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Sdhd - succinate dehydrogenase complex subunit D (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-18
Description
Predicted to enable heme binding activity; succinate dehydrogenase (quinone) activity; and ubiquinone binding activity. Predicted to be involved in mitochondrial electron transport, succinate to ubiquinone and tricarboxylic acid cycle. Predicted to act upstream of or within cellular response to hypoxia and regulation of catecholamine secretion. Predicted to be located in mitochondrial inner membrane. Predicted to be part of respiratory chain complex II (succinate dehydrogenase). Predicted to be active in mitochondrion. Human ortholog(s) of this gene implicated in Carney-Stratakis syndrome; mitochondrial complex II deficiency; and paraganglioma. Orthologous to human SDHD (succinate dehydrogenase complex subunit D).

1 Names and Identifiers

1.1 Synonyms

  • CII-4
  • QPs3
  • cybS
  • succinate dehydrogenase [ubiquinone] cytochrome b small subunit, mitochondrial
  • malate dehydrogenase [quinone] cytochrome b small subunit
  • succinate dehydrogenase complex, subunit D, integral membrane protein
  • succinate-ubiquinone oxidoreductase cytochrome b small subunit
  • succinate-ubiquinone reductase membrane anchor subunit

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 RGD ID

1.2.5 Wikidata

3 Proteins

3.1 Protein Function

Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (By similarity). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate. Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate (By similarity).

3.2 Protein 3D Structures

3.2.1 AlphaFold Structures

Highly accurate protein structure prediction with AlphaFold. Nature. 2021 Aug;596(7873):583-589. DOI:10.1038/s41586-021-03819-2. PMID:34265844; PMCID:PMC8371605

3.3 Protein Targets

4 Interactions and Pathways

4.1 Interactions

4.2 Pathways

5 Biochemical Reactions

6 Expression

7 Literature

7.1 Gene-Chemical Co-Occurrences in Literature

7.2 Gene-Gene Co-Occurrences in Literature

7.3 Gene-Disease Co-Occurrences in Literature

8 Patents

8.1 Gene-Chemical Co-Occurrences in Patents

8.2 Gene-Gene Co-Occurrences in Patents

8.3 Gene-Disease Co-Occurrences in Patents

9 Information Sources

  1. NCBI Gene
    LICENSE
    NCBI Website and Data Usage Policies and Disclaimers
    https://www.ncbi.nlm.nih.gov/home/about/policies/
  2. PubChem
  3. Alliance of Genome Resources
    LICENSE
    All annotations and data produced by Alliance members that are accessible from alliancegenome.org are distributed under a CC BY 4.0 license (https://creativecommons.org/licenses/by/4.0/).
    https://www.alliancegenome.org/privacy-warranty-licensing
  4. NCBI Gene Expression Omnibus (GEO)
  5. Rat Genome Database (RGD)
    LICENSE
    Creative Commons Attribution 4.0 International license (CC BY 4.0)
    https://creativecommons.org/licenses/by/4.0/
  6. STRING: functional protein association networks
  7. Swiss Institute of Bioinformatics Bgee
    LICENSE
    Creative Commons Zero license (CC0)
    https://www.bgee.org/about/
  8. UniProt
    LICENSE
    We have chosen to apply the Creative Commons Attribution (CC BY 4.0, http://creativecommons.org/licenses/by/4.0/) License to all copyrightable parts of our databases.
    https://www.uniprot.org/help/license
  9. Wikidata
  10. AlphaFold DB
    LICENSE
    All of the data provided is freely available for both academic and commercial use under Creative Commons Attribution 4.0 (CC-BY 4.0) licence terms.
    https://alphafold.ebi.ac.uk/faq
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