental
      and IBA annotations.
    action: ACCEPT
    reason: Correct core BP; duplicates the IDA/IBA/IEA annotations to GO:0043048.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene
        unit of polyprenols to form dolichols
- term:
    id: GO:0003865
    label: 3-oxo-5-alpha-steroid 4-dehydrogenase activity
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9705714
  qualifier: enables
  review:
    summary: Reactome-derived steroid 5-alpha-reductase MF annotation (SRD5A3 dehydrogenates
      TEST to DHTEST), tracing to the in-vitro testosterone-to-DHT activity of Uemura
      et al. 2008. This is a weak, non-physiological side activity and an over-annotation
      relative to the enzyme's dolichol-pathway function.
    action: MARK_AS_OVER_ANNOTATED
    reason: Steroid 5-alpha-reductase activity is in-vitro and marginal; SRD5A3 is
      physiologically a polyprenal reductase. Retained (TAS/experimental origin) but
      flagged as over-annotation, not removed.
    supported_by:
    - reference_id: PMID:17986282
      supporting_text: validated its ability to produce DHT from testosterone, similar
        to type
- term:
    id: GO:0160198
    label: polyprenal reductase activity
  evidence_type: EXP
  original_reference_id: PMID:38821050
  qualifier: enables
  review:
    summary: Experimental demonstration (Wilson et al. 2024) that SRD5A3 is the NADPH-dependent
      polyprenal reductase catalyzing the second step of the revised dolichol-biosynthesis
      pathway (polyprenal to dolichal). This is the core molecular function.
    action: ACCEPT
    reason: Direct experimental evidence for the precise current MF term (GO:0160198).
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: SRD5A3 catalyzes only the second reaction
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:20637498
  qualifier: involved_in
  review:
    summary: Direct experimental evidence (Cantagrel et al. 2010) that SRD5A3 is required
      for converting polyprenol to dolichol, supplying dolichol-phosphate for glycosylation;
      SRD5A3-deficient cells show reduced dolichol-phosphate-dependent LLO synthesis
      rescuable by exogenous Dol-P. Core BP.
    action: ACCEPT
    reason: Strong IDA evidence for the core dolichyl monophosphate biosynthetic process
      (note GO:0019408 dolichol biosynthetic process was obsoleted into GO:0043048).
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene
        unit of polyprenols to form dolichols
- term:
    id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  evidence_type: IDA
  original_reference_id: PMID:38821050
  qualifier: involved_in
  review:
    summary: Direct experimental evidence (Wilson et al. 2024) that SRD5A3 acts in
      dolichol biosynthesis, catalyzing the NADPH-dependent polyprenal-to-dolichal
      step feeding dolichol/dolichol-phosphate production. Core BP.
    action: ACCEPT
    reason: Strong IDA evidence for the core dolichyl monophosphate biosynthetic process
      in the revised pathway.
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: SRD5A3 catalyzes only the second reaction
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: IDA
  original_reference_id: PMID:20637498
  qualifier: is_active_in
  review:
    summary: Direct experimental evidence that epitope-tagged SRD5A3 localizes predominantly
      to the ER, where dolichol synthesis and LLO assembly occur. Core localization.
    action: ACCEPT
    reason: Experimentally supported active-in ER membrane localization for a multi-pass
      membrane enzyme.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0160198
    label: polyprenal reductase activity
  evidence_type: IDA
  original_reference_id: PMID:38821050
  qualifier: enables
  review:
    summary: Direct experimental evidence (Wilson et al. 2024) for SRD5A3 polyprenal
      reductase activity, the core molecular function. Duplicates the EXP annotation
      to the same term.
    action: ACCEPT
    reason: Direct experimental support for the precise current MF.
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: as a NADPH-dependent reductase in two non-consecutive steps
- term:
    id: GO:0047751
    label: 3-oxo-5-alpha-steroid 4-dehydrogenase (NADP+) activity
  evidence_type: IDA
  original_reference_id: PMID:17986282
  qualifier: enables
  review:
    summary: Experimental annotation from the discovery paper (Uemura et al. 2008),
      which showed in-vitro conversion of testosterone to dihydrotestosterone by SRD5A3
      overexpressed in prostate-cancer cells. This established the "steroid 5-alpha-reductase
      3" naming but reflects a weak, non-physiological side activity; SRD5A3's physiological
      role is polyprenal reduction in dolichol synthesis.
    action: MARK_AS_OVER_ANNOTATED
    reason: Experimental (IDA), so retained rather than removed, but flagged as an
      over-annotation. The 5-alpha-steroid reductase activity is in-vitro and marginal,
      and does not represent the enzyme's physiological function (null mutations cause
      a glycosylation disorder, not androgen deficiency).
    supported_by:
    - reference_id: PMID:17986282
      supporting_text: validated its ability to produce DHT from testosterone, similar
        to type
    - reference_id: PMID:17986282
      supporting_text: resulted in a significant decrease in DHT production and a drastic
        reduction in cell
- term:
    id: GO:0016628
    label: oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP
      as acceptor
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4755572
  qualifier: enables
  review:
    summary: Reactome-derived high-level oxidoreductase MF annotation. Correct as a
      parent class of the polyprenal reductase reaction (NADPH-dependent reduction
      of a C=C bond) but general.
    action: KEEP_AS_NON_CORE
    reason: Accurate parent term; the specific polyprenal reductase activity (GO:0160198)
      is the informative core MF.
    supported_by:
    - reference_id: PMID:38821050
      supporting_text: as a NADPH-dependent reductase in two non-consecutive steps
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-4755572
  qualifier: located_in
  review:
    summary: Reactome-authored ER membrane localization, consistent with the experimental
      IDA localization. Core localization.
    action: ACCEPT
    reason: Correct localization for this multi-pass ER membrane enzyme; duplicates
      the IDA/IEA ER-membrane annotations.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9705714
  qualifier: located_in
  review:
    summary: Reactome-authored ER membrane localization (from the steroid-reaction
      module), consistent with experimental data. Core localization.
    action: ACCEPT
    reason: Correct ER membrane localization; duplicates other ER-membrane annotations.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0005789
    label: endoplasmic reticulum membrane
  evidence_type: TAS
  original_reference_id: Reactome:R-HSA-9937295
  qualifier: located_in
  review:
    summary: Reactome-authored ER membrane localization (from the revised polyprenal-to-dolichal
      reaction module), consistent with experimental data. Core localization.
    action: ACCEPT
    reason: Correct ER membrane localization; duplicates other ER-membrane annotations.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0005783
    label: endoplasmic reticulum
  evidence_type: IDA
  original_reference_id: PMID:20637498
  qualifier: located_in
  review:
    summary: Direct experimental evidence that epitope-tagged SRD5A3 localizes predominantly
      to the ER. Correct, though the more specific ER membrane term (GO:0005789) better
      captures its location as a multi-pass membrane protein.
    action: ACCEPT
    reason: Experimentally supported ER localization; the coexisting ER-membrane annotations
      provide the more specific compartment.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: Epitope tagged SRD5A3 localized predominantly to the ER
- term:
    id: GO:0016628
    label: oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP
      as acceptor
  evidence_type: IDA
  original_reference_id: PMID:20637498
  qualifier: enables
  review:
    summary: Experimental annotation to a high-level NADP-dependent CH-CH oxidoreductase
      class, based on the demonstration that SRD5A3 reduces the alpha-isoprene C=C
      bond of polyprenol to form dolichol. Correct but general.
    action: KEEP_AS_NON_CORE
    reason: Accurate parent term for the reductase activity; the specific polyprenal
      reductase activity (GO:0160198) is the informative core MF.
    supported_by:
    - reference_id: PMID:20637498
      supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene
        unit of polyprenols to form dolichols
core_functions:
- description: NADPH-dependent polyprenal reductase acting in the terminal steps of
    de novo dolichol biosynthesis, reducing the alpha-isoprene unit of di-trans,poly-cis-polyprenal
    to the corresponding dolichal en route to dolichol
  molecular_function:
    id: GO:0160198
    label: polyprenal reductase activity
  directly_involved_in:
  - id: GO:0043048
    label: dolichyl monophosphate biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:38821050
    supporting_text: SRD5A3 catalyzes only the second reaction
  - reference_id: PMID:20637498
    supporting_text: SRD5A3 is necessary for the reduction of the alpha-isoprene unit
      of polyprenols to form dolichols
- description: Supplies dolichol/dolichol-phosphate, the lipid carrier used to build
    the lipid-linked oligosaccharide precursor, thereby enabling protein N-linked glycosylation
  molecular_function:
    id: GO:0160198
    label: polyprenal reductase activity
  directly_involved_in:
  - id: GO:0006488
    label: dolichol-linked oligosaccharide biosynthetic process
  locations:
  - id: GO:0005789
    label: endoplasmic reticulum membrane
  supported_by:
  - reference_id: PMID:20637498
    supporting_text: required for synthesis of dolichol-linked monosaccharides, and
      the oligosaccharide precursor used for N-glycosylation
proposed_new_terms: []
suggested_questions:
- question: Given the revised pathway (Wilson et al. 2024), is the physiological substrate
    of SRD5A3 strictly polyprenal, and does it have any residual direct polyprenol-reducing
    activity in vivo?
- question: Is the in-vitro testosterone-to-dihydrotestosterone activity of SRD5A3
    physiologically relevant in any tissue (e.g. prostate cancer), or purely an artifact
    of overexpression?
suggested_experiments:
- description: Structural/biochemical characterization of SRD5A3 with polyprenal versus
    steroid substrates to quantify catalytic efficiency and confirm the physiological
    substrate.
- description: Tissue-specific conditional knockouts to test whether any androgen/steroid
    phenotype arises independently of the glycosylation defect.
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: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: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: PMID:17986282
  title: Novel 5 alpha-steroid reductase (SRD5A3, type-3) is overexpressed in hormone-refractory
    prostate cancer.
  findings: []
  reference_review:
    relevance: MEDIUM
    correctness: VERIFIED
    review_notes: PubMed-verified discovery paper; establishes the steroid 5-alpha-reductase
      naming and in-vitro testosterone-to-DHT activity, which is a weak side activity
      rather than the physiological function. Supports the steroid annotations flagged
      as over-annotated.
- id: PMID:20637498
  title: SRD5A3 is required for converting polyprenol to dolichol and is mutated in
    a congenital glycosylation disorder.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Landmark paper identifying SRD5A3 as the polyprenol reductase required
      for dolichol synthesis and N-glycosylation; establishes ER localization and SRD5A3-CDG.
- id: PMID:38821050
  title: A pseudoautosomal glycosylation disorder prompts the revision of dolichol
    biosynthesis.
  findings: []
  reference_review:
    relevance: HIGH
    correctness: VERIFIED
    review_notes: Revises the pathway; shows SRD5A3 catalyzes the second (polyprenal-to-dolichal)
      NADPH-dependent reduction step, supporting the GO:0160198 polyprenal reductase
      MF term.
- id: Reactome:R-HSA-193048
  title: Androgen biosynthesis
  findings: []
- id: Reactome:R-HSA-446199
  title: Synthesis of dolichyl-phosphate
  findings: []
- id: Reactome:R-HSA-4755572
  title: Defective SRD5A3 does not reduce pPNOL to DCHOL
  findings: []
- id: Reactome:R-HSA-9705714
  title: SRD5A3 dehydrogenates TEST to DHTEST
  findings: []
- id: Reactome:R-HSA-9937295
  title: SRD5A3 reduces polyprenal to dolichal
  findings: []
- id: file:human/SRD5A3/SRD5A3-uniprot.txt
  title: UniProtKB Q9H8P0 (SR5A3_HUMAN) record
  findings: []