Hmdb loader
Identification
HMDB Protein ID HMDBP01555
Secondary Accession Numbers
  • 6851
  • HMDBP05593
Name Cytochrome P450 1A1
Synonyms
  1. CYPIA1
  2. Cytochrome P450 form 6
  3. Cytochrome P450-C
  4. Cytochrome P450-P1
Gene Name CYP1A1
Protein Type Unknown
Biological Properties
General Function Involved in monooxygenase activity
Specific Function Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Pathways
  • Chemical carcinogenesis - DNA adducts
  • Estrone Metabolism
  • Metabolism of xenobiotics by cytochrome P450
  • Retinol metabolism
  • Steroid hormone biosynthesis
  • Tryptophan metabolism
  • Tryptophan metabolism
Reactions
RH + reduced flavoprotein + Oxygen → ROH + oxidized flavoprotein + Water details
GO Classification
Biological Process
response to arsenic-containing substance
drug metabolic process
response to lipopolysaccharide
cell proliferation
vitamin D metabolic process
response to wounding
camera-type eye development
coumarin metabolic process
response to drug
dibenzo-p-dioxin catabolic process
digestive tract development
embryo development ending in birth or egg hatching
flavonoid metabolic process
hepatocyte differentiation
hydrogen peroxide biosynthetic process
insecticide metabolic process
maternal process involved in parturition
porphyrin-containing compound metabolic process
positive regulation of S phase of mitotic cell cycle
response to food
response to nematode
response to virus
xenobiotic metabolic process
amine metabolic process
response to antibiotic
9-cis-retinoic acid biosynthetic process
response to organic cyclic compound
cellular lipid metabolic process
response to iron(III) ion
response to hyperoxia
response to vitamin A
response to hypoxia
response to herbicide
Cellular Component
endoplasmic reticulum membrane
mitochondrion
Function
ion binding
cation binding
metal ion binding
binding
catalytic activity
transition metal ion binding
electron carrier activity
iron ion binding
monooxygenase activity
heme binding
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
oxidoreductase activity
Molecular Function
electron carrier activity
oxygen binding
aromatase activity
demethylase activity
flavonoid 3'-monooxygenase activity
oxidoreductase activity, acting on diphenols and related substances as donors
vitamin D 24-hydroxylase activity
iron ion binding
steroid hydroxylase activity
heme binding
Process
metabolic process
oxidation reduction
Cellular Location
  1. Peripheral membrane protein
  2. Peripheral membrane protein
  3. Endoplasmic reticulum membrane
  4. Microsome membrane
Gene Properties
Chromosome Location 15
Locus 15q24.1
SNPs CYP1A1
Gene Sequence
>1539 bp
ATGCTTTTCCCAATCTCCATGTCGGCCACGGAGTTTCTTCTGGCCTCTGTCATCTTCTGT
CTGGTATTCTGGGTAATGAGGGCCTCAAGACCTCAGGTCCCCAAAGGCCTGAAGAATCCA
CCAGGGCCATGGGGCTGGCCTCTGATTGGGCACATGCTGACCCTGGGAAAGAACCCGCAC
CTGGCACTGTCAAGGATGAGCCAGCAGTATGGGGACGTGCTGCAGATCCGAATTGGCTCC
ACACCCGTGGTGGTGCTGAGCGGCCTGGACACCATCCGGCAGGCCCTGGTGCGGCAGGGC
GATGATTTCAAGGGCCGGCCCGACCTCTACACCTTCACCCTCATCAGTAATGGTCAGAGC
ATGTCCTTCAGCCCAGACTCTGGACCAGTGTGGGCTGCCCGCCGGCGCCTGGCCCAGAAT
GGCCTGAAAAGTTTCTCCATTGCCTCTGACCCAGCCTCCTCAACCTCCTGCTACCTGGAA
GAGCATGTGAGCAAGGAGGCTGAGGTCCTGATAAGCACGTTGCAGGAGCTGATGGCAGGG
CCTGGGCACTTTAACCCCTACAGGTATGTGGTGGTATCAGTGACCAATGTCATCTGTGCC
ATTTGCTTTGGCCGGCGCTATGACCACAACCACCAAGAACTGCTTAGCCTAGTCAACCTG
AATAATAATTTCGGGGAGGTGGTTGGCTCTGGAAACCCAGCTGAGTTCATCCCTATTCTT
CGCTACCTACCCAACCCTTCCCTGAATGCCTTCAAGGACCTGAATGAGAAGTTCTACAGC
TTCATGCAGAAGATGGTCAAGGAGCACTACAAAACCTTTGAGAAGGGCCACATCCGGGAC
ATCACAGACAGCCTGATTGAGCACTGTCAGGAGAAGCAGCTGGATGAGAACGCCAATGTC
CAGCTGTCAGATGAGAAGATCATTAACATCGTCTTGGACCTCTTTGGAGCTGGGTTTGAC
ACAGTCACAACTGCTATCTCCTGGAGCCTCATGTATTTGGTGATGAACCCCAGGGTACAG
AGAAAGATCCAAGAGGAGCTAGACACAGTGATTGGCAGGTCACGGCGGCCCCGGCTCTCT
GACAGATCCCATCTGCCCTATATGGAGGCCTTCATCCTGGAGACCTTCCGACACTCTTCC
TTCGTCCCCTTCACCATCCCCCACAGCACAACAAGAGACACAAGTTTGAAAGGCTTTTAC
ATCCCCAAGGGGCGTTGTGTCTTTGTAAACCAGTGGCAGATCAACCATGACCAGAAGCTA
TGGGTCAACCCATCTGAGTTCCTACCTGAACGGTTTCTCACCCCTGATGGTGCTATCGAC
AAGGTGTTAAGTGAGAAGGTGATTATCTTTGGCATGGGCAAGCGGAAGTGTATCGGTGAG
ACCGTTGCCCGCTGGGAGGTCTTTCTCTTCCTGGCTATCCTGCTGCAACGGGTGGAATTC
AGCGTGCCACTGGGCGTGAAGGTGGACATGACCCCCATCTATGGGCTAACCATGAAGCAT
GCCTGCTGTGAGCACTTCCAAATGCAGCTGCGCTCTTAG
Protein Properties
Number of Residues 512
Molecular Weight 58164.815
Theoretical pI 8.347
Pfam Domain Function
Signals Not Available
Transmembrane Regions Not Available
Protein Sequence
>Cytochrome P450 1A1
MLFPISMSATEFLLASVIFCLVFWVIRASRPQVPKGLKNPPGPWGWPLIGHMLTLGKNPH
LALSRMSQQYGDVLQIRIGSTPVVVLSGLDTIRQALVRQGDDFKGRPDLYTFTLISNGQS
MSFSPDSGPVWAARRRLAQNGLKSFSIASDPASSTSCYLEEHVSKEAEVLISTLQELMAG
PGHFNPYRYVVVSVTNVICAICFGRRYDHNHQELLSLVNLNNNFGEVVGSGNPADFIPIL
RYLPNPSLNAFKDLNEKFYSFMQKMVKEHYKTFEKGHIRDITDSLIEHCQEKQLDENANV
QLSDEKIINIVLDLFGAGFDTVTTAISWSLMYLVMNPRVQRKIQEELDTVIGRSRRPRLS
DRSHLPYMEAFILETFRHSSFVPFTIPHSTTRDTSLKGFYIPKGRCVFVNQWQINHDQKL
WVNPSEFLPERFLTPDGAIDKVLSEKVIIFGMGKRKCIGETIARWEVFLFLAILLQRVEF
SVPLGVKVDMTPIYGLTMKHACCEHFQMQLRS
GenBank ID Protein 181276
UniProtKB/Swiss-Prot ID P04798
UniProtKB/Swiss-Prot Entry Name CP1A1_HUMAN
PDB IDs Not Available
GenBank Gene ID K03191
GeneCard ID CYP1A1
GenAtlas ID CYP1A1
HGNC ID HGNC:2595
References
General References
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  5. Jaiswal AK, Gonzalez FJ, Nebert DW: Human P1-450 gene sequence and correlation of mRNA with genetic differences in benzo[a]pyrene metabolism. Nucleic Acids Res. 1985 Jun 25;13(12):4503-20. [PubMed:2989797 ]
  6. Jaiswal AK, Gonzalez FJ, Nebert DW: Human dioxin-inducible cytochrome P1-450: complementary DNA and amino acid sequence. Science. 1985 Apr 5;228(4695):80-3. [PubMed:3838385 ]
  7. Kawajiri K, Watanabe J, Gotoh O, Tagashira Y, Sogawa K, Fujii-Kuriyama Y: Structure and drug inducibility of the human cytochrome P-450c gene. Eur J Biochem. 1986 Sep 1;159(2):219-25. [PubMed:3019683 ]
  8. Corchero J, Pimprale S, Kimura S, Gonzalez FJ: Organization of the CYP1A cluster on human chromosome 15: implications for gene regulation. Pharmacogenetics. 2001 Feb;11(1):1-6. [PubMed:11207026 ]
  9. Yun CH, Park HJ, Kim SJ, Kim HK: Identification of cytochrome P450 1A1 in human brain. Biochem Biophys Res Commun. 1998 Feb 24;243(3):808-10. [PubMed:9500998 ]
  10. Quattrochi LC, Okino ST, Pendurthi UR, Tukey RH: Cloning and isolation of human cytochrome P-450 cDNAs homologous to dioxin-inducible rabbit mRNAs encoding P-450 4 and P-450 6. DNA. 1985 Oct;4(5):395-400. [PubMed:3000715 ]
  11. Hayashi S, Watanabe J, Nakachi K, Kawajiri K: Genetic linkage of lung cancer-associated MspI polymorphisms with amino acid replacement in the heme binding region of the human cytochrome P450IA1 gene. J Biochem. 1991 Sep;110(3):407-11. [PubMed:1722803 ]
  12. Cascorbi I, Brockmoller J, Roots I: A C4887A polymorphism in exon 7 of human CYP1A1: population frequency, mutation linkages, and impact on lung cancer susceptibility. Cancer Res. 1996 Nov 1;56(21):4965-9. [PubMed:8895751 ]
  13. Smart J, Daly AK: Variation in induced CYP1A1 levels: relationship to CYP1A1, Ah receptor and GSTM1 polymorphisms. Pharmacogenetics. 2000 Feb;10(1):11-24. [PubMed:10739168 ]
  14. Chevalier D, Allorge D, Lo-Guidice JM, Cauffiez C, Lhermitte M, Lafitte JJ, Broly F: Detection of known and two novel (M331I and R464S) missense mutations in the human CYP1A1 gene in a French Caucasian population. Hum Mutat. 2001 Apr;17(4):355. [PubMed:11295847 ]
  15. Saito T, Egashira M, Kiyotani K, Fujieda M, Yamazaki H, Kiyohara C, Kunitoh H, Kamataki T: Novel nonsynonymous polymorphisms of the CYP1A1 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(3):218-21. [PubMed:15618738 ]
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