CYP2A13

Protein-coding gene in the species Homo sapiens
CYP2A13
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2P85, 2PG5, 2PG6, 2PG7, 3T3S, 4EJG, 4EJH, 4EJI

Identifiers
AliasesCYP2A13, CPAD, CYP2A, CYPIIA13, cytochrome P450 family 2 subfamily A member 13
External IDsOMIM: 608055 MGI: 88597 HomoloGene: 85917 GeneCards: CYP2A13
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for CYP2A13
Genomic location for CYP2A13
Band19q13.2Start41,088,451 bp[1]
End41,096,195 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for CYP2A13
Genomic location for CYP2A13
Band7 A3|7 15.54 cMStart26,534,730 bp[2]
End26,542,973 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • Brodmann area 10

  • quadriceps femoris muscle

  • middle frontal gyrus

  • frontal pole

  • bronchial epithelial cell

  • liver

  • placenta

  • cervix

  • right lobe of liver

  • blood
Top expressed in
  • proximal tubule

  • kidney

  • hepatobiliary system

  • liver

  • esophagus

  • respiratory epithelium

  • thymus

  • olfactory epithelium

  • lung

  • ovary
More reference expression data
BioGPS




More reference expression data
Gene ontology
Molecular function
  • iron ion binding
  • oxidoreductase activity
  • aromatase activity
  • 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
  • heme binding
  • oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
  • metal ion binding
  • coumarin 7-hydroxylase activity
  • steroid hydroxylase activity
  • monooxygenase activity
Cellular component
  • organelle membrane
  • endoplasmic reticulum membrane
  • endoplasmic reticulum
  • membrane
  • intracellular membrane-bounded organelle
  • cytoplasm
Biological process
  • xenobiotic metabolic process
  • epoxygenase P450 pathway
  • coumarin metabolic process
  • organic acid metabolic process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

1553

13087

Ensembl

ENSG00000197838

ENSMUSG00000005547

UniProt

Q16696

P20852

RefSeq (mRNA)

NM_000766

NM_007812

RefSeq (protein)

NP_000757

n/a

Location (UCSC)Chr 19: 41.09 – 41.1 MbChr 7: 26.53 – 26.54 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Cytochrome P450 2A13 is a protein that in humans is encoded by the CYP2A13 gene.[5][6][7]

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. Although its endogenous substrate has not been determined, it is known to metabolize 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a major nitrosamine specific to tobacco. This gene is part of a large cluster of cytochrome P450 genes from the CYP2A, CYP2B and CYP2F subfamilies on chromosome 19q.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000197838 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000005547 – 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. ^ Fernandez-Salguero P, Hoffman SM, Cholerton S, Mohrenweiser H, Raunio H, Rautio A, Pelkonen O, Huang JD, Evans WE, Idle JR, et al. (Oct 1995). "A genetic polymorphism in coumarin 7-hydroxylation: sequence of the human CYP2A genes and identification of variant CYP2A6 alleles". Am J Hum Genet. 57 (3): 651–60. PMC 1801261. PMID 7668294.
  6. ^ Nelson DR, Zeldin DC, Hoffman SM, Maltais LJ, Wain HM, Nebert DW (May 2004). "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): 1–18. doi:10.1097/00008571-200401000-00001. PMID 15128046.
  7. ^ a b "Entrez Gene: CYP2A13 cytochrome P450, family 2, subfamily A, polypeptide 13".

External links

Further reading

  • Fernandez-Salguero P, Gonzalez FJ (1995). "The CYP2A gene subfamily: species differences, regulation, catalytic activities and role in chemical carcinogenesis". Pharmacogenetics. 5 (Special Issue): S123–8. doi:10.1097/00008571-199512001-00013. PMID 7581481.
  • Smith G, Stubbins MJ, Harries LW, Wolf CR (1999). "Molecular genetics of the human cytochrome P450 monooxygenase superfamily". Xenobiotica. 28 (12): 1129–65. doi:10.1080/004982598238868. PMID 9890157.
  • 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.
  • Koskela S, Hakkola J, Hukkanen J, et al. (1999). "Expression of CYP2A genes in human liver and extrahepatic tissues". Biochem. Pharmacol. 57 (12): 1407–13. doi:10.1016/S0006-2952(99)00015-5. PMID 10353262.
  • Su T, Bao Z, Zhang QY, et al. (2000). "Human cytochrome P450 CYP2A13: predominant expression in the respiratory tract and its high efficiency metabolic activation of a tobacco-specific carcinogen, 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone". Cancer Res. 60 (18): 5074–9. PMID 11016631.
  • Zhang X, Su T, Zhang QY, et al. (2002). "Genetic polymorphisms of the human CYP2A13 gene: identification of single-nucleotide polymorphisms and functional characterization of an Arg257Cys variant". J. Pharmacol. Exp. Ther. 302 (2): 416–23. doi:10.1124/jpet.302.2.416. PMID 12130698.
  • Saito S, Iida A, Sekine A, et al. (2003). "Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population". J. Hum. Genet. 48 (5): 249–70. doi:10.1007/s10038-003-0021-7. PMID 12721789.
  • Wang H, Tan W, Hao B, et al. (2004). "Substantial reduction in risk of lung adenocarcinoma associated with genetic polymorphism in CYP2A13, the most active cytochrome P450 for the metabolic activation of tobacco-specific carcinogen NNK". Cancer Res. 63 (22): 8057–61. PMID 14633739.
  • Cauffiez C, Lo-Guidice JM, Quaranta S, et al. (2004). "Genetic polymorphism of the human cytochrome CYP2A13 in a French population: implication in lung cancer susceptibility". Biochem. Biophys. Res. Commun. 317 (2): 662–9. doi:10.1016/j.bbrc.2004.03.092. PMID 15063809.
  • Cheng XY, Chen GL, Zhang WX, et al. (2004). "Arg257Cys polymorphism of CYP2A13 in a Chinese population". Clin. Chim. Acta. 343 (1–2): 213–6. doi:10.1016/j.cccn.2004.01.017. PMID 15115698.
  • He XY, Shen J, Ding X, et al. (2005). "Identification of critical amino acid residues of human CYP2A13 for the metabolic activation of 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone, a tobacco-specific carcinogen". Drug Metab. Dispos. 32 (12): 1516–21. doi:10.1124/dmd.104.001370. PMID 15333516. S2CID 26225467.
  • Fujieda M, Yamazaki H, Kiyotani K, et al. (2005). "Eighteen novel polymorphisms of the CYP2A13 gene in Japanese". Drug Metab. Pharmacokinet. 18 (1): 86–90. doi:10.2133/dmpk.18.86. PMID 15618722.
  • Smith BD, Sanders JL, Porubsky PR, et al. (2007). "Structure of the human lung cytochrome P450 2A13". J. Biol. Chem. 282 (23): 17306–13. doi:10.1074/jbc.M702361200. PMID 17428784.
  • v
  • t
  • e
  • 1z10: Crystal Structure of Human Microsomal P450 2A6 with Coumarin Bound
    1z10: Crystal Structure of Human Microsomal P450 2A6 with Coumarin Bound
  • 1z11: Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound
    1z11: Crystal Structure of Human Microsomal P450 2A6 with Methoxsalen Bound
  • 2fdu: Microsomal P450 2A6 with the inhibitor N,N-Dimethyl(5-(pyridin-3-yl)furan-2-yl)methanamine bound
    2fdu: Microsomal P450 2A6 with the inhibitor N,N-Dimethyl(5-(pyridin-3-yl)furan-2-yl)methanamine bound
  • 2fdv: Microsomal P450 2A6 with the inhibitor N-Methyl(5-(pyridin-3-yl)furan-2-yl)methanamine bound
    2fdv: Microsomal P450 2A6 with the inhibitor N-Methyl(5-(pyridin-3-yl)furan-2-yl)methanamine bound
  • 2fdw: Crystal Structure Of Human Microsomal P450 2A6 with the inhibitor (5-(Pyridin-3-yl)furan-2-yl)methanamine bound
    2fdw: Crystal Structure Of Human Microsomal P450 2A6 with the inhibitor (5-(Pyridin-3-yl)furan-2-yl)methanamine bound
  • 2fdy: Microsomal P450 2A6 with the inhibitor Adrithiol bound
    2fdy: Microsomal P450 2A6 with the inhibitor Adrithiol bound
  • 2p85: Structure of Human Lung Cytochrome P450 2A13 with indole bound in two alternate conformations
    2p85: Structure of Human Lung Cytochrome P450 2A13 with indole bound in two alternate conformations
  • v
  • t
  • e
Cytochromes, oxygenases: cytochrome P450 (Most belong to EC 1.14)
CYP1
CYP2
CYP3 (CYP3A)
CYP4
CYP5-20
CYP21-49
CYP51-69
CYP71-99
CYP101-281
CYP301-499
CYP501-699
CYP701-999


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