Entry - *615341 - CYTOCHROME P450, FAMILY 4, SUBFAMILY A, POLYPEPTIDE 22; CYP4A22 - OMIM

 
 
* 615341

CYTOCHROME P450, FAMILY 4, SUBFAMILY A, POLYPEPTIDE 22; CYP4A22


HGNC Approved Gene Symbol: CYP4A22

Cytogenetic location: 1p33     Genomic coordinates (GRCh38): 1:47,137,441-47,149,727 (from NCBI)


TEXT

▼ Description

CYP4A22 belongs to a large family of cytochrome P450 genes that encode heme-binding monooxygenases. Members of this enzyme family are involved in the metabolism of drugs and in the synthesis and/or metabolism of steroids, cholesterol, vitamin D3, and eicosanoids (summary by Pikuleva and Waterman, 2013).


▼ Cloning and Expression

Kawashima et al. (2000) isolated a CYP4A22 clone, which they designated CYP4A11. The deduced protein contains 519 amino acids.

Using PCR analysis, Savas et al. (2003) found that both CYP4A11 (601310) and CYP4A22 were expressed in 100 human liver samples. Quantitative real-time PCR of 7 samples revealed that the enzymes were independently and variably expressed and that expression of CYP4A11 was significantly higher than that of CYP4A22.


▼ Gene Function

Pikuleva and Waterman (2013) stated that CYP4A11 (601310) and CYP4A22 oxidize arachidonic acid to 20-hydroxyeicosatetraenoic acid in the endoplasmic reticulum of kidney tubules.

Kawashima et al. (2000) assayed the activity of human CYP4A22, which they called CYP4A11, in the presence of NADPH-cytochrome P450 reductase (POR; 124015), cytochrome B5 (CYB5A; 613218), and NADPH. CYP4A22 showed omega-hydroxylation activity against laurate and palmitate, but not against arachidonate or prostaglandin A1.


▼ Gene Structure

Kawashima et al. (2000) determined that the CYP4A22 gene contains 12 exons and spans 12.6 kb.


▼ Mapping

By genomic sequence analysis, Nelson et al. (2004) mapped the CYP4A22 gene to a cluster of cytochrome P450 genes on chromosome 1p33.


▼ REFERENCES

  1. Kawashima, H., Naganuma, T., Kusunose, E., Kono, T., Yasumoto, R., Sugimura, K., Kishimoto, T. Human fatty acid omega-hydroxylase, CYP4A11: determination of complete genomic sequence and characterization of purified recombinant protein. Arch. Biochem. Biophys. 378: 333-339, 2000. [PubMed: 10860550, related citations] [Full Text]

  2. Nelson, D. R., Zeldin, D. C., Hoffman, S. M. G., Maltais, L. J., Wain, H. M., Nebert, D. W. Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14: 1-18, 2004. [PubMed: 15128046, related citations] [Full Text]

  3. Pikuleva, I. A., Waterman, M. R. Cytochromes P450: roles in diseases. J. Biol. Chem. 288: 17091-17098, 2013. [PubMed: 23632021, related citations] [Full Text]

  4. Savas, U., Hsu, M.-H., Johnson, E. F. Differential regulation of human CYP4A genes by peroxisome proliferators and dexamethasone. Arch. Biochem. Biophys. 409: 212-220, 2003. [PubMed: 12464261, related citations] [Full Text]


Contributors:
Patricia A. Hartz - updated : 8/13/2013
Creation Date:
Patricia A. Hartz : 7/26/2013
Edit History:
alopez : 02/23/2021
joanna : 11/23/2016
tpirozzi : 08/14/2013
tpirozzi : 8/14/2013
tpirozzi : 8/13/2013
tpirozzi : 7/26/2013
tpirozzi : 7/26/2013
tpirozzi : 7/26/2013

* 615341

CYTOCHROME P450, FAMILY 4, SUBFAMILY A, POLYPEPTIDE 22; CYP4A22


HGNC Approved Gene Symbol: CYP4A22

Cytogenetic location: 1p33     Genomic coordinates (GRCh38): 1:47,137,441-47,149,727 (from NCBI)


TEXT

Description

CYP4A22 belongs to a large family of cytochrome P450 genes that encode heme-binding monooxygenases. Members of this enzyme family are involved in the metabolism of drugs and in the synthesis and/or metabolism of steroids, cholesterol, vitamin D3, and eicosanoids (summary by Pikuleva and Waterman, 2013).


Cloning and Expression

Kawashima et al. (2000) isolated a CYP4A22 clone, which they designated CYP4A11. The deduced protein contains 519 amino acids.

Using PCR analysis, Savas et al. (2003) found that both CYP4A11 (601310) and CYP4A22 were expressed in 100 human liver samples. Quantitative real-time PCR of 7 samples revealed that the enzymes were independently and variably expressed and that expression of CYP4A11 was significantly higher than that of CYP4A22.


Gene Function

Pikuleva and Waterman (2013) stated that CYP4A11 (601310) and CYP4A22 oxidize arachidonic acid to 20-hydroxyeicosatetraenoic acid in the endoplasmic reticulum of kidney tubules.

Kawashima et al. (2000) assayed the activity of human CYP4A22, which they called CYP4A11, in the presence of NADPH-cytochrome P450 reductase (POR; 124015), cytochrome B5 (CYB5A; 613218), and NADPH. CYP4A22 showed omega-hydroxylation activity against laurate and palmitate, but not against arachidonate or prostaglandin A1.


Gene Structure

Kawashima et al. (2000) determined that the CYP4A22 gene contains 12 exons and spans 12.6 kb.


Mapping

By genomic sequence analysis, Nelson et al. (2004) mapped the CYP4A22 gene to a cluster of cytochrome P450 genes on chromosome 1p33.


REFERENCES

  1. Kawashima, H., Naganuma, T., Kusunose, E., Kono, T., Yasumoto, R., Sugimura, K., Kishimoto, T. Human fatty acid omega-hydroxylase, CYP4A11: determination of complete genomic sequence and characterization of purified recombinant protein. Arch. Biochem. Biophys. 378: 333-339, 2000. [PubMed: 10860550] [Full Text: https://doi.org/10.1006/abbi.2000.1831]

  2. Nelson, D. R., Zeldin, D. C., Hoffman, S. M. G., Maltais, L. J., Wain, H. M., Nebert, D. W. Comparison of cytochrome P450 (CYP) genes from the mouse and human genomes, including nomenclature recommendations for genes, pseudogenes and alternative-splice variants. Pharmacogenetics 14: 1-18, 2004. [PubMed: 15128046] [Full Text: https://doi.org/10.1097/00008571-200401000-00001]

  3. Pikuleva, I. A., Waterman, M. R. Cytochromes P450: roles in diseases. J. Biol. Chem. 288: 17091-17098, 2013. [PubMed: 23632021] [Full Text: https://doi.org/10.1074/jbc.R112.431916]

  4. Savas, U., Hsu, M.-H., Johnson, E. F. Differential regulation of human CYP4A genes by peroxisome proliferators and dexamethasone. Arch. Biochem. Biophys. 409: 212-220, 2003. [PubMed: 12464261] [Full Text: https://doi.org/10.1016/s0003-9861(02)00499-x]


Contributors:
Patricia A. Hartz - updated : 8/13/2013

Creation Date:
Patricia A. Hartz : 7/26/2013

Edit History:
alopez : 02/23/2021
joanna : 11/23/2016
tpirozzi : 08/14/2013
tpirozzi : 8/14/2013
tpirozzi : 8/13/2013
tpirozzi : 7/26/2013
tpirozzi : 7/26/2013
tpirozzi : 7/26/2013



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OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.

NOTE: OMIM is intended for use primarily by physicians and other professionals concerned with genetic disorders, by genetics researchers, and by advanced students in science and medicine. While the OMIM database is open to the public, users seeking information about a personal medical or genetic condition are urged to consult with a qualified physician for diagnosis and for answers to personal questions.
OMIM® and Online Mendelian Inheritance in Man® are registered trademarks of the Johns Hopkins University.
Copyright® 1966-2024 Johns Hopkins University.
Printed: June 3, 2024