CYP4Z1

Identifiers

CYP4Z1, CYP4A20, cytochrome P450 family 4 subfamily Z member 1

External IDs

Gene ontology
Molecular function	• iron ion binding • oxidoreductase activity • aromatase activity • heme binding • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen • metal ion binding • monooxygenase activity
Cellular component	• integral component of membrane • organelle membrane • endoplasmic reticulum membrane • endoplasmic reticulum • membrane • intracellular membrane-bounded organelle
Biological process	• oxidation-reduction process
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


199974


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Ensembl


ENSG00000186160


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UniProt


Q86W10


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RefSeq (mRNA)


NM_178134


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RefSeq (protein)


NP_835235


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Location (UCSC)

Chr 1: 47.07 – 47.12 Mb

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PubMed search

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CYP4Z1 (cytochrome P450, family 4, subfamily Z, polypeptide 1) is a protein that in humans is encoded by the CYP4Z1 gene.

This gene encodes a member of the 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 gene is part of a cluster of cytochrome P450 genes on chromosome 1p33.

CYP4Z1 is overexpressed in breast cancer cells. It has also been demonstrated that the expression of the CYP4Z1 gene is upregulated by activated glucocorticoid and progesterone receptors. The overexpression of CYP4Z1 is associated with the breast cancer cells' increased production of 20-Hydroxyeicosatetraenoic acid (20-HETE); it is hypothesized that CYP4Z1 metabolizes arachidonic acid to 20-HETE and that this overproduction is responsible for increasing the growth and spread of breast cancer cells in human breast cancer. CPZ4Z1 is likewise overexpressed in ovarian cancer cells. These studies also suggest that CYP4Z1 will be a valuable marker to distinguish between benign and malignant breast and ovarian growths in humans and/or the prognoses of malignant growths in these tissues.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

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