CYP2F1

CYP2F1
Identifiers
Aliases	CYP2F1 , C2F1, CYP2F, CYPIIF1, cytochrome P450 family 2 subfamily F member 1
External IDs	OMIM: 124070 MGI: 88608 HomoloGene: 73898 GeneCards: CYP2F1
Gene location (Human) Chr. Chromosome 19 (human) [1] Band 19q13.2 Start 41,114,432 bp [1] End 41,128,381 bp [1]
Gene location (Mouse) Chr. Chromosome 7 (mouse) [2] Band 7|7 A3 Start 26,819,334 bp [2] End 26,833,085 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in stromal cell of endometrium right lung testicle sural nerve minor salivary gland bone marrow thymus upper lobe of left lung vagina blood Top expressed in right lung right lung lobe olfactory epithelium left lobe of liver lacrimal gland conjunctival fornix parotid gland esophagus left lung superior surface of tongue More reference expression data BioGPS n/a
Gene ontology Molecular function iron ion binding oxygen binding arachidonic acid epoxygenase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen metal ion binding monooxygenase activity heme binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity aromatase activity steroid hydroxylase activity Cellular component organelle membrane endoplasmic reticulum membrane intracellular membrane-bounded organelle membrane endoplasmic reticulum cytoplasm Biological process epoxygenase P450 pathway trichloroethylene metabolic process xenobiotic metabolic process response to toxic substance organic acid metabolic process Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1572 13107 Ensembl ENSG00000197446 ENSMUSG00000052974 UniProt P24903 P33267 RefSeq (mRNA) NM_000774 NM_007817 RefSeq (protein) NP_000765 NP_031843 Location (UCSC) Chr 19: 41.11 – 41.13 Mb Chr 7: 26.82 – 26.83 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Cytochrome P450 2F1 is a protein that in humans is encoded by the CYP2F1 gene. ^[5]

This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This protein localizes to the endoplasmic reticulum and is known to dehydrogenate 3-methylindole, an endogenous toxin derived from the fermentation of tryptophan, as well as xenobiotic substrates, such as naphthalene and ethoxycoumarin. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000197446 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000052974 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: CYP2F1 cytochrome P450, family 2, subfamily F, polypeptide 1".

External links

• Human CYP2F1 genome location and CYP2F1 gene details page in the UCSC Genome Browser .

Further reading

• Nhamburo PT, Kimura S, McBride OW, et al. (1990). "The human CYP2F gene subfamily: identification of a cDNA encoding a new cytochrome P450, cDNA-directed expression, and chromosome mapping". Biochemistry. 29 (23): 5491–9. doi:10.1021/bi00475a012. PMID   1974816.
• Bale AE, Mitchell AL, Gonzalez FJ, McBride OW (1991). "Localization of CYP2F1 by multipoint linkage analysis and pulsed-field gel electrophoresis". Genomics. 10 (1): 284–6. doi:10.1016/0888-7543(91)90514-F. PMID   2045106.
• Trask B, Fertitta A, Christensen M, et al. (1993). "Fluorescence in situ hybridization mapping of human chromosome 19: cytogenetic band location of 540 cosmids and 70 genes or DNA markers". Genomics. 15 (1): 133–45. doi:10.1006/geno.1993.1021. PMID   8432525.
• Hoffman SM, Fernandez-Salguero P, Gonzalez FJ, Mohrenweiser HW (1996). "Organization and evolution of the cytochrome P450 CYP2A-2B-2F subfamily gene cluster on human chromosome 19". J. Mol. Evol. 41 (6): 894–900. doi:10.1007/bf00173169. PMID   8587134. S2CID   12153961.
• Hakkola J, Pasanen M, Hukkanen J, et al. (1996). "Expression of xenobiotic-metabolizing cytochrome P450 forms in human full-term placenta". Biochem. Pharmacol. 51 (4): 403–11. doi:10.1016/0006-2952(95)02184-1. PMID   8619884.
• Andersen MR, Farin FM, Omiecinski CJ (1998). "Quantification of multiple human cytochrome P450 mRNA molecules using competitive reverse transcriptase-PCR". DNA Cell Biol. 17 (3): 231–8. doi:10.1089/dna.1998.17.231. PMID   9539103.
• Lanza DL, Code E, Crespi CL, et al. (1999). "Specific dehydrogenation of 3-methylindole and epoxidation of naphthalene by recombinant human CYP2F1 expressed in lymphoblastoid cells". Drug Metab. Dispos. 27 (7): 798–803. PMID   10383923.
• Chen N, Whitehead SE, Caillat AW, et al. (2002). "Identification and cross-species comparisons of CYP2F subfamily genes in mammals". Mutat. Res. 499 (2): 155–61. doi:10.1016/S0027-5107(01)00274-3. PMID   11827709.
• Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC   139241 . PMID   12477932.
• Carr BA, Wan J, Hines RN, Yost GS (2003). "Characterization of the human lung CYP2F1 gene and identification of a novel lung-specific binding motif". J. Biol. Chem. 278 (18): 15473–83. doi: 10.1074/jbc.M300319200 . PMID   12598524.
• Tournel G, Cauffiez C, Billaut-Laden I, et al. (2007). "Molecular analysis of the CYP2F1 gene: identification of a frequent non-functional allelic variant". Mutat. Res. 617 (1–2): 79–89. doi:10.1016/j.mrfmmm.2007.01.007. PMID   17327131.