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Cyp4v3 - cytochrome P450, family 4, subfamily v, polypeptide 3 (Norway rat)

Gene
Symbol
Dates
  • Create:
    2016-09-14
  • Modify:
    2025-01-25
Description
Predicted to enable heme binding activity; iron ion binding activity; and long-chain fatty acid omega-hydroxylase activity. Predicted to be involved in fatty acid omega-oxidation. Predicted to be located in endoplasmic reticulum membrane. Human ortholog(s) of this gene implicated in Bietti crystalline corneoretinal dystrophy. Orthologous to human CYP4V2 (cytochrome P450 family 4 subfamily V member 2).

1 Names and Identifiers

1.1 Synonyms

  • Cyp4v2
  • cytochrome P450 4V2
  • cytochrome P450 4V3
  • cytochrome P450-like protein
  • docosahexaenoic acid omega-hydroxylase CYP4V2
  • long-chain fatty acid omega-monooxygenase

1.2 Other Identifiers

1.2.1 Ensembl ID

1.2.2 Alliance Gene ID

1.2.3 Bgee Gene ID

1.2.4 Enzyme Commission (EC) Number

1.2.5 RGD ID

1.2.6 Wikidata

3 Proteins

3.1 Protein Function

A cytochrome P450 monooxygenase involved in fatty acid metabolism in the eye. Catalyzes the omega-hydroxylation of polyunsaturated fatty acids (PUFAs) docosahexaenoate (DHA) and its precursor eicosapentaenoate (EPA), and may contribute to the homeostasis of these retinal PUFAs. Omega hydroxylates saturated fatty acids such as laurate, myristate and palmitate, the catalytic efficiency decreasing in the following order: myristate > laurate > palmitate (C14>C12>C16). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).

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

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
  11. Rhea - annotated reactions database
    LICENSE
    Rhea has chosen to apply the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/). This means that you are free to copy, distribute, display and make commercial use of the database in all legislations, provided you credit (cite) Rhea.
    https://www.rhea-db.org/help/license-disclaimer
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