CYP4F8

From Wikipedia, the free encyclopedia

Cytochrome P450, family 4, subfamily F, polypeptide 8

Identifiers

CYP4F8; CPF8; CYPIVF8

External IDs

Gene ontology
Molecular Function:	• iron ion binding • fatty acid (omega-1)-hydroxylase activity • heme binding • metal ion binding • unspecific monooxygenase activity
Cellular Component:	• endoplasmic reticulum • microsome • membrane • integral to membrane
Biological Process:	• electron transport • prostaglandin metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

n/a

Refseq

NM_007253 (mRNA)
NP_009184 (protein)

NM_134127 (mRNA)
NP_598888 (protein)

Location

Chr 19: 15.59 - 15.6 Mb

Chr 17: 32.42 - 32.44 Mb

Pubmed search

[1]

[2]

Cytochrome P450, family 4, subfamily F, polypeptide 8, also known as CYP4F8, is a human gene.^[1]

This gene, CYP4F8, 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 functions as a 19-hydroxylase of prostaglandins in seminal vesicles. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F3, is approximately 18 kb away.^[1]

[edit] References

^ ^a ^b Entrez Gene: CYP4F8 cytochrome P450, family 4, subfamily F, polypeptide 8.

[edit] Further reading

Simpson AE (1997). "The cytochrome P450 4 (CYP4) family.". Gen. Pharmacol. 28 (3): 351–9. PMID 9068972.
Bylund J, Finnström N, Oliw EH (1999). "Gene expression of a novel cytochrome P450 of the CYP4F subfamily in human seminal vesicles.". Biochem. Biophys. Res. Commun. 261 (1): 169–74. doi:10.1006/bbrc.1999.1011. PMID 10405341.
Bylund J, Hidestrand M, Ingelman-Sundberg M, Oliw EH (2000). "Identification of CYP4F8 in human seminal vesicles as a prominent 19-hydroxylase of prostaglandin endoperoxides.". J. Biol. Chem. 275 (29): 21844–9. doi:10.1074/jbc.M001712200. PMID 10791960.
Oliw EH, Stark K, Bylund J (2001). "Oxidation of prostaglandin H(2) and prostaglandin H(2) analogues by human cytochromes P450: analysis of omega-side chain hydroxy metabolites and four steroisomers of 5-hydroxyprostaglandin I(1) by mass spectrometry.". Biochem. Pharmacol. 62 (4): 407–15. PMID 11448449.
Stark K, Törmä H, Cristea M, Oliw EH (2003). "Expression of CYP4F8 (prostaglandin H 19-hydroxylase) in human epithelia and prominent induction in epidermis of psoriatic lesions.". Arch. Biochem. Biophys. 409 (1): 188–96. PMID 12464258.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Stark K, Bylund J, Törmä H, et al. (2005). "On the mechanism of biosynthesis of 19-hydroxyprostaglandins of human seminal fluid and expression of cyclooxygenase-2, PGH 19-hydroxylase (CYP4F8) and microsomal PGE synthase-1 in seminal vesicles and vas deferens.". Prostaglandins Other Lipid Mediat. 75 (1-4): 47–64. PMID 15789615.
Stark K, Wongsud B, Burman R, Oliw EH (2005). "Oxygenation of polyunsaturated long chain fatty acids by recombinant CYP4F8 and CYP4F12 and catalytic importance of Tyr-125 and Gly-328 of CYP4F8.". Arch. Biochem. Biophys. 441 (2): 174–81. doi:10.1016/j.abb.2005.07.003. PMID 16112640.
Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes.". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMID 16344560.
Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry.". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMID 17353931.